A series of phenolic acids and phenol natural products, such as p-hydroxybenzoic acid, p-coumaric acid, caffeic acid, ferulic acid, gallic acid, << syringic acid >>, quercetin, and ellagic acid, were investigated for their inhibitory effects against the metalloenzyme carbonic anhydrase (CA, [[ EC 4.2.1.1 ]]).


A series of phenolic acids and phenol natural products, such as p-hydroxybenzoic acid, p-coumaric acid, caffeic acid, ferulic acid, gallic acid, syringic acid, << quercetin >>, and ellagic acid, were investigated for their inhibitory effects against the [[ metalloenzyme ]] carbonic anhydrase (CA, EC 4.2.1.1).


A series of phenolic acids and phenol natural products, such as p-hydroxybenzoic acid, p-coumaric acid, caffeic acid, ferulic acid, gallic acid, syringic acid, << quercetin >>, and ellagic acid, were investigated for their inhibitory effects against the metalloenzyme [[ carbonic anhydrase ]] (CA, EC 4.2.1.1).


A series of phenolic acids and phenol natural products, such as p-hydroxybenzoic acid, p-coumaric acid, caffeic acid, ferulic acid, gallic acid, syringic acid, << quercetin >>, and ellagic acid, were investigated for their inhibitory effects against the metalloenzyme carbonic anhydrase ([[ CA ]], EC 4.2.1.1).


A series of phenolic acids and phenol natural products, such as p-hydroxybenzoic acid, p-coumaric acid, caffeic acid, ferulic acid, gallic acid, syringic acid, << quercetin >>, and ellagic acid, were investigated for their inhibitory effects against the metalloenzyme carbonic anhydrase (CA, [[ EC 4.2.1.1 ]]).


A series of phenolic acids and phenol natural products, such as p-hydroxybenzoic acid, p-coumaric acid, caffeic acid, ferulic acid, gallic acid, syringic acid, quercetin, and << ellagic acid >>, were investigated for their inhibitory effects against the [[ metalloenzyme ]] carbonic anhydrase (CA, EC 4.2.1.1).


A series of phenolic acids and phenol natural products, such as p-hydroxybenzoic acid, p-coumaric acid, caffeic acid, ferulic acid, gallic acid, syringic acid, quercetin, and << ellagic acid >>, were investigated for their inhibitory effects against the metalloenzyme [[ carbonic anhydrase ]] (CA, EC 4.2.1.1).


A series of phenolic acids and phenol natural products, such as p-hydroxybenzoic acid, p-coumaric acid, caffeic acid, ferulic acid, gallic acid, syringic acid, quercetin, and << ellagic acid >>, were investigated for their inhibitory effects against the metalloenzyme carbonic anhydrase ([[ CA ]], EC 4.2.1.1).


A series of phenolic acids and phenol natural products, such as p-hydroxybenzoic acid, p-coumaric acid, caffeic acid, ferulic acid, gallic acid, syringic acid, quercetin, and << ellagic acid >>, were investigated for their inhibitory effects against the metalloenzyme carbonic anhydrase (CA, [[ EC 4.2.1.1 ]]).


A series of phenolic acids and << phenol >> natural products, such as p-hydroxybenzoic acid, p-coumaric acid, caffeic acid, ferulic acid, gallic acid, syringic acid, quercetin, and ellagic acid, were investigated for their inhibitory effects against the [[ metalloenzyme ]] carbonic anhydrase (CA, EC 4.2.1.1).


A series of phenolic acids and << phenol >> natural products, such as p-hydroxybenzoic acid, p-coumaric acid, caffeic acid, ferulic acid, gallic acid, syringic acid, quercetin, and ellagic acid, were investigated for their inhibitory effects against the metalloenzyme [[ carbonic anhydrase ]] (CA, EC 4.2.1.1).


A series of phenolic acids and << phenol >> natural products, such as p-hydroxybenzoic acid, p-coumaric acid, caffeic acid, ferulic acid, gallic acid, syringic acid, quercetin, and ellagic acid, were investigated for their inhibitory effects against the metalloenzyme carbonic anhydrase ([[ CA ]], EC 4.2.1.1).


A series of phenolic acids and << phenol >> natural products, such as p-hydroxybenzoic acid, p-coumaric acid, caffeic acid, ferulic acid, gallic acid, syringic acid, quercetin, and ellagic acid, were investigated for their inhibitory effects against the metalloenzyme carbonic anhydrase (CA, [[ EC 4.2.1.1 ]]).


<< Phenols >> like the ones investigated here possess a [[ CA ]] inhibition mechanism distinct of that of the sulfonamides/sulfamates used clinically or the coumarins.


Phenols like the ones investigated here possess a << CA >> inhibition mechanism distinct of that of the [[ sulfonamides ]]/sulfamates used clinically or the coumarins.


Phenols like the ones investigated here possess a << CA >> inhibition mechanism distinct of that of the sulfonamides/[[ sulfamates ]] used clinically or the coumarins.


Phenols like the ones investigated here possess a << CA >> inhibition mechanism distinct of that of the sulfonamides/sulfamates used clinically or the [[ coumarins ]].


<< L-serine dehydratase >> (SDH), a member of the beta-family of pyridoxal phosphate-dependent (PLP) enzymes, catalyzes the deamination of L-serine and L-threonine to yield [[ pyruvate ]] or 2-oxobutyrate.


L-serine dehydratase (<< SDH >>), a member of the beta-family of pyridoxal phosphate-dependent (PLP) enzymes, catalyzes the deamination of L-serine and L-threonine to yield [[ pyruvate ]] or 2-oxobutyrate.


<< L-serine dehydratase >> (SDH), a member of the beta-family of pyridoxal phosphate-dependent (PLP) enzymes, catalyzes the deamination of L-serine and L-threonine to yield pyruvate or [[ 2-oxobutyrate ]].


L-serine dehydratase (<< SDH >>), a member of the beta-family of pyridoxal phosphate-dependent (PLP) enzymes, catalyzes the deamination of L-serine and L-threonine to yield pyruvate or [[ 2-oxobutyrate ]].


<< L-serine dehydratase >> (SDH), a member of the beta-family of pyridoxal phosphate-dependent (PLP) enzymes, catalyzes the deamination of [[ L-serine ]] and L-threonine to yield pyruvate or 2-oxobutyrate.


L-serine dehydratase (<< SDH >>), a member of the beta-family of pyridoxal phosphate-dependent (PLP) enzymes, catalyzes the deamination of [[ L-serine ]] and L-threonine to yield pyruvate or 2-oxobutyrate.


<< L-serine dehydratase >> (SDH), a member of the beta-family of pyridoxal phosphate-dependent (PLP) enzymes, catalyzes the deamination of L-serine and [[ L-threonine ]] to yield pyruvate or 2-oxobutyrate.


L-serine dehydratase (<< SDH >>), a member of the beta-family of pyridoxal phosphate-dependent (PLP) enzymes, catalyzes the deamination of L-serine and [[ L-threonine ]] to yield pyruvate or 2-oxobutyrate.


Synthesis and evaluation of << carbamoylmethylene >> linked prodrugs of BMS-582949, a clinical [[ p38α ]] inhibitor.


Synthesis and evaluation of carbamoylmethylene linked prodrugs of << BMS-582949 >>, a clinical [[ p38α ]] inhibitor.


A series of << carbamoylmethylene >> linked prodrugs of 1 (BMS-582949), a clinical [[ p38α ]] inhibitor, were synthesized and evaluated.


A series of carbamoylmethylene linked prodrugs of 1 (<< BMS-582949 >>), a clinical [[ p38α ]] inhibitor, were synthesized and evaluated.


RESULTS: << Ethanol >> given to rats in drinking water decreased the level of [[ p-CREB ]] protein in the nucleus accumbens (-75 %) at the time of exposure to ethanol.


The decrement of << p-CREB >> protein in the nucleus accumbens remained at 24 h (-35 %) and 72 h (-28 %) of [[ ethanol ]] withdrawal, which recovered toward control level after 7 d of ethanol withdrawal.


The decrement of << p-CREB >> protein in the nucleus accumbens remained at 24 h (-35 %) and 72 h (-28 %) of ethanol withdrawal, which recovered toward control level after 7 d of [[ ethanol ]] withdrawal.


However, when naloxone was administered concurrently with << ethanol >> treatment, it antagonized the down-regulation of [[ p-CREB ]] protein in the nucleus accumbens (142 %) of rats exposed to ethanol.


However, when naloxone was administered concurrently with ethanol treatment, it antagonized the down-regulation of << p-CREB >> protein in the nucleus accumbens (142 %) of rats exposed to [[ ethanol ]].


CONCLUSION: A long-term intake of ethanol solution down-regulates the phosphorylation of << CREB >> in the nucleus accumbens, and those changes can be reversed by [[ naloxone ]], which may be one kind of the molecular mechanisms associated with ethanol dependence.


CONCLUSION: A long-term intake of << ethanol >> solution down-regulates the phosphorylation of [[ CREB ]] in the nucleus accumbens, and those changes can be reversed by naloxone, which may be one kind of the molecular mechanisms associated with ethanol dependence.


Adenosine and N(6)-cyclopentyl-adenosine (<< CPA >>, [[ A1R ]] agonist) constricted MVs but not MAs.


<< Adenosine >> and N(6)-cyclopentyl-adenosine (CPA, [[ A1R ]] agonist) constricted MVs but not MAs.


Adenosine and << N(6)-cyclopentyl-adenosine >> (CPA, [[ A1R ]] agonist) constricted MVs but not MAs.


The << A2A adenosine receptor >> agonist CGS21680 ([[ C23H29N7O6.HCl.xH2O ]]) (0.001-0.1 μM) did not alter NE oxidation currents.


The << A2A adenosine receptor >> agonist [[ CGS21680 ]] (C23H29N7O6.HCl.xH2O) (0.001-0.1 μM) did not alter NE oxidation currents.


<< Pasireotide >> (Signifor(®)) is a new subcutaneous somatostatin analogue that acts via somatostatin receptors to inhibit the secretion of [[ corticotropin ]] from the pituitary adenoma in patients with Cushing's disease.


Pasireotide (<< Signifor >>(®)) is a new subcutaneous somatostatin analogue that acts via somatostatin receptors to inhibit the secretion of [[ corticotropin ]] from the pituitary adenoma in patients with Cushing's disease.


Also, << SB365 >> showed anti-angiogenic activity by decreasing the expression of [[ HIF-1α ]] and VEGF.


Also, << SB365 >> showed anti-angiogenic activity by decreasing the expression of HIF-1α and [[ VEGF ]].


When further examined for its anticancer mechanism, << SB365 >> effectively suppressed the [[ AKT ]]/mTOR pathway both in vitro and in vivo.


When further examined for its anticancer mechanism, << SB365 >> effectively suppressed the AKT/[[ mTOR ]] pathway both in vitro and in vivo.


Taken together, our study demonstrated that << SB365 >> inhibits the [[ AKT ]]/mTOR pathway, leading to the suppression of tumor growth and angiogenesis together with induction of apoptosis.


Taken together, our study demonstrated that << SB365 >> inhibits the AKT/[[ mTOR ]] pathway, leading to the suppression of tumor growth and angiogenesis together with induction of apoptosis.


Apolipoprotein E3 (apoE3) safeguards pig proximal tubular LLC-PK1 cells against reduction in << SGLT1 >> activity induced by [[ gentamicin C ]].


Megalin, a family of << endocytic receptors >> related to the low-density lipoprotein (LDL) receptor, is a major pathway for proximal tubular [[ aminoglycoside ]] accumulation.


Megalin, a family of endocytic receptors related to the << low-density lipoprotein (LDL) receptor >>, is a major pathway for proximal tubular [[ aminoglycoside ]] accumulation.


We previously reported that << aminoglycoside >> antibiotics reduce [[ SGLT1 ]]-dependent glucose transport in pig proximal tubular epithelial LLC-PK1 cells in parallel with the order of their nephrotoxicity.


In this study, using a model of << gentamicin C >> (GMC)-induced reduction in [[ SGLT1 ]] activity, we examined whether ligands for megalin protect LLC-PK1 cells from the GMC-induced reduction in SGLT1 activity.


In this study, using a model of gentamicin C (<< GMC >>)-induced reduction in [[ SGLT1 ]] activity, we examined whether ligands for megalin protect LLC-PK1 cells from the GMC-induced reduction in SGLT1 activity.


In this study, using a model of gentamicin C (GMC)-induced reduction in SGLT1 activity, we examined whether ligands for megalin protect LLC-PK1 cells from the << GMC >>-induced reduction in [[ SGLT1 ]] activity.


Then the cells were treated with various concentrations of apoE3, lactoferrin and bovine serum albumin with or without 100 microg/ml of GMC, and the << SGLT1 >>-dependent [[ methyl alpha-D-glucopyranoside ]] (AMG) uptake and levels of SGLT1 expression were determined.


Then the cells were treated with various concentrations of apoE3, lactoferrin and bovine serum albumin with or without 100 microg/ml of GMC, and the << SGLT1 >>-dependent methyl alpha-D-glucopyranoside ([[ AMG ]]) uptake and levels of SGLT1 expression were determined.


Actions of << nizatidine >>, a selective [[ histamine H2-receptor ]] antagonist, on gastric acid secretion in dogs, rats and frogs.


<< Nizatidine >> (LY139037), a selective [[ histamine H2-receptor ]] antagonist, is a potent inhibitor of gastric acid secretion.


Nizatidine (<< LY139037 >>), a selective [[ histamine H2-receptor ]] antagonist, is a potent inhibitor of gastric acid secretion.


3D-QSAR-assisted drug design: identification of a potent << quinazoline >>-based [[ Aurora kinase ]] inhibitor.


Three different 3D-QSAR models were built and validated by using a set of 66 << pyrazole >> (Model I) and furanopyrimidine (Model II) compounds with IC(50) values toward [[ Aurora kinase A ]] ranging from 33 nM to 10.5 μM.


Three different 3D-QSAR models were built and validated by using a set of 66 pyrazole (Model I) and << furanopyrimidine >> (Model II) compounds with IC(50) values toward [[ Aurora kinase A ]] ranging from 33 nM to 10.5 μM.


Based on these suggestions, the rational redesign of << furanopyrimidine >> 24 (clog P=7.41; [[ Aurora A ]] IC(50) =43 nM; HCT-116 IC(50) =400 nM) led to the identification of quinazoline 67 (clog P=5.28; Aurora A IC(50) =25 nM; HCT-116 IC(50) =23 nM).


Based on these suggestions, the rational redesign of furanopyrimidine 24 (clog P=7.41; Aurora A IC(50) =43 nM; HCT-116 IC(50) =400 nM) led to the identification of << quinazoline >> 67 (clog P=5.28; [[ Aurora A ]] IC(50) =25 nM; HCT-116 IC(50) =23 nM).


Chelation of calcium ions by BAPTA-AM or blockade of << ERK1/2 >> activation by [[ UO126 ]] also prevented the NMDA effects.


Thus prolonged activation of NMDA receptors in hippocampal neurons reduced << GABAR δ subunit >> expression through [[ Ca2+ ]] entry and at least in part by ERK1/2 activation.


<< Amitriptyline >> is a [[ TrkA ]] and TrkB receptor agonist that promotes TrkA/TrkB heterodimerization and has potent neurotrophic activity.


<< Amitriptyline >> is a TrkA and [[ TrkB ]] receptor agonist that promotes TrkA/TrkB heterodimerization and has potent neurotrophic activity.


<< Amitriptyline >>, but not any other tricyclic or selective serotonin reuptake inhibitor antidepressants, promotes [[ TrkA ]] autophosphorylation in primary neurons and induces neurite outgrowth in PC12 cells.


Thus, << amitriptyline >> acts as a TrkA and [[ TrkB ]] agonist and possesses marked neurotrophic activity.


Thus, << amitriptyline >> acts as a [[ TrkA ]] and TrkB agonist and possesses marked neurotrophic activity.


Truncated ErbB2 receptor (p95ErbB2) is regulated by heregulin through heterodimer formation with ErbB3 yet remains sensitive to the dual EGFR/<< ErbB2 >> kinase inhibitor [[ GW572016 ]].


<< GW572016 >>, a reversible small molecule inhibitor of [[ EGFR ]] and ErbB2 tyrosine kinases, inhibits baseline p95ErbB2 phosphorylation in BT474 cells and tumor xenografts.


<< GW572016 >>, a reversible small molecule inhibitor of EGFR and [[ ErbB2 ]] tyrosine kinases, inhibits baseline p95ErbB2 phosphorylation in BT474 cells and tumor xenografts.


<< GW572016 >>, a reversible small molecule inhibitor of EGFR and ErbB2 [[ tyrosine kinases ]], inhibits baseline p95ErbB2 phosphorylation in BT474 cells and tumor xenografts.


<< GW572016 >>, a reversible small molecule inhibitor of EGFR and ErbB2 tyrosine kinases, inhibits baseline [[ p95ErbB2 ]] phosphorylation in BT474 cells and tumor xenografts.


Inhibition of p95ErbB2, p185ErbB2, and EGFR phosphorylation by << GW572016 >> resulted in the inhibition of downstream phospho-[[ Erk1/2 ]], phospho-AKT, and cyclin D steady-state protein levels.


Inhibition of p95ErbB2, p185ErbB2, and EGFR phosphorylation by << GW572016 >> resulted in the inhibition of downstream phospho-Erk1/2, phospho-[[ AKT ]], and cyclin D steady-state protein levels.


Inhibition of p95ErbB2, p185ErbB2, and EGFR phosphorylation by << GW572016 >> resulted in the inhibition of downstream phospho-Erk1/2, phospho-AKT, and [[ cyclin D ]] steady-state protein levels.


Inhibition of << p95ErbB2 >>, p185ErbB2, and EGFR phosphorylation by [[ GW572016 ]] resulted in the inhibition of downstream phospho-Erk1/2, phospho-AKT, and cyclin D steady-state protein levels.


Inhibition of p95ErbB2, << p185ErbB2 >>, and EGFR phosphorylation by [[ GW572016 ]] resulted in the inhibition of downstream phospho-Erk1/2, phospho-AKT, and cyclin D steady-state protein levels.


Inhibition of p95ErbB2, p185ErbB2, and << EGFR >> phosphorylation by [[ GW572016 ]] resulted in the inhibition of downstream phospho-Erk1/2, phospho-AKT, and cyclin D steady-state protein levels.


Increased phosphorylation of << p95ErbB2 >> and AKT in response to HRG was abrogated to varying degrees by [[ GW572016 ]].


Increased phosphorylation of p95ErbB2 and << AKT >> in response to HRG was abrogated to varying degrees by [[ GW572016 ]].


<< Sulindac sulfide >> inhibited [[ 14-3-3epsilon proteins ]] in HT-29 and DLD-1 cells in a time- and concentration-dependent manner.


<< Indomethacin >> and SC-236, a selective [[ cyclooxygenase-2 ]] (COX-2) inhibitor, exerted a similar effect as sulindac.


<< Indomethacin >> and SC-236, a selective cyclooxygenase-2 ([[ COX-2 ]]) inhibitor, exerted a similar effect as sulindac.


Indomethacin and << SC-236 >>, a selective [[ cyclooxygenase-2 ]] (COX-2) inhibitor, exerted a similar effect as sulindac.


Indomethacin and << SC-236 >>, a selective cyclooxygenase-2 ([[ COX-2 ]]) inhibitor, exerted a similar effect as sulindac.


<< Sulindac sulfide >> inhibited [[ PPARdelta ]] protein expression and PPARdelta transcriptional activity.


<< Sulindac sulfide >> inhibited PPARdelta protein expression and [[ PPARdelta ]] transcriptional activity.


Synergistic cytotoxicity was demonstrated, and << pemetrexed >> significantly decreased the amount of phosphorylated Akt, enhanced apoptosis, and increased the expression of [[ dCK ]] in A549 and Calu-6 cells, as well as the expression of the human nucleoside equilibrative transporter 1 (hENT1) in all cell lines.


Synergistic cytotoxicity was demonstrated, and << pemetrexed >> significantly decreased the amount of phosphorylated Akt, enhanced apoptosis, and increased the expression of dCK in A549 and Calu-6 cells, as well as the expression of the [[ human nucleoside equilibrative transporter 1 ]] (hENT1) in all cell lines.


Synergistic cytotoxicity was demonstrated, and << pemetrexed >> significantly decreased the amount of phosphorylated Akt, enhanced apoptosis, and increased the expression of dCK in A549 and Calu-6 cells, as well as the expression of the human nucleoside equilibrative transporter 1 ([[ hENT1 ]]) in all cell lines.


Synergistic cytotoxicity was demonstrated, and << pemetrexed >> significantly decreased the amount of [[ phosphorylated Akt ]], enhanced apoptosis, and increased the expression of dCK in A549 and Calu-6 cells, as well as the expression of the human nucleoside equilibrative transporter 1 (hENT1) in all cell lines.


These data demonstrated that 1) gemcitabine and pemetrexed synergistically interact against NSCLC cells through the suppression of Akt phosphorylation and induction of apoptosis; 2) the gene expression profile of critical genes may predict for drug chemosensitivity; and 3) << pemetrexed >> enhances [[ dCK ]] and hENT1 expression, thus suggesting the role of gene-expression modulation for rational development of chemotherapy combinations.


These data demonstrated that 1) gemcitabine and pemetrexed synergistically interact against NSCLC cells through the suppression of Akt phosphorylation and induction of apoptosis; 2) the gene expression profile of critical genes may predict for drug chemosensitivity; and 3) << pemetrexed >> enhances dCK and [[ hENT1 ]] expression, thus suggesting the role of gene-expression modulation for rational development of chemotherapy combinations.


These data demonstrated that 1) << gemcitabine >> and pemetrexed synergistically interact against NSCLC cells through the suppression of [[ Akt ]] phosphorylation and induction of apoptosis; 2) the gene expression profile of critical genes may predict for drug chemosensitivity; and 3) pemetrexed enhances dCK and hENT1 expression, thus suggesting the role of gene-expression modulation for rational development of chemotherapy combinations.


These data demonstrated that 1) gemcitabine and << pemetrexed >> synergistically interact against NSCLC cells through the suppression of [[ Akt ]] phosphorylation and induction of apoptosis; 2) the gene expression profile of critical genes may predict for drug chemosensitivity; and 3) pemetrexed enhances dCK and hENT1 expression, thus suggesting the role of gene-expression modulation for rational development of chemotherapy combinations.


<< Kynurenic acid >> (KA) is an endogenous [[ glutamate receptor ]] antagonist at the level of the different ionotropic glutamate receptors.


<< Kynurenic acid >> (KA) is an endogenous glutamate receptor antagonist at the level of the different [[ ionotropic glutamate receptors ]].


Kynurenic acid (<< KA >>) is an endogenous [[ glutamate receptor ]] antagonist at the level of the different ionotropic glutamate receptors.


Kynurenic acid (<< KA >>) is an endogenous glutamate receptor antagonist at the level of the different [[ ionotropic glutamate receptors ]].


One of the enzymes responsible for the production of << KA >>, [[ kynurenine aminotransferase I ]] (KATI), also catalyses the reversible transamination of glutamine to oxoglutaramic acid (GTK, EC 2.6.1.15).


One of the enzymes responsible for the production of << KA >>, kynurenine aminotransferase I ([[ KATI ]]), also catalyses the reversible transamination of glutamine to oxoglutaramic acid (GTK, EC 2.6.1.15).


One of the enzymes responsible for the production of KA, << kynurenine aminotransferase I >> (KATI), also catalyses the reversible transamination of [[ glutamine ]] to oxoglutaramic acid (GTK, EC 2.6.1.15).


One of the enzymes responsible for the production of KA, kynurenine aminotransferase I (<< KATI >>), also catalyses the reversible transamination of [[ glutamine ]] to oxoglutaramic acid (GTK, EC 2.6.1.15).


One of the enzymes responsible for the production of KA, kynurenine aminotransferase I (KATI), also catalyses the reversible transamination of << glutamine >> to oxoglutaramic acid ([[ GTK ]], EC 2.6.1.15).


One of the enzymes responsible for the production of KA, << kynurenine aminotransferase I >> (KATI), also catalyses the reversible transamination of glutamine to [[ oxoglutaramic acid ]] (GTK, EC 2.6.1.15).


One of the enzymes responsible for the production of KA, kynurenine aminotransferase I (<< KATI >>), also catalyses the reversible transamination of glutamine to [[ oxoglutaramic acid ]] (GTK, EC 2.6.1.15).


One of the enzymes responsible for the production of KA, kynurenine aminotransferase I (KATI), also catalyses the reversible transamination of glutamine to << oxoglutaramic acid >> ([[ GTK ]], EC 2.6.1.15).


One of the enzymes responsible for the production of KA, kynurenine aminotransferase I (KATI), also catalyses the reversible transamination of glutamine to << oxoglutaramic acid >> (GTK, [[ EC 2.6.1.15 ]]).


Combined treatment of << Mn >> and DA further augments cell toxicity, ROS production and [[ JNK ]] phosphorylation in LRRK2 deficient cells compared to controls.


The results showed that IR tyrosine phosphorylation (<< pIR >>) was reduced by 42 % in MSG-obese mice (MSG, 6.7 ± 0.2 arbitrary units (a.u.); control, 11.5 ± 0.4 a.u.); on the other hand, exercise training increased pIR by 76 % in MSG mice without affecting control mice ([[ MSG ]], 11.8 ± 0.3; control, 12.8 ± 0.2 a.u.).


The results showed that IR tyrosine phosphorylation (pIR) was reduced by 42 % in MSG-obese mice (MSG, 6.7 ± 0.2 arbitrary units (a.u.); control, 11.5 ± 0.4 a.u.); on the other hand, exercise training increased << pIR >> by 76 % in MSG mice without affecting control mice ([[ MSG ]], 11.8 ± 0.3; control, 12.8 ± 0.2 a.u.).


The results showed that IR tyrosine phosphorylation (<< pIR >>) was reduced by 42 % in [[ MSG ]]-obese mice (MSG, 6.7 ± 0.2 arbitrary units (a.u.); control, 11.5 ± 0.4 a.u.); on the other hand, exercise training increased pIR by 76 % in MSG mice without affecting control mice (MSG, 11.8 ± 0.3; control, 12.8 ± 0.2 a.u.).


The results showed that IR tyrosine phosphorylation (pIR) was reduced by 42 % in << MSG >>-obese mice (MSG, 6.7 ± 0.2 arbitrary units (a.u.); control, 11.5 ± 0.4 a.u.); on the other hand, exercise training increased [[ pIR ]] by 76 % in MSG mice without affecting control mice (MSG, 11.8 ± 0.3; control, 12.8 ± 0.2 a.u.).


The results showed that IR tyrosine phosphorylation (<< pIR >>) was reduced by 42 % in MSG-obese mice ([[ MSG ]], 6.7 ± 0.2 arbitrary units (a.u.); control, 11.5 ± 0.4 a.u.); on the other hand, exercise training increased pIR by 76 % in MSG mice without affecting control mice (MSG, 11.8 ± 0.3; control, 12.8 ± 0.2 a.u.).


The results showed that IR tyrosine phosphorylation (pIR) was reduced by 42 % in MSG-obese mice (<< MSG >>, 6.7 ± 0.2 arbitrary units (a.u.); control, 11.5 ± 0.4 a.u.); on the other hand, exercise training increased [[ pIR ]] by 76 % in MSG mice without affecting control mice (MSG, 11.8 ± 0.3; control, 12.8 ± 0.2 a.u.).


The results showed that IR tyrosine phosphorylation (<< pIR >>) was reduced by 42 % in MSG-obese mice (MSG, 6.7 ± 0.2 arbitrary units (a.u.); control, 11.5 ± 0.4 a.u.); on the other hand, exercise training increased pIR by 76 % in [[ MSG ]] mice without affecting control mice (MSG, 11.8 ± 0.3; control, 12.8 ± 0.2 a.u.).


The results showed that IR tyrosine phosphorylation (pIR) was reduced by 42 % in MSG-obese mice (MSG, 6.7 ± 0.2 arbitrary units (a.u.); control, 11.5 ± 0.4 a.u.); on the other hand, exercise training increased << pIR >> by 76 % in [[ MSG ]] mice without affecting control mice (MSG, 11.8 ± 0.3; control, 12.8 ± 0.2 a.u.).


Although the treatment with << MSG >> increased IRS-1 tyrosine phosphorylation ([[ pIRS-1 ]]) by 96 % (MSG, 17.02 ± 0.6; control, 8.7 ± 0.2 a.u.), exercise training also increased it in both groups (control, 13.6 ± 0.1; MSG, 22.2 ± 1.1 a.u.).


Although the treatment with MSG increased IRS-1 tyrosine phosphorylation (<< pIRS-1 >>) by 96 % ([[ MSG ]], 17.02 ± 0.6; control, 8.7 ± 0.2 a.u.), exercise training also increased it in both groups (control, 13.6 ± 0.1; MSG, 22.2 ± 1.1 a.u.).


Although the treatment with MSG increased IRS-1 tyrosine phosphorylation (<< pIRS-1 >>) by 96 % (MSG, 17.02 ± 0.6; control, 8.7 ± 0.2 a.u.), exercise training also increased it in both groups (control, 13.6 ± 0.1; [[ MSG ]], 22.2 ± 1.1 a.u.).


The scientific basis of this treatment of ED includes relaxation of the corpus cavernosum smooth muscle tissue by inhibition of << PDE5 >> that breaks down [[ cGMP ]], the key pathway for the production of erectile function in humans.


Many clinical studies, both pre- and post-marketing, have demonstrated the clinical efficacy and safety of << sildenafil >> (Viagra, Pfizer) - the first approved selective [[ PDE ]] inhibitor for the treatment of ED.


Many clinical studies, both pre- and post-marketing, have demonstrated the clinical efficacy and safety of sildenafil (<< Viagra >>, Pfizer) - the first approved selective [[ PDE ]] inhibitor for the treatment of ED.


<< Sildenafil >> is inhibitory of [[ PDE5 ]] at a rate tenfold higher than for the next PDE (PDE6), which produces visual changes through the retinal rods.


<< Sildenafil >> is inhibitory of PDE5 at a rate tenfold higher than for the next [[ PDE ]] (PDE6), which produces visual changes through the retinal rods.


<< Sildenafil >> is inhibitory of PDE5 at a rate tenfold higher than for the next PDE ([[ PDE6 ]]), which produces visual changes through the retinal rods.


With the use of << sildenafil >>, it has been clearly, clinically demonstrated that the selective inhibition of [[ PDE5 ]] is an appropriate, effective, safe method for the treatment of ED of all aetiologies and severities.


<< cAspAT >> activity, as well as the incorporation of [(14)C]aspartate into the neutral lipid fraction of 3T3-F442A adipocytes was stimulated by the [[ thiazolidinedione ]] (TZD) rosiglitazone.


<< cAspAT >> activity, as well as the incorporation of [(14)C]aspartate into the neutral lipid fraction of 3T3-F442A adipocytes was stimulated by the thiazolidinedione ([[ TZD ]]) rosiglitazone.


<< cAspAT >> activity, as well as the incorporation of [(14)C]aspartate into the neutral lipid fraction of 3T3-F442A adipocytes was stimulated by the thiazolidinedione (TZD) [[ rosiglitazone ]].


<< RORalpha >> ectopic expression activated the cAspAT gene transcription in absence of rosiglitazone, and its protein amount in nuclear extracts is 1.8-fold increased by [[ rosiglitazone ]] treatment of adipocytes.


RORalpha ectopic expression activated the << cAspAT >> gene transcription in absence of rosiglitazone, and its protein amount in nuclear extracts is 1.8-fold increased by [[ rosiglitazone ]] treatment of adipocytes.


Finally, the amounts of << RORalpha >> and cAspAT mRNAs were similarly increased by [[ TZD ]] treatment of human adipose tissue explants, confirming coordinated regulation.


Finally, the amounts of RORalpha and << cAspAT >> mRNAs were similarly increased by [[ TZD ]] treatment of human adipose tissue explants, confirming coordinated regulation.


Our data identify << cAspAT >> as a new member of glyceroneogenesis, transcriptionally regulated by [[ TZD ]] via the control of RORalpha expression by PPARgamma in adipocytes.


<< ABT-199 >>, a potent and selective [[ BCL-2 ]] inhibitor, achieves antitumor activity while sparing platelets.


The therapeutic potential of directly inhibiting prosurvival proteins was unveiled with the development of << navitoclax >>, a selective inhibitor of both [[ BCL-2 ]] and BCL-2-like 1 (BCL-X(L)), which has shown clinical efficacy in some BCL-2-dependent hematological cancers.


The therapeutic potential of directly inhibiting prosurvival proteins was unveiled with the development of << navitoclax >>, a selective inhibitor of both BCL-2 and [[ BCL-2-like 1 ]] (BCL-X(L)), which has shown clinical efficacy in some BCL-2-dependent hematological cancers.


The therapeutic potential of directly inhibiting prosurvival proteins was unveiled with the development of << navitoclax >>, a selective inhibitor of both BCL-2 and BCL-2-like 1 ([[ BCL-X(L) ]]), which has shown clinical efficacy in some BCL-2-dependent hematological cancers.


Here we report the re-engineering of << navitoclax >> to create a highly potent, orally bioavailable and [[ BCL-2 ]]-selective inhibitor, ABT-199.


Here we report the re-engineering of navitoclax to create a highly potent, orally bioavailable and << BCL-2 >>-selective inhibitor, [[ ABT-199 ]].


Suppression of TβR1 by the pharmacological inhibitor (<< SB431542 >>) markedly reduced [[ VEGF ]] release by HFL-1 in response to CSE and this effect was confirmed by TβR1 siRNA.


Suppression of << TβR1 >> by the pharmacological inhibitor ([[ SB431542 ]]) markedly reduced VEGF release by HFL-1 in response to CSE and this effect was confirmed by TβR1 siRNA.


<< NCFP >> binds to the CPPHA site on mGlu5 and potentiates [[ mGlu5 ]]-mediated responses in both recombinant and native systems.


Combination treatment with the selective << 5-HT1A >> antagonist [[ WAY100635 ]] produced a dose-dependent augmentation of venlafaxine-induced (3-30 mg/kg s.c) extracellular 5-HT concentrations, but had no further effect on NA above that produced by venlafaxine alone.


The beta-adrenergic/<< 5-HT1A >> receptor antagonist [[ (+/-)pindolol ]] and the selective 5-HT1B/D antagonist GR127935 produced no significant augmentation of venlafaxine-induced changes in either 5-HT or NA.


The selective GluR5 kainate receptor agonist ATPA induces spontaneous epileptiform bursting that is sensitive to the << GluR5 >> kainate receptor antagonist [[ LY293558 ]].


The selective GluR5 kainate receptor agonist ATPA induces spontaneous epileptiform bursting that is sensitive to the GluR5 << kainate receptor >> antagonist [[ LY293558 ]].


However, << topiramate >> at low concentrations causes slow inhibition of [[ GluR5 ]] kainate receptor-mediated synaptic currents in the basolateral amygdala, indicating that it may protect against seizures, at least in part, through suppression of GluR5 kainate receptor responses.


However, << topiramate >> at low concentrations causes slow inhibition of GluR5 [[ kainate receptor ]]-mediated synaptic currents in the basolateral amygdala, indicating that it may protect against seizures, at least in part, through suppression of GluR5 kainate receptor responses.


However, << topiramate >> at low concentrations causes slow inhibition of GluR5 kainate receptor-mediated synaptic currents in the basolateral amygdala, indicating that it may protect against seizures, at least in part, through suppression of [[ GluR5 ]] kainate receptor responses.


However, << topiramate >> at low concentrations causes slow inhibition of GluR5 kainate receptor-mediated synaptic currents in the basolateral amygdala, indicating that it may protect against seizures, at least in part, through suppression of GluR5 [[ kainate receptor ]] responses.


<< Multidrug resistance-associated proteins >> are involved in the transport of the [[ glutathione ]] conjugates of the ultimate carcinogen of benzo[a]pyrene in human Caco-2 cells.


The ultimate carcinogenic Phase I BP metabolite anti-BP-7,8-dihydrodiol-9,10-epoxide (BPDE) can be detoxified by << glutathione >> conjugate formation catalyzed by [[ glutathione S-transferases ]].


Inhibition studies revealed that the << multidrug resistance-associated proteins >> (ABCCs) are involved in the transport of [[ BPDE glutathione ]] conjugates.


Inhibition studies revealed that the multidrug resistance-associated proteins (<< ABCCs >>) are involved in the transport of [[ BPDE glutathione ]] conjugates.


Stable << ABCC1 >>, ABCC2 and ABCC3 knockdown cell lines were generated, thus making it possible to demonstrate that ABCC1 mediates the basolateral and ABCC2 the apical excretion of [[ BPDE glutathione ]] conjugates.


Stable ABCC1, << ABCC2 >> and ABCC3 knockdown cell lines were generated, thus making it possible to demonstrate that ABCC1 mediates the basolateral and ABCC2 the apical excretion of [[ BPDE glutathione ]] conjugates.


Stable ABCC1, ABCC2 and ABCC3 knockdown cell lines were generated, thus making it possible to demonstrate that << ABCC1 >> mediates the basolateral and ABCC2 the apical excretion of [[ BPDE glutathione ]] conjugates.


Stable ABCC1, ABCC2 and ABCC3 knockdown cell lines were generated, thus making it possible to demonstrate that ABCC1 mediates the basolateral and << ABCC2 >> the apical excretion of [[ BPDE glutathione ]] conjugates.


Pretreatment of human breast carcinoma MCF-7 cells for 24 h with the groundnut extract and soybean << isoflavone >> increased gene expression of [[ heme oxygenase-1 ]] (HO-1), a major antioxidative stress enzyme.


Pretreatment of human breast carcinoma MCF-7 cells for 24 h with the groundnut extract and soybean << isoflavone >> increased gene expression of heme oxygenase-1 ([[ HO-1 ]]), a major antioxidative stress enzyme.


Comparison of << cyclooxygenase >> inhibitory activity and ocular anti-inflammatory effects of ketorolac tromethamine and [[ bromfenac sodium ]].


Comparison of << cyclooxygenase >> inhibitory activity and ocular anti-inflammatory effects of [[ ketorolac tromethamine ]] and bromfenac sodium.


METHODS: << Cyclooxygenase >> activity and selectivity was determined in vitro by measuring [[ prostaglandin E(2) ]] (PGE(2)) production following incubation of varying concentrations of NSAID with human recombinant COX-1 or COX-2 and arachidonic acid.


METHODS: << Cyclooxygenase >> activity and selectivity was determined in vitro by measuring prostaglandin E(2) ([[ PGE(2) ]]) production following incubation of varying concentrations of NSAID with human recombinant COX-1 or COX-2 and arachidonic acid.


RESULTS: << Ketorolac >> was six times more active against COX-1 (IC(50) = 0.02 microM) than COX-2 (IC(50) = 0.12 microM) while bromfenac was approximately 32 times more active against [[ COX-2 ]] (IC(50) = 0.0066 microM) than COX-1 (IC(50) = 0.210 microM).


RESULTS: << Ketorolac >> was six times more active against COX-1 (IC(50) = 0.02 microM) than COX-2 (IC(50) = 0.12 microM) while bromfenac was approximately 32 times more active against COX-2 (IC(50) = 0.0066 microM) than [[ COX-1 ]] (IC(50) = 0.210 microM).


RESULTS: Ketorolac was six times more active against << COX-1 >> (IC(50) = 0.02 microM) than COX-2 (IC(50) = 0.12 microM) while [[ bromfenac ]] was approximately 32 times more active against COX-2 (IC(50) = 0.0066 microM) than COX-1 (IC(50) = 0.210 microM).


RESULTS: Ketorolac was six times more active against COX-1 (IC(50) = 0.02 microM) than << COX-2 >> (IC(50) = 0.12 microM) while [[ bromfenac ]] was approximately 32 times more active against COX-2 (IC(50) = 0.0066 microM) than COX-1 (IC(50) = 0.210 microM).


Tumor-growth-promoting << cyclooxygenase-2 >> [[ prostaglandin E2 ]] pathway provides medulloblastoma therapeutic targets.


<< PGE(2) >> is synthesized from arachidonic acid by [[ cyclooxygenases ]] (COX) and prostaglandin E synthases (PGES) and mediates its biological activity through binding to the four prostanoid receptors EP(1) through EP(4).


<< PGE(2) >> is synthesized from arachidonic acid by cyclooxygenases ([[ COX ]]) and prostaglandin E synthases (PGES) and mediates its biological activity through binding to the four prostanoid receptors EP(1) through EP(4).


<< PGE(2) >> is synthesized from arachidonic acid by cyclooxygenases (COX) and [[ prostaglandin E synthases ]] (PGES) and mediates its biological activity through binding to the four prostanoid receptors EP(1) through EP(4).


<< PGE(2) >> is synthesized from arachidonic acid by cyclooxygenases (COX) and prostaglandin E synthases ([[ PGES ]]) and mediates its biological activity through binding to the four prostanoid receptors EP(1) through EP(4).


PGE(2) is synthesized from << arachidonic acid >> by [[ cyclooxygenases ]] (COX) and prostaglandin E synthases (PGES) and mediates its biological activity through binding to the four prostanoid receptors EP(1) through EP(4).


PGE(2) is synthesized from << arachidonic acid >> by cyclooxygenases ([[ COX ]]) and prostaglandin E synthases (PGES) and mediates its biological activity through binding to the four prostanoid receptors EP(1) through EP(4).


PGE(2) is synthesized from << arachidonic acid >> by cyclooxygenases (COX) and [[ prostaglandin E synthases ]] (PGES) and mediates its biological activity through binding to the four prostanoid receptors EP(1) through EP(4).


PGE(2) is synthesized from << arachidonic acid >> by cyclooxygenases (COX) and prostaglandin E synthases ([[ PGES ]]) and mediates its biological activity through binding to the four prostanoid receptors EP(1) through EP(4).


<< EP(1) >> and EP(3) receptor antagonists [[ ONO-8713 ]] and ONO-AE3-240, but not the EP(4) antagonists ONO-AE3-208 and AH 23848, inhibited tumor cell proliferation, indicating the significance of EP(1) and EP(3) but not EP(4) for MB growth.


EP(1) and << EP(3) receptor >> antagonists [[ ONO-8713 ]] and ONO-AE3-240, but not the EP(4) antagonists ONO-AE3-208 and AH 23848, inhibited tumor cell proliferation, indicating the significance of EP(1) and EP(3) but not EP(4) for MB growth.


<< EP(1) >> and EP(3) receptor antagonists ONO-8713 and [[ ONO-AE3-240 ]], but not the EP(4) antagonists ONO-AE3-208 and AH 23848, inhibited tumor cell proliferation, indicating the significance of EP(1) and EP(3) but not EP(4) for MB growth.


EP(1) and << EP(3) receptor >> antagonists ONO-8713 and [[ ONO-AE3-240 ]], but not the EP(4) antagonists ONO-AE3-208 and AH 23848, inhibited tumor cell proliferation, indicating the significance of EP(1) and EP(3) but not EP(4) for MB growth.


EP(1) and EP(3) receptor antagonists ONO-8713 and ONO-AE3-240, but not the << EP(4) >> antagonists [[ ONO-AE3-208 ]] and AH 23848, inhibited tumor cell proliferation, indicating the significance of EP(1) and EP(3) but not EP(4) for MB growth.


EP(1) and EP(3) receptor antagonists ONO-8713 and ONO-AE3-240, but not the << EP(4) >> antagonists ONO-AE3-208 and [[ AH 23848 ]], inhibited tumor cell proliferation, indicating the significance of EP(1) and EP(3) but not EP(4) for MB growth.


Inhibitors of << PDE4 >> ([[ rolipram ]]; 0.1-10 microM) and PDE3 (cilostazol; 0.1-10 microM) delayed spontaneous eosinophil apoptosis maximally by 25% and 15%, respectively.


Inhibitors of PDE4 (rolipram; 0.1-10 microM) and << PDE3 >> ([[ cilostazol ]]; 0.1-10 microM) delayed spontaneous eosinophil apoptosis maximally by 25% and 15%, respectively.


Inhibitor of << cGMP-specific PDE5 >> ([[ zaprinast ]]; 0.1-10 microM) did not affect eosinophil apoptosis and only slightly increased spontaneous neutrophil apoptosis.


<< GW9662 >>, a PPARgamma antagonist, prevented (P < 0.01) the lutein-induced [[ iNOS ]] mRNA downregulation in HD11 cells.


<< GW9662 >>, a [[ PPARgamma ]] antagonist, prevented (P < 0.01) the lutein-induced iNOS mRNA downregulation in HD11 cells.


Stereospecific inhibition of << monoamine uptake transporters >> by [[ meta-hydroxyephedrine ]] isomers.


To extend structure-activity analyses of binding sites within << monoamine transporters >> and to determine which stereoisomer displayed the best selectivity for PET imaging applications, we tested the [[ HED ]] compounds for their abilities to inhibit [(3)H]neurotransmitter uptake into platelets, transfected cells, and chromaffin vesicles.


We hypothesized that the << HED >> compounds would be most potent at the [[ norepinephrine transporter ]] (NET) compared to the serotonin or dopamine transporters and that the 1R diastereomers would be more effective than 1S diastereomers.


We hypothesized that the << HED >> compounds would be most potent at the norepinephrine transporter ([[ NET ]]) compared to the serotonin or dopamine transporters and that the 1R diastereomers would be more effective than 1S diastereomers.


<< TCDD >> inhibition of canonical [[ wnt ]] signaling disrupts prostatic bud formation in mouse urogenital sinus.


In support of the hypothesis that TCDD decreases canonical Wnt signaling, we identify inhibitory effects of TCDD on multiple components of the canonical Wnt signaling pathway in the UGS that temporally coincide with the inhibitory effect of << TCDD >> on prostatic bud formation: (1) expression of R-spondins (Rspo2 and Rspo3) that promote canonical Wnt signaling is reduced; (2) expression of Lef1, Tcf1, and Wif1, established canonical Wnt target genes, is decreased; (3) expression of [[ Lgr5 ]], a RSPO receptor that activates canonical Wnt signaling, is reduced; and (4) expression of Dickkopfs (Dkks), inhibitors of canonical Wnt signaling, is not increased by TCDD.


In support of the hypothesis that TCDD decreases canonical Wnt signaling, we identify inhibitory effects of TCDD on multiple components of the canonical Wnt signaling pathway in the UGS that temporally coincide with the inhibitory effect of << TCDD >> on prostatic bud formation: (1) expression of R-spondins (Rspo2 and Rspo3) that promote canonical Wnt signaling is reduced; (2) expression of Lef1, Tcf1, and Wif1, established canonical Wnt target genes, is decreased; (3) expression of Lgr5, a [[ RSPO receptor ]] that activates canonical Wnt signaling, is reduced; and (4) expression of Dickkopfs (Dkks), inhibitors of canonical Wnt signaling, is not increased by TCDD.


In support of the hypothesis that TCDD decreases canonical Wnt signaling, we identify inhibitory effects of TCDD on multiple components of the canonical Wnt signaling pathway in the UGS that temporally coincide with the inhibitory effect of << TCDD >> on prostatic bud formation: (1) expression of [[ R-spondins ]] (Rspo2 and Rspo3) that promote canonical Wnt signaling is reduced; (2) expression of Lef1, Tcf1, and Wif1, established canonical Wnt target genes, is decreased; (3) expression of Lgr5, a RSPO receptor that activates canonical Wnt signaling, is reduced; and (4) expression of Dickkopfs (Dkks), inhibitors of canonical Wnt signaling, is not increased by TCDD.


In support of the hypothesis that TCDD decreases canonical Wnt signaling, we identify inhibitory effects of TCDD on multiple components of the canonical Wnt signaling pathway in the UGS that temporally coincide with the inhibitory effect of << TCDD >> on prostatic bud formation: (1) expression of R-spondins ([[ Rspo2 ]] and Rspo3) that promote canonical Wnt signaling is reduced; (2) expression of Lef1, Tcf1, and Wif1, established canonical Wnt target genes, is decreased; (3) expression of Lgr5, a RSPO receptor that activates canonical Wnt signaling, is reduced; and (4) expression of Dickkopfs (Dkks), inhibitors of canonical Wnt signaling, is not increased by TCDD.


In support of the hypothesis that TCDD decreases canonical Wnt signaling, we identify inhibitory effects of TCDD on multiple components of the canonical Wnt signaling pathway in the UGS that temporally coincide with the inhibitory effect of << TCDD >> on prostatic bud formation: (1) expression of R-spondins (Rspo2 and [[ Rspo3 ]]) that promote canonical Wnt signaling is reduced; (2) expression of Lef1, Tcf1, and Wif1, established canonical Wnt target genes, is decreased; (3) expression of Lgr5, a RSPO receptor that activates canonical Wnt signaling, is reduced; and (4) expression of Dickkopfs (Dkks), inhibitors of canonical Wnt signaling, is not increased by TCDD.


In support of the hypothesis that TCDD decreases canonical Wnt signaling, we identify inhibitory effects of TCDD on multiple components of the canonical Wnt signaling pathway in the UGS that temporally coincide with the inhibitory effect of << TCDD >> on prostatic bud formation: (1) expression of R-spondins (Rspo2 and Rspo3) that promote canonical Wnt signaling is reduced; (2) expression of [[ Lef1 ]], Tcf1, and Wif1, established canonical Wnt target genes, is decreased; (3) expression of Lgr5, a RSPO receptor that activates canonical Wnt signaling, is reduced; and (4) expression of Dickkopfs (Dkks), inhibitors of canonical Wnt signaling, is not increased by TCDD.


In support of the hypothesis that TCDD decreases canonical Wnt signaling, we identify inhibitory effects of TCDD on multiple components of the canonical Wnt signaling pathway in the UGS that temporally coincide with the inhibitory effect of << TCDD >> on prostatic bud formation: (1) expression of R-spondins (Rspo2 and Rspo3) that promote canonical Wnt signaling is reduced; (2) expression of Lef1, [[ Tcf1 ]], and Wif1, established canonical Wnt target genes, is decreased; (3) expression of Lgr5, a RSPO receptor that activates canonical Wnt signaling, is reduced; and (4) expression of Dickkopfs (Dkks), inhibitors of canonical Wnt signaling, is not increased by TCDD.


In support of the hypothesis that TCDD decreases canonical Wnt signaling, we identify inhibitory effects of TCDD on multiple components of the canonical Wnt signaling pathway in the UGS that temporally coincide with the inhibitory effect of << TCDD >> on prostatic bud formation: (1) expression of R-spondins (Rspo2 and Rspo3) that promote canonical Wnt signaling is reduced; (2) expression of Lef1, Tcf1, and [[ Wif1 ]], established canonical Wnt target genes, is decreased; (3) expression of Lgr5, a RSPO receptor that activates canonical Wnt signaling, is reduced; and (4) expression of Dickkopfs (Dkks), inhibitors of canonical Wnt signaling, is not increased by TCDD.


In support of the hypothesis that << TCDD >> decreases canonical [[ Wnt ]] signaling, we identify inhibitory effects of TCDD on multiple components of the canonical Wnt signaling pathway in the UGS that temporally coincide with the inhibitory effect of TCDD on prostatic bud formation: (1) expression of R-spondins (Rspo2 and Rspo3) that promote canonical Wnt signaling is reduced; (2) expression of Lef1, Tcf1, and Wif1, established canonical Wnt target genes, is decreased; (3) expression of Lgr5, a RSPO receptor that activates canonical Wnt signaling, is reduced; and (4) expression of Dickkopfs (Dkks), inhibitors of canonical Wnt signaling, is not increased by TCDD.


Thus, the << TCDD >>-induced reduction in canonical Wnt signaling is associated with a decrease in activators ([[ Rspo2 ]] and Rspo3) rather than an increase in inhibitors (Dkk1 and Dkk2) of the pathway.


Thus, the << TCDD >>-induced reduction in canonical Wnt signaling is associated with a decrease in activators (Rspo2 and [[ Rspo3 ]]) rather than an increase in inhibitors (Dkk1 and Dkk2) of the pathway.


Thus, the << TCDD >>-induced reduction in canonical Wnt signaling is associated with a decrease in activators (Rspo2 and Rspo3) rather than an increase in inhibitors ([[ Dkk1 ]] and Dkk2) of the pathway.


Thus, the << TCDD >>-induced reduction in canonical Wnt signaling is associated with a decrease in activators (Rspo2 and Rspo3) rather than an increase in inhibitors (Dkk1 and [[ Dkk2 ]]) of the pathway.


Thus, the << TCDD >>-induced reduction in canonical [[ Wnt ]] signaling is associated with a decrease in activators (Rspo2 and Rspo3) rather than an increase in inhibitors (Dkk1 and Dkk2) of the pathway.


This study focuses on determining whether treatment of TCDD-exposed UGS organ cultures with RSPO2 and/or RSPO3 is capable of rescuing the inhibitory effects of << TCDD >> on canonical [[ Wnt ]] signaling and prostatic bud formation.


We discovered that each RSPO alone or in combination partially rescues << TCDD >> inhibition of both canonical [[ Wnt ]] signaling and prostatic bud formation.


<< Cytochrome P450 epoxygenase 2J2 >> (CYP2J2) metabolizes arachidonic acids to form epoxyeicosatrienoic acids ([[ EETs ]]), which possess various beneficial effects on the cardiovascular system.


Cytochrome P450 epoxygenase 2J2 (<< CYP2J2 >>) metabolizes arachidonic acids to form epoxyeicosatrienoic acids ([[ EETs ]]), which possess various beneficial effects on the cardiovascular system.


<< Cytochrome P450 epoxygenase 2J2 >> (CYP2J2) metabolizes arachidonic acids to form [[ epoxyeicosatrienoic acids ]] (EETs), which possess various beneficial effects on the cardiovascular system.


Cytochrome P450 epoxygenase 2J2 (<< CYP2J2 >>) metabolizes arachidonic acids to form [[ epoxyeicosatrienoic acids ]] (EETs), which possess various beneficial effects on the cardiovascular system.


<< Cytochrome P450 epoxygenase 2J2 >> (CYP2J2) metabolizes [[ arachidonic acids ]] to form epoxyeicosatrienoic acids (EETs), which possess various beneficial effects on the cardiovascular system.


Cytochrome P450 epoxygenase 2J2 (<< CYP2J2 >>) metabolizes [[ arachidonic acids ]] to form epoxyeicosatrienoic acids (EETs), which possess various beneficial effects on the cardiovascular system.


However, whether increasing << EETs >> production by [[ CYP2J2 ]] overexpression in vivo could prevent abdominal aortic aneurysm (AAA) remains unknown.


In cultured vascular smooth muscle cells (VSMCs), rAAV-mediated CYP2J2 overexpression and << EETs >> markedly suppressed Ang II-induced inflammatory [[ cytokine ]] expression.


In cultured vascular smooth muscle cells (VSMCs), rAAV-mediated CYP2J2 overexpression and << EETs >> markedly suppressed [[ Ang II ]]-induced inflammatory cytokine expression.


Moreover, overexpressed CYP2J2 and << EETs >> inhibited [[ Ang II ]]-induced macrophage migration in a VSMC-macrophage coculture system.


A decrease in << ADA >> activity was observed when the slices were exposed to [[ organoselenium ]] at the concentrations of 1, 10 and 30 µM.


Cotreatments of 5, 10 and 20 µg/mL concentrations of MEP with << aflatoxin B(1) >> decreased the frequencies of SCE and the malondialdehyde level and increased amount of [[ superoxide dismutase ]], glutathione and glutathione peroxidase which were decreased by aflatoxin.


Cotreatments of 5, 10 and 20 µg/mL concentrations of MEP with aflatoxin B(1) decreased the frequencies of SCE and the malondialdehyde level and increased amount of superoxide dismutase, glutathione and << glutathione peroxidase >> which were decreased by [[ aflatoxin ]].


<< Phenobarbital >> (PB), a typical [[ CAR ]] activator, increased the gene expression of HIF-target genes in the livers of mice, including erythropoietin, heme oxygenase-1 and vascular endothelial growth factor-a.


<< Phenobarbital >> (PB), a typical CAR activator, increased the gene expression of HIF-target genes in the livers of mice, including [[ erythropoietin ]], heme oxygenase-1 and vascular endothelial growth factor-a.


<< Phenobarbital >> (PB), a typical CAR activator, increased the gene expression of HIF-target genes in the livers of mice, including erythropoietin, [[ heme oxygenase-1 ]] and vascular endothelial growth factor-a.


<< Phenobarbital >> (PB), a typical CAR activator, increased the gene expression of HIF-target genes in the livers of mice, including erythropoietin, heme oxygenase-1 and [[ vascular endothelial growth factor-a ]].


<< Cobalt chloride >>, a typical [[ HIF ]] activator, induced the gene expression of CAR-target genes, including cyp2b9 and cyp2b10, an accumulation of nuclear CAR and an increase in the PB-responsive enhancer module-mediated transactivation in the mouse liver.


<< Cobalt chloride >>, a typical HIF activator, induced the gene expression of CAR-target genes, including [[ cyp2b9 ]] and cyp2b10, an accumulation of nuclear CAR and an increase in the PB-responsive enhancer module-mediated transactivation in the mouse liver.


<< Cobalt chloride >>, a typical HIF activator, induced the gene expression of CAR-target genes, including cyp2b9 and [[ cyp2b10 ]], an accumulation of nuclear CAR and an increase in the PB-responsive enhancer module-mediated transactivation in the mouse liver.


BACKGROUND & AIMS: Of the 2 genes (MAT1A, MAT2A) encoding methionine adenosyltransferase, the enzyme that synthesizes << S-adenosylmethionine >>, [[ MAT1A ]], is expressed in liver, whereas MAT2A is expressed in extrahepatic tissues.


BACKGROUND & AIMS: Of the 2 genes (<< MAT1A >>, MAT2A) encoding methionine adenosyltransferase, the enzyme that synthesizes [[ S-adenosylmethionine ]], MAT1A, is expressed in liver, whereas MAT2A is expressed in extrahepatic tissues.


BACKGROUND & AIMS: Of the 2 genes (MAT1A, << MAT2A >>) encoding methionine adenosyltransferase, the enzyme that synthesizes [[ S-adenosylmethionine ]], MAT1A, is expressed in liver, whereas MAT2A is expressed in extrahepatic tissues.


BACKGROUND & AIMS: Of the 2 genes (MAT1A, MAT2A) encoding << methionine adenosyltransferase >>, the enzyme that synthesizes [[ S-adenosylmethionine ]], MAT1A, is expressed in liver, whereas MAT2A is expressed in extrahepatic tissues.


The beta subunit has been cloned and shown to lower the K(m) of << methionine adenosyltransferase II alpha2 >> (the MAT2A product) for methionine and to render the enzyme more susceptible to [[ S-adenosylmethionine ]] inhibition.


The beta subunit has been cloned and shown to lower the K(m) of methionine adenosyltransferase II alpha2 (the << MAT2A >> product) for methionine and to render the enzyme more susceptible to [[ S-adenosylmethionine ]] inhibition.


The beta subunit has been cloned and shown to lower the K(m) of << methionine adenosyltransferase II alpha2 >> (the MAT2A product) for [[ methionine ]] and to render the enzyme more susceptible to S-adenosylmethionine inhibition.


The beta subunit has been cloned and shown to lower the K(m) of methionine adenosyltransferase II alpha2 (the << MAT2A >> product) for [[ methionine ]] and to render the enzyme more susceptible to S-adenosylmethionine inhibition.


Structural features of the central cannabinoid CB1 receptor involved in the binding of the specific << CB1 >> antagonist [[ SR 141716A ]].


The channel activators << avermectin >> and moxidectin usually retain their inhibitory potency in the [[ Rdl ]] subunit mutants.


The channel activators avermectin and << moxidectin >> usually retain their inhibitory potency in the [[ Rdl ]] subunit mutants.


At 10(-6)M in transcription assays, none of these compounds showed progestin agonist activity, whereas << mifepristone >> and its monodemethylated metabolite manifested slight [[ glucocorticoid ]] agonist activity.


5-Fluorouracil (<< 5-FU >>), 5-fluoro-2'-deoxyuridine (FdUrd) and 5-trifluorothymidine (F3(d)Thd) are antimetabolites which are metabolized to their corresponding active forms which inhibit DNA synthesis via inhibition of [[ thymidylate synthase ]] (TS).


5-Fluorouracil (<< 5-FU >>), 5-fluoro-2'-deoxyuridine (FdUrd) and 5-trifluorothymidine (F3(d)Thd) are antimetabolites which are metabolized to their corresponding active forms which inhibit DNA synthesis via inhibition of thymidylate synthase ([[ TS ]]).


<< 5-Fluorouracil >> (5-FU), 5-fluoro-2'-deoxyuridine (FdUrd) and 5-trifluorothymidine (F3(d)Thd) are antimetabolites which are metabolized to their corresponding active forms which inhibit DNA synthesis via inhibition of [[ thymidylate synthase ]] (TS).


<< 5-Fluorouracil >> (5-FU), 5-fluoro-2'-deoxyuridine (FdUrd) and 5-trifluorothymidine (F3(d)Thd) are antimetabolites which are metabolized to their corresponding active forms which inhibit DNA synthesis via inhibition of thymidylate synthase ([[ TS ]]).


5-Fluorouracil (5-FU), << 5-fluoro-2'-deoxyuridine >> (FdUrd) and 5-trifluorothymidine (F3(d)Thd) are antimetabolites which are metabolized to their corresponding active forms which inhibit DNA synthesis via inhibition of [[ thymidylate synthase ]] (TS).


5-Fluorouracil (5-FU), << 5-fluoro-2'-deoxyuridine >> (FdUrd) and 5-trifluorothymidine (F3(d)Thd) are antimetabolites which are metabolized to their corresponding active forms which inhibit DNA synthesis via inhibition of thymidylate synthase ([[ TS ]]).


5-Fluorouracil (5-FU), 5-fluoro-2'-deoxyuridine (<< FdUrd >>) and 5-trifluorothymidine (F3(d)Thd) are antimetabolites which are metabolized to their corresponding active forms which inhibit DNA synthesis via inhibition of [[ thymidylate synthase ]] (TS).


5-Fluorouracil (5-FU), 5-fluoro-2'-deoxyuridine (<< FdUrd >>) and 5-trifluorothymidine (F3(d)Thd) are antimetabolites which are metabolized to their corresponding active forms which inhibit DNA synthesis via inhibition of thymidylate synthase ([[ TS ]]).


5-Fluorouracil (5-FU), 5-fluoro-2'-deoxyuridine (FdUrd) and << 5-trifluorothymidine >> (F3(d)Thd) are antimetabolites which are metabolized to their corresponding active forms which inhibit DNA synthesis via inhibition of [[ thymidylate synthase ]] (TS).


5-Fluorouracil (5-FU), 5-fluoro-2'-deoxyuridine (FdUrd) and << 5-trifluorothymidine >> (F3(d)Thd) are antimetabolites which are metabolized to their corresponding active forms which inhibit DNA synthesis via inhibition of thymidylate synthase ([[ TS ]]).


5-Fluorouracil (5-FU), 5-fluoro-2'-deoxyuridine (FdUrd) and 5-trifluorothymidine (<< F3(d)Thd >>) are antimetabolites which are metabolized to their corresponding active forms which inhibit DNA synthesis via inhibition of [[ thymidylate synthase ]] (TS).


5-Fluorouracil (5-FU), 5-fluoro-2'-deoxyuridine (FdUrd) and 5-trifluorothymidine (<< F3(d)Thd >>) are antimetabolites which are metabolized to their corresponding active forms which inhibit DNA synthesis via inhibition of thymidylate synthase ([[ TS ]]).


When DLD-1/FdUrd cells expressing increased TS mRNA were treated with FdUrd and F3(d)Thd for only 4 h, the resistance ratios of DLD-1/FdUrd cells to parental DLD-1 cells were markedly different for FdUrd and F3(d)Thd, suggesting that the cytotoxicity with short-time exposure to << F3(d)Thd >> is due to a mechanism other than [[ TS ]] inhibition, although the cytotoxicity of F3(d)Thd in the short-time is low compared to that of long-time exposure.


In conclusion, << F3(d)Thd >>, an antimetabolite that inhibits [[ TS ]] activity, may be effective against 5-FU and/or FdUrd-resistance in colorectal cancer cells caused by amplification of TS and/or deletion of orotate phosphoribosyltransferase.


The failure of the myometrium to respond to << ritodrine >> (desensitization) was associated with significant reductions in agonist-induced cyclic adenosine monophosphate production and [[ beta 2-adrenergic receptor ]] concentration in myometrial tissue collected from these animals compared with the saline solution-treated controls.


Antiarrhythmic effects of << (-)-epicatechin-3-gallate >>, a novel [[ sodium channel ]] agonist in cultured neonatal rat ventricular myocytes.


<< Choline dehydrogenase >> (CHDH) and betaine-homocysteine methyltransferase (BHMT) are 2 enzymes involved in [[ choline ]] oxidation.


Choline dehydrogenase (<< CHDH >>) and betaine-homocysteine methyltransferase (BHMT) are 2 enzymes involved in [[ choline ]] oxidation.


Choline dehydrogenase (CHDH) and << betaine-homocysteine methyltransferase >> (BHMT) are 2 enzymes involved in [[ choline ]] oxidation.


Choline dehydrogenase (CHDH) and betaine-homocysteine methyltransferase (<< BHMT >>) are 2 enzymes involved in [[ choline ]] oxidation.


Liver << BHMT >> activity was 1.3-fold higher in rats fed the Met deficient diet containing [[ choline ]], which was reflected in corresponding increases in mRNA content and immunodetectable protein.


Independent of dietary << choline >>, supplemental Met increased hepatic [[ BHMT ]] activity approximately 30%.


Independent of dietary choline, supplemental << Met >> increased hepatic [[ BHMT ]] activity approximately 30%.


The << calcium >> homeostasis proteins sarcoendoplasmic reticulum ATPase 2a (SERCA2a), sodium calcium exchanger-1, phospholamban ([[ PLB ]]), phospho-PLB, and calsequestrin 2 are important for contraction and relaxation.


The << calcium >> homeostasis proteins sarcoendoplasmic reticulum ATPase 2a (SERCA2a), sodium calcium exchanger-1, phospholamban (PLB), [[ phospho-PLB ]], and calsequestrin 2 are important for contraction and relaxation.


The << calcium >> homeostasis proteins sarcoendoplasmic reticulum ATPase 2a (SERCA2a), sodium calcium exchanger-1, phospholamban (PLB), phospho-PLB, and [[ calsequestrin 2 ]] are important for contraction and relaxation.


The << calcium >> homeostasis proteins [[ sarcoendoplasmic reticulum ATPase 2a ]] (SERCA2a), sodium calcium exchanger-1, phospholamban (PLB), phospho-PLB, and calsequestrin 2 are important for contraction and relaxation.


The << calcium >> homeostasis proteins sarcoendoplasmic reticulum ATPase 2a ([[ SERCA2a ]]), sodium calcium exchanger-1, phospholamban (PLB), phospho-PLB, and calsequestrin 2 are important for contraction and relaxation.


The << calcium >> homeostasis proteins sarcoendoplasmic reticulum ATPase 2a (SERCA2a), [[ sodium calcium exchanger-1 ]], phospholamban (PLB), phospho-PLB, and calsequestrin 2 are important for contraction and relaxation.


The << calcium >> homeostasis proteins sarcoendoplasmic reticulum ATPase 2a (SERCA2a), sodium calcium exchanger-1, [[ phospholamban ]] (PLB), phospho-PLB, and calsequestrin 2 are important for contraction and relaxation.


<< DNA methyltransferase 3a >> expression was increased in all [[ BPA ]] males and BPA 0.5 females and reduced in BPA 200 females.


<< DNA methyltransferase 3a >> expression was increased in all BPA males and [[ BPA ]] 0.5 females and reduced in BPA 200 females.


<< DNA methyltransferase 3a >> expression was increased in all BPA males and BPA 0.5 females and reduced in [[ BPA ]] 200 females.


The results showed that << wogonoside >> promotes the expression of [[ LC3-II ]] and Beclin-1.


The results showed that << wogonoside >> promotes the expression of LC3-II and [[ Beclin-1 ]].


<< Wogonoside >> also suppressed the activation of mammalian target of rapamycin (mTOR) and [[ p70-S6 kinase ]] (p70S6K) by regulating the expression of the extracellular signal-regulated kinase (ERK1/2) and p38 involved mitogen-activated protein kinase (MAPK) signaling pathway.


<< Wogonoside >> also suppressed the activation of mammalian target of rapamycin (mTOR) and p70-S6 kinase ([[ p70S6K) ]] by regulating the expression of the extracellular signal-regulated kinase (ERK1/2) and p38 involved mitogen-activated protein kinase (MAPK) signaling pathway.


<< Wogonoside >> also suppressed the activation of [[ mammalian target of rapamycin ]] (mTOR) and p70-S6 kinase (p70S6K) by regulating the expression of the extracellular signal-regulated kinase (ERK1/2) and p38 involved mitogen-activated protein kinase (MAPK) signaling pathway.


<< Wogonoside >> also suppressed the activation of mammalian target of rapamycin ([[ mTOR ]]) and p70-S6 kinase (p70S6K) by regulating the expression of the extracellular signal-regulated kinase (ERK1/2) and p38 involved mitogen-activated protein kinase (MAPK) signaling pathway.


The << mitochondrial respiratory chain complex IV >> (cytochrome c oxidase) is a multi-subunit enzyme that transfers electrons from cytochrome c to molecular [[ oxygen ]], yielding water.


The mitochondrial respiratory chain complex IV (<< cytochrome c oxidase >>) is a multi-subunit enzyme that transfers electrons from cytochrome c to molecular [[ oxygen ]], yielding water.


<< Pelargonidin >> activates the [[ AhR ]] and induces CYP1A1 in primary human hepatocytes and human cancer cell lines HepG2 and LS174T.


<< AhR >>-dependent reporter gene expression in transfected HepG2 cells was increased by [[ pelargonidin ]] in a concentration-dependent manner at 24h.


Similarly, pelargonidin induced the expression of CYP1A1 mRNA up to 5-fold in HepG2 and LS174T cells relative to the induction by 5 nM << 2,3,7,8-tetrachlorodibenzodioxin >> (TCDD), the most potent activator of [[ AhR ]].


Similarly, pelargonidin induced the expression of CYP1A1 mRNA up to 5-fold in HepG2 and LS174T cells relative to the induction by 5 nM 2,3,7,8-tetrachlorodibenzodioxin (<< TCDD >>), the most potent activator of [[ AhR ]].


Similarly, << pelargonidin >> induced the expression of [[ CYP1A1 ]] mRNA up to 5-fold in HepG2 and LS174T cells relative to the induction by 5 nM 2,3,7,8-tetrachlorodibenzodioxin (TCDD), the most potent activator of AhR.


Similarly, pelargonidin induced the expression of << CYP1A1 >> mRNA up to 5-fold in HepG2 and LS174T cells relative to the induction by 5 nM [[ 2,3,7,8-tetrachlorodibenzodioxin ]] (TCDD), the most potent activator of AhR.


Similarly, pelargonidin induced the expression of << CYP1A1 >> mRNA up to 5-fold in HepG2 and LS174T cells relative to the induction by 5 nM 2,3,7,8-tetrachlorodibenzodioxin ([[ TCDD ]]), the most potent activator of AhR.


<< CYP1A1 >> and CYP1A2 mRNAs were also increased by [[ pelargonidin ]] in three primary human hepatocytes cultures (approximately 5% of TCDD potency) and the increase in CYP1A1 protein in HepG2 and LS174T cells was comparable to the increase in catalytic activity of CYP1A1 enzyme.


CYP1A1 and << CYP1A2 >> mRNAs were also increased by [[ pelargonidin ]] in three primary human hepatocytes cultures (approximately 5% of TCDD potency) and the increase in CYP1A1 protein in HepG2 and LS174T cells was comparable to the increase in catalytic activity of CYP1A1 enzyme.


CYP1A1 and CYP1A2 mRNAs were also increased by << pelargonidin >> in three primary human hepatocytes cultures (approximately 5% of TCDD potency) and the increase in [[ CYP1A1 ]] protein in HepG2 and LS174T cells was comparable to the increase in catalytic activity of CYP1A1 enzyme.


CYP1A1 and CYP1A2 mRNAs were also increased by << pelargonidin >> in three primary human hepatocytes cultures (approximately 5% of TCDD potency) and the increase in CYP1A1 protein in HepG2 and LS174T cells was comparable to the increase in catalytic activity of [[ CYP1A1 ]] enzyme.


<< CYP1A1 >> and CYP1A2 mRNAs were also increased by pelargonidin in three primary human hepatocytes cultures (approximately 5% of [[ TCDD ]] potency) and the increase in CYP1A1 protein in HepG2 and LS174T cells was comparable to the increase in catalytic activity of CYP1A1 enzyme.


CYP1A1 and << CYP1A2 >> mRNAs were also increased by pelargonidin in three primary human hepatocytes cultures (approximately 5% of [[ TCDD ]] potency) and the increase in CYP1A1 protein in HepG2 and LS174T cells was comparable to the increase in catalytic activity of CYP1A1 enzyme.


CYP1A1 and CYP1A2 mRNAs were also increased by pelargonidin in three primary human hepatocytes cultures (approximately 5% of << TCDD >> potency) and the increase in [[ CYP1A1 ]] protein in HepG2 and LS174T cells was comparable to the increase in catalytic activity of CYP1A1 enzyme.


CYP1A1 and CYP1A2 mRNAs were also increased by pelargonidin in three primary human hepatocytes cultures (approximately 5% of << TCDD >> potency) and the increase in CYP1A1 protein in HepG2 and LS174T cells was comparable to the increase in catalytic activity of [[ CYP1A1 ]] enzyme.


Enzyme kinetic analyses using human liver microsomes revealed inhibition of << CYP1A1 >> activity by [[ delphinidin ]] (IC50 78 μM) and pelargonidin (IC50 33 μM).


Enzyme kinetic analyses using human liver microsomes revealed inhibition of << CYP1A1 >> activity by delphinidin (IC50 78 μM) and [[ pelargonidin ]] (IC50 33 μM).


Overall, although most anthocyanidins had no effects on AhR-CYP1A1 signaling, << pelargonidin >> can bind to and activate the [[ AhR ]] and AhR-dependent gene expression, and pelargonidin and delphinidin inhibit the CYP1A1 catalytic activity.


Overall, although most anthocyanidins had no effects on AhR-CYP1A1 signaling, pelargonidin can bind to and activate the AhR and AhR-dependent gene expression, and << pelargonidin >> and delphinidin inhibit the [[ CYP1A1 ]] catalytic activity.


Overall, although most anthocyanidins had no effects on AhR-CYP1A1 signaling, pelargonidin can bind to and activate the AhR and AhR-dependent gene expression, and pelargonidin and << delphinidin >> inhibit the [[ CYP1A1 ]] catalytic activity.


In HEK-293 cells stably transfected with this receptor, << serotonin >> elicits a potent stimulation of [[ adenylyl cyclase ]] activity, which is blocked by antipsychotic and antidepressant drugs.


A head-to-head comparison between insulin detemir and NPH insulin in women with type 1 diabetes showed that while foetal outcomes did not differ, fasting plasma << glucose >> improved with [[ insulin ]] detemir without an increased incidence of hypoglycaemia.


OBJECTIVE: The aim was to test whether the common deletion [T/-] in the promoter of << FADS2 >> affects the [[ PUFA ]] biosynthetic pathway and consequently modifies the effect of alpha-linolenic acid (ALA) on myocardial infarction (MI).


OBJECTIVE: The aim was to test whether the common deletion [T/-] in the promoter of << FADS2 >> affects the PUFA biosynthetic pathway and consequently modifies the effect of [[ alpha-linolenic acid ]] (ALA) on myocardial infarction (MI).


OBJECTIVE: The aim was to test whether the common deletion [T/-] in the promoter of << FADS2 >> affects the PUFA biosynthetic pathway and consequently modifies the effect of alpha-linolenic acid ([[ ALA ]]) on myocardial infarction (MI).


We evaluated the effects of << angiotensin II >> and an angiotensin-converting enzyme inhibitor ([[ cilazapril ]]) on nerve blood flow (NBF) and electrophysiology in control and diabetic rats.


We evaluated the effects of angiotensin II and an << angiotensin-converting enzyme >> inhibitor ([[ cilazapril ]]) on nerve blood flow (NBF) and electrophysiology in control and diabetic rats.


We topically applied the nitric oxide synthase (<< NOS >>) inhibitor, [[ NG-nitro-L-arginine ]], on sciatic nerve and observed reduced inhibition of NBF in EDN, which was correctable with a cilazapril diet.


We topically applied the << nitric oxide synthase >> (NOS) inhibitor, [[ NG-nitro-L-arginine ]], on sciatic nerve and observed reduced inhibition of NBF in EDN, which was correctable with a cilazapril diet.


<< Cadmium >> activates [[ NADPH oxidase ]].


However, after 12h << CdCl2 >> treatment, cell viability diminished in 50%, accompanied by a drastic decrease of metallothionein-II production, and an increase in [[ p53 ]] activation and the pro-apoptotic protein Bax.


However, after 12h << CdCl2 >> treatment, cell viability diminished in 50%, accompanied by a drastic decrease of metallothionein-II production, and an increase in p53 activation and the pro-apoptotic protein [[ Bax ]].


However, after 12h << CdCl2 >> treatment, cell viability diminished in 50%, accompanied by a drastic decrease of [[ metallothionein-II ]] production, and an increase in p53 activation and the pro-apoptotic protein Bax.


The inhibitory effect of << ginseng saponins >> on the stress-induced plasma [[ interleukin-6 ]] level in mice.


Ginseng total << saponins >>, ginsenosides Rb2, Rg1 and Rd administered intraperitoneally attenuated the immobilization stress-induced increase in plasma [[ IL-6 ]] level.


Ginseng total saponins, << ginsenosides Rb2, Rg1 and Rd >> administered intraperitoneally attenuated the immobilization stress-induced increase in plasma [[ IL-6 ]] level.


Ginsenosides Rb2, Rd and Rg1 significantly decreased << norepinephrine >> and/or epinephrine-induced increase of [[ IL-6 ]] level in macrophage cell line (RAW 264.7).


Ginsenosides Rb2, Rd and Rg1 significantly decreased norepinephrine and/or << epinephrine >>-induced increase of [[ IL-6 ]] level in macrophage cell line (RAW 264.7).


<< Ginsenosides Rb2, Rd and Rg1 >> significantly decreased norepinephrine and/or epinephrine-induced increase of [[ IL-6 ]] level in macrophage cell line (RAW 264.7).


Thus, it can be suggested that the inhibitory action of ginseng saponins against the immobilization stress-induced increase of plasma IL-6 level would be in periphery; at least in part, mediated by blocking norepinephrine- and/or << epinephrine >>-induced increase of [[ IL-6 ]] level in macrophage rather than in the brain.


Thus, it can be suggested that the inhibitory action of ginseng saponins against the immobilization stress-induced increase of plasma IL-6 level would be in periphery; at least in part, mediated by blocking << norepinephrine >>- and/or epinephrine-induced increase of [[ IL-6 ]] level in macrophage rather than in the brain.


Thus, it can be suggested that the inhibitory action of << ginseng saponins >> against the immobilization stress-induced increase of plasma [[ IL-6 ]] level would be in periphery; at least in part, mediated by blocking norepinephrine- and/or epinephrine-induced increase of IL-6 level in macrophage rather than in the brain.


Thus, it can be suggested that the inhibitory action of << ginseng saponins >> against the immobilization stress-induced increase of plasma IL-6 level would be in periphery; at least in part, mediated by blocking norepinephrine- and/or epinephrine-induced increase of [[ IL-6 ]] level in macrophage rather than in the brain.


Sitagliptin. << Sitagliptin >>, an oral dipeptidyl peptidase-4 (DPP-4) inhibitor, improves glycaemic control by inhibiting DPP-4 inactivation of the [[ incretin hormones ]] glucagon-like peptide-1 and glucose-dependent insulinotropic polypeptide.


Sitagliptin. << Sitagliptin >>, an oral dipeptidyl peptidase-4 (DPP-4) inhibitor, improves glycaemic control by inhibiting DPP-4 inactivation of the incretin hormones [[ glucagon-like peptide-1 ]] and glucose-dependent insulinotropic polypeptide.


Sitagliptin. << Sitagliptin >>, an oral dipeptidyl peptidase-4 (DPP-4) inhibitor, improves glycaemic control by inhibiting DPP-4 inactivation of the incretin hormones glucagon-like peptide-1 and [[ glucose-dependent insulinotropic polypeptide ]].


Sitagliptin. << Sitagliptin >>, an oral dipeptidyl peptidase-4 (DPP-4) inhibitor, improves glycaemic control by inhibiting [[ DPP-4 ]] inactivation of the incretin hormones glucagon-like peptide-1 and glucose-dependent insulinotropic polypeptide.


Sitagliptin. << Sitagliptin >>, an oral [[ dipeptidyl peptidase-4 ]] (DPP-4) inhibitor, improves glycaemic control by inhibiting DPP-4 inactivation of the incretin hormones glucagon-like peptide-1 and glucose-dependent insulinotropic polypeptide.


Sitagliptin. << Sitagliptin >>, an oral dipeptidyl peptidase-4 ([[ DPP-4 ]]) inhibitor, improves glycaemic control by inhibiting DPP-4 inactivation of the incretin hormones glucagon-like peptide-1 and glucose-dependent insulinotropic polypeptide.


Improvements from baseline in mean << glycosylated haemoglobin >> (HbA(1c)) were significantly greater with [[ sitagliptin ]] monotherapy than with placebo in patients with type 2 diabetes.


Improvements from baseline in mean glycosylated haemoglobin (<< HbA(1c) >>) were significantly greater with [[ sitagliptin ]] monotherapy than with placebo in patients with type 2 diabetes.


As add-on therapy in patients with suboptimal glycaemic control despite oral antihyperglycaemic treatment, << sitagliptin >> improved [[ HbA(1c) ]] to a significantly greater extent than placebo when added to metformin or pioglitazone and was noninferior to glipizide when added to metformin.


As add-on therapy in patients with suboptimal glycaemic control despite oral antihyperglycaemic treatment, sitagliptin improved << HbA(1c) >> to a significantly greater extent than placebo when added to [[ metformin ]] or pioglitazone and was noninferior to glipizide when added to metformin.


As add-on therapy in patients with suboptimal glycaemic control despite oral antihyperglycaemic treatment, sitagliptin improved << HbA(1c) >> to a significantly greater extent than placebo when added to metformin or [[ pioglitazone ]] and was noninferior to glipizide when added to metformin.


As add-on therapy in patients with suboptimal glycaemic control despite oral antihyperglycaemic treatment, sitagliptin improved << HbA(1c) >> to a significantly greater extent than placebo when added to metformin or pioglitazone and was noninferior to glipizide when added to [[ metformin ]].


In addition, pretreatment with << Z-Val-Ala-Asp-fluoromethylketone >> (Z-VAD-fmk), a broad spectrum of [[ caspase ]] inhibitor, could not rescue apoptotic cells from ClpP toxicity.


In addition, pretreatment with Z-Val-Ala-Asp-fluoromethylketone (<< Z-VAD-fmk >>), a broad spectrum of [[ caspase ]] inhibitor, could not rescue apoptotic cells from ClpP toxicity.


<< Orlistat >> is a new inhibitor of [[ pancreatic lipase ]] enzyme.


In the long term, << orlistat >> has been shown to be more effective than placebo in reducing body weight and serum total and [[ low-density lipoprotein ]] cholesterol levels.


<< Genistin >> decreased [[ myosin light chain kinase ]] (MLCK) protein contents and MLCK mRNA expression in IJS, and inhibited both phosphorylation and Mg(2+)-ATPase activity of purified myosin, implicating that the decrease of MLCK contents and inhibition of MLCK activity are involved in the genistin-induced inhibitory effects.


<< Genistin >> decreased myosin light chain kinase ([[ MLCK ]]) protein contents and MLCK mRNA expression in IJS, and inhibited both phosphorylation and Mg(2+)-ATPase activity of purified myosin, implicating that the decrease of MLCK contents and inhibition of MLCK activity are involved in the genistin-induced inhibitory effects.


<< Genistin >> decreased myosin light chain kinase (MLCK) protein contents and [[ MLCK ]] mRNA expression in IJS, and inhibited both phosphorylation and Mg(2+)-ATPase activity of purified myosin, implicating that the decrease of MLCK contents and inhibition of MLCK activity are involved in the genistin-induced inhibitory effects.


Genistin decreased myosin light chain kinase (MLCK) protein contents and MLCK mRNA expression in IJS, and inhibited both phosphorylation and Mg(2+)-ATPase activity of purified myosin, implicating that the decrease of << MLCK >> contents and inhibition of MLCK activity are involved in the [[ genistin ]]-induced inhibitory effects.


<< Genistin >> decreased myosin light chain kinase (MLCK) protein contents and MLCK mRNA expression in IJS, and inhibited both phosphorylation and Mg(2+)-[[ ATPase ]] activity of purified myosin, implicating that the decrease of MLCK contents and inhibition of MLCK activity are involved in the genistin-induced inhibitory effects.


Genistin decreased myosin light chain kinase (MLCK) protein contents and MLCK mRNA expression in IJS, and inhibited both phosphorylation and Mg(2+)-ATPase activity of purified myosin, implicating that the decrease of MLCK contents and inhibition of << MLCK >> activity are involved in the [[ genistin ]]-induced inhibitory effects.


It was found that expression of << Sim2 >> protein in cortical neurons was increased in [[ streptozotocin ]]-induced diabetes mellitus rat model.


Moreover, << curcumin >> alleviated [[ Sim2 ]] expression, and reversely raised Drebrin expression in neurons treated with hyperglycaemia.


Moreover, << curcumin >> alleviated Sim2 expression, and reversely raised [[ Drebrin ]] expression in neurons treated with hyperglycaemia.


Polymorphisms in dopamine transporter (<< SLC6A3 >>) are associated with stimulant effects of [[ D-amphetamine ]]: an exploratory pharmacogenetic study using healthy volunteers.


Polymorphisms in << dopamine transporter >> (SLC6A3) are associated with stimulant effects of [[ D-amphetamine ]]: an exploratory pharmacogenetic study using healthy volunteers.


Endothelium-dependent relaxations, nitric oxide (NO) and endothelium derived hyperpolarizing factor (EDHF)-type, were studied in rabbit iliac artery and aortic rings using the G protein-coupled receptor agonist acetylcholine (ACh) and by << cyclopiazonic acid >> (CPA), which promotes store-operated Ca(2+) entry by inhibiting the endothelial [[ SERCA ]] pump.


Endothelium-dependent relaxations, nitric oxide (NO) and endothelium derived hyperpolarizing factor (EDHF)-type, were studied in rabbit iliac artery and aortic rings using the G protein-coupled receptor agonist acetylcholine (ACh) and by cyclopiazonic acid (<< CPA >>), which promotes store-operated Ca(2+) entry by inhibiting the endothelial [[ SERCA ]] pump.


Endothelium-dependent relaxations, nitric oxide (NO) and endothelium derived hyperpolarizing factor (EDHF)-type, were studied in rabbit iliac artery and aortic rings using the << G protein-coupled receptor >> agonist [[ acetylcholine ]] (ACh) and by cyclopiazonic acid (CPA), which promotes store-operated Ca(2+) entry by inhibiting the endothelial SERCA pump.


Endothelium-dependent relaxations, nitric oxide (NO) and endothelium derived hyperpolarizing factor (EDHF)-type, were studied in rabbit iliac artery and aortic rings using the << G protein-coupled receptor >> agonist acetylcholine ([[ ACh ]]) and by cyclopiazonic acid (CPA), which promotes store-operated Ca(2+) entry by inhibiting the endothelial SERCA pump.


Potentiation was prevented by catalase, the catalase/superoxide dismutase mimetic manganese porphyrin and the << NADPH oxidase >> inhibitor [[ apocynin ]].


Our results suggest that arsenite can potentiate EDHF-type relaxations via a mechanism that is dependent on hydrogen peroxide, thus demonstrating that dismutation of the << superoxide >> anion generated by [[ NADPH oxidase ]] can potentially offset loss of NO bioavailability under conditions of reduced eNOS activity.


We isolated partial cDNAs that codified for enzymes implicated in the << anthocyanin >> biosynthesis such as [[ l-phenylalanine ammonia-lyase ]] (PAL) and chalcone synthase (CHS), and an antioxidant enzyme such as ascorbate peroxidase (APX).


We isolated partial cDNAs that codified for enzymes implicated in the << anthocyanin >> biosynthesis such as l-phenylalanine ammonia-lyase ([[ PAL ]]) and chalcone synthase (CHS), and an antioxidant enzyme such as ascorbate peroxidase (APX).


We isolated partial cDNAs that codified for enzymes implicated in the << anthocyanin >> biosynthesis such as l-phenylalanine ammonia-lyase (PAL) and [[ chalcone synthase ]] (CHS), and an antioxidant enzyme such as ascorbate peroxidase (APX).


We isolated partial cDNAs that codified for enzymes implicated in the << anthocyanin >> biosynthesis such as l-phenylalanine ammonia-lyase (PAL) and chalcone synthase ([[ CHS ]]), and an antioxidant enzyme such as ascorbate peroxidase (APX).


We isolated partial cDNAs that codified for enzymes implicated in the << anthocyanin >> biosynthesis such as l-phenylalanine ammonia-lyase (PAL) and chalcone synthase (CHS), and an antioxidant enzyme such as [[ ascorbate peroxidase ]] (APX).


We isolated partial cDNAs that codified for enzymes implicated in the << anthocyanin >> biosynthesis such as l-phenylalanine ammonia-lyase (PAL) and chalcone synthase (CHS), and an antioxidant enzyme such as ascorbate peroxidase ([[ APX ]]).


<< Acetaminophen >> (paracetamol) is a selective [[ cyclooxygenase-2 ]] inhibitor in man.


Acetaminophen (<< paracetamol >>) is a selective [[ cyclooxygenase-2 ]] inhibitor in man.


The fact that << acetaminophen >> acts functionally as a selective [[ COX-2 ]] inhibitor led us to investigate the hypothesis of whether it works via preferential COX-2 blockade.


Ex vivo << COX >> inhibition and pharmacokinetics of [[ acetaminophen ]] were assessed in 5 volunteers receiving single 1000 mg doses orally.


Coagulation-induced << thromboxane B(2) >> and lipopolysaccharide-induced prostaglandin E(2) were measured ex vivo and in vitro in human whole blood as indices of [[ COX-1 ]] and COX-2 activity.


Coagulation-induced thromboxane B(2) and lipopolysaccharide-induced << prostaglandin E(2) >> were measured ex vivo and in vitro in human whole blood as indices of COX-1 and [[ COX-2 ]] activity.


In vitro, << acetaminophen >> elicited a 4.4-fold selectivity toward [[ COX-2 ]] inhibition (IC(50)=113.7 micromol/L for COX-1; IC(50)=25.8 micromol/L for COX-2).


In vitro, << acetaminophen >> elicited a 4.4-fold selectivity toward COX-2 inhibition (IC(50)=113.7 micromol/L for [[ COX-1 ]]; IC(50)=25.8 micromol/L for COX-2).


In vitro, << acetaminophen >> elicited a 4.4-fold selectivity toward COX-2 inhibition (IC(50)=113.7 micromol/L for COX-1; IC(50)=25.8 micromol/L for [[ COX-2 ]]).


<< Acetaminophen >> plasma concentrations remained above the in vitro IC(50) for [[ COX-2 ]] for at least 5 h postadministration.


Ex vivo IC(50) values (<< COX-1 >>: 105.2 micromol/L; COX-2: 26.3 micromol/L) of [[ acetaminophen ]] compared favorably with its in vitro IC(50) values.


Ex vivo IC(50) values (COX-1: 105.2 micromol/L; << COX-2 >>: 26.3 micromol/L) of [[ acetaminophen ]] compared favorably with its in vitro IC(50) values.


In contrast to previous concepts, << acetaminophen >> inhibited [[ COX-2 ]] by more than 80%, i.e., to a degree comparable to nonsteroidal antiinflammatory drugs (NSAIDs) and selective COX-2 inhibitors.


In view of its substantial << COX-2 >> inhibition, recently defined cardiovascular warnings for use of COX-2 inhibitors should also be considered for [[ acetaminophen ]].


OBJECTIVES: The alkaloid << galantamine >> (GAL), which exhibits a combined [[ anticholinesterase ]] and direct parasympathomimetic mechanism of action, is employed in conjunction with therapeutic interventions in the stimulation of central cholinergic transfer in cognitive diseases.


OBJECTIVES: The alkaloid galantamine (<< GAL >>), which exhibits a combined [[ anticholinesterase ]] and direct parasympathomimetic mechanism of action, is employed in conjunction with therapeutic interventions in the stimulation of central cholinergic transfer in cognitive diseases.


RESULTS: Following administration of the highest of the << GAL >> doses used (2.5; 5; 10 mg/kg i.m.), [[ AChE ]] activity decreased mainly in the frontal cortex, hippocampus and hypophysis.


In the interaction of << GAL >> and CAR, [[ AChE ]] inhibition was stronger but without any statistical significance.


<< NaAsO(2) >> increased the mRNA levels of the [[ light and medium subunits of neurofilament ]] and decreased the mRNA levels of tau and tubulin in a dose-dependent manner; no significant effect was found in the mRNA levels of the heavy subunit of neurofilament, microtubule-associated protein 2, or actin.


<< NaAsO(2) >> increased the mRNA levels of the light and medium subunits of neurofilament and decreased the mRNA levels of [[ tau ]] and tubulin in a dose-dependent manner; no significant effect was found in the mRNA levels of the heavy subunit of neurofilament, microtubule-associated protein 2, or actin.


<< NaAsO(2) >> increased the mRNA levels of the light and medium subunits of neurofilament and decreased the mRNA levels of tau and [[ tubulin ]] in a dose-dependent manner; no significant effect was found in the mRNA levels of the heavy subunit of neurofilament, microtubule-associated protein 2, or actin.


A << naloxone-steroid hybrid azine >> with selective and long-acting opioid antagonism at [[ delta receptors ]] in vitro.


Inhibition of << dipeptidyl peptidase-IV >> (DPP-IV) by [[ atorvastatin ]].


Inhibition of dipeptidyl peptidase-IV (<< DPP-IV >>) by [[ atorvastatin ]].


In this report, we show that the hypolipidemic agent << atorvastatin >> is a competitive inhibitor of [[ porcine DPP-IV ]] in vitro, with K(i)=57.8+/-2.3 microM.


These results may have implications in the development of novel << DPP-IV >> inhibitors based on the use of [[ atorvastatin ]] as a lead compound for the treatment of type 2 diabetes.


<< Neoechinulin A >> suppresses [[ amyloid-β ]] oligomer-induced microglia activation and thereby protects PC-12 cells from inflammation-mediated toxicity.


In this study, focus was given to evaluate the ability of << neoechinulin A >>, an indole alkaloid isolated from marine-derived Microsporum sp., to attenuate microglial activation by oligomeric [[ amyloid-β 1-42 ]] (Aβ42).


In this study, focus was given to evaluate the ability of << neoechinulin A >>, an indole alkaloid isolated from marine-derived Microsporum sp., to attenuate microglial activation by oligomeric amyloid-β 1-42 ([[ Aβ42 ]]).


In this study, focus was given to evaluate the ability of neoechinulin A, an << indole >> alkaloid isolated from marine-derived Microsporum sp., to attenuate microglial activation by oligomeric [[ amyloid-β 1-42 ]] (Aβ42).


In this study, focus was given to evaluate the ability of neoechinulin A, an << indole >> alkaloid isolated from marine-derived Microsporum sp., to attenuate microglial activation by oligomeric amyloid-β 1-42 ([[ Aβ42 ]]).


<< Neoechinulin A >> treatment significantly inhibited the generation of reactive oxygen and nitrogen species in [[ Aβ42 ]]-activated BV-2 microglia cells.


In addition, we found that << neoechinulin A >> significantly suppressed the production of neurotoxic inflammatory mediator [[ tumour necrosis factor-α ]] (TNF-α), interleukin-1β (IL-1β), interleukin-6 (IL-6), and prostaglandin E2 (PGE2) in activated BV-2 cells.


In addition, we found that << neoechinulin A >> significantly suppressed the production of neurotoxic inflammatory mediator tumour necrosis factor-α ([[ TNF-α ]]), interleukin-1β (IL-1β), interleukin-6 (IL-6), and prostaglandin E2 (PGE2) in activated BV-2 cells.


In addition, we found that << neoechinulin A >> significantly suppressed the production of neurotoxic inflammatory mediator tumour necrosis factor-α (TNF-α), [[ interleukin-1β ]] (IL-1β), interleukin-6 (IL-6), and prostaglandin E2 (PGE2) in activated BV-2 cells.


In addition, we found that << neoechinulin A >> significantly suppressed the production of neurotoxic inflammatory mediator tumour necrosis factor-α (TNF-α), interleukin-1β ([[ IL-1β ]]), interleukin-6 (IL-6), and prostaglandin E2 (PGE2) in activated BV-2 cells.


In addition, we found that << neoechinulin A >> significantly suppressed the production of neurotoxic inflammatory mediator tumour necrosis factor-α (TNF-α), interleukin-1β (IL-1β), [[ interleukin-6 ]] (IL-6), and prostaglandin E2 (PGE2) in activated BV-2 cells.


In addition, we found that << neoechinulin A >> significantly suppressed the production of neurotoxic inflammatory mediator tumour necrosis factor-α (TNF-α), interleukin-1β (IL-1β), interleukin-6 ([[ IL-6 ]]), and prostaglandin E2 (PGE2) in activated BV-2 cells.


The molecular mechanism studies suggested that << neoechinulin A >> may block the phosphorylation of mitogen-activated protein kinase (MAPK) molecule p38, apoptosis signal-regulating kinase 1 (ASK-1) and nuclear translocation of [[ nuclear factor-κB ]] (NF-κB) p65 and p50 subunits.


The molecular mechanism studies suggested that << neoechinulin A >> may block the phosphorylation of mitogen-activated protein kinase (MAPK) molecule p38, apoptosis signal-regulating kinase 1 (ASK-1) and nuclear translocation of nuclear factor-κB ([[ NF-κB ]]) p65 and p50 subunits.


The molecular mechanism studies suggested that << neoechinulin A >> may block the phosphorylation of mitogen-activated protein kinase (MAPK) molecule p38, apoptosis signal-regulating kinase 1 (ASK-1) and nuclear translocation of nuclear factor-κB (NF-κB) [[ p65 ]] and p50 subunits.


The molecular mechanism studies suggested that << neoechinulin A >> may block the phosphorylation of mitogen-activated protein kinase (MAPK) molecule p38, apoptosis signal-regulating kinase 1 (ASK-1) and nuclear translocation of nuclear factor-κB (NF-κB) p65 and [[ p50 ]] subunits.


The molecular mechanism studies suggested that << neoechinulin A >> may block the phosphorylation of [[ mitogen-activated protein kinase ]] (MAPK) molecule p38, apoptosis signal-regulating kinase 1 (ASK-1) and nuclear translocation of nuclear factor-κB (NF-κB) p65 and p50 subunits.


The molecular mechanism studies suggested that << neoechinulin A >> may block the phosphorylation of mitogen-activated protein kinase ([[ MAPK ]]) molecule p38, apoptosis signal-regulating kinase 1 (ASK-1) and nuclear translocation of nuclear factor-κB (NF-κB) p65 and p50 subunits.


The molecular mechanism studies suggested that << neoechinulin A >> may block the phosphorylation of mitogen-activated protein kinase (MAPK) molecule [[ p38 ]], apoptosis signal-regulating kinase 1 (ASK-1) and nuclear translocation of nuclear factor-κB (NF-κB) p65 and p50 subunits.


The molecular mechanism studies suggested that << neoechinulin A >> may block the phosphorylation of mitogen-activated protein kinase (MAPK) molecule p38, [[ apoptosis signal-regulating kinase 1 ]] (ASK-1) and nuclear translocation of nuclear factor-κB (NF-κB) p65 and p50 subunits.


The molecular mechanism studies suggested that << neoechinulin A >> may block the phosphorylation of mitogen-activated protein kinase (MAPK) molecule p38, apoptosis signal-regulating kinase 1 ([[ ASK-1 ]]) and nuclear translocation of nuclear factor-κB (NF-κB) p65 and p50 subunits.


<< Epi >> increased the activity of the [[ human WNT6 promoter ]] through Cav1-dependent binding of β-catenin to the proximal WNT6 promoter.


<< Epi >> increased the activity of the human WNT6 promoter through Cav1-dependent binding of β-catenin to the proximal [[ WNT6 promoter ]].


<< Epi >> increased both [[ WNT6 ]]/Wnt6 and Cav1 expression in human GC cells and within the tumor area of a murine model of GC (CEA424-SV40 TAg).


<< Epi >> increased both WNT6/[[ Wnt6 ]] and Cav1 expression in human GC cells and within the tumor area of a murine model of GC (CEA424-SV40 TAg).


<< Epi >> increased both WNT6/Wnt6 and [[ Cav1 ]] expression in human GC cells and within the tumor area of a murine model of GC (CEA424-SV40 TAg).


These results showed that << WNT6 >> and Cav1 are upregulated by chemotherapeutics and enhance the resistance of GC cells to [[ anthracycline ]] drugs.


These results showed that WNT6 and << Cav1 >> are upregulated by chemotherapeutics and enhance the resistance of GC cells to [[ anthracycline ]] drugs.


In this study, using reverse transcriptase PCR (RT-PCR) and ELISA, we showed that << TCDD >> up-regulated the expression and secretion of [[ tumor necrosis factor-alpha ]] (TNF-α) in a time-dependent manner in cultured HAPI microglial cells.


In this study, using reverse transcriptase PCR (RT-PCR) and ELISA, we showed that << TCDD >> up-regulated the expression and secretion of tumor necrosis factor-alpha ([[ TNF-α ]]) in a time-dependent manner in cultured HAPI microglial cells.


<< TCDD >> also caused a fast (within 30min as judged by the increase in its mRNA level) activation of [[ cytosolic phospholipase A2 ]] (cPLA2).


<< TCDD >> also caused a fast (within 30min as judged by the increase in its mRNA level) activation of cytosolic phospholipase A2 ([[ cPLA2 ]]).


This initial action was accompanied by up-regulation of << cyclooxygenase-2 >> (COX-2), an important inflammation marker within 1h after [[ TCDD ]] treatment.


This initial action was accompanied by up-regulation of cyclooxygenase-2 (<< COX-2 >>), an important inflammation marker within 1h after [[ TCDD ]] treatment.


Further, << TCDD >> exposure could induce phosphorylation- and ubiquitination-dependent degradation of [[ IкBα ]], and the translocation of NF-κB p65 from the cytosol to the nucleus in this microglial cell line.


Thus, the << NF-κB >> signaling pathway can be activated after [[ TCDD ]] treatment.


However, Ca(2+) blockers also obviously attenuated << NF-κB >> activation and transnuclear transport induced by [[ TCDD ]].


In concert with these results, we highlighted that the secretion of pro-inflammatory << cytokine >> and NF-κB activation induced by [[ TCDD ]] can be mediated by elevation of [Ca(2+)]i in HAPI microglial cells.


In concert with these results, we highlighted that the secretion of pro-inflammatory cytokine and << NF-κB >> activation induced by [[ TCDD ]] can be mediated by elevation of [Ca(2+)]i in HAPI microglial cells.


The ARB << eprosartan >> is a nonbiphenyl nontetrazole [[ angiotensin II type 1 receptor ]] (AT1) antagonist, which acts to decrease total peripheral resistance.


The ARB << eprosartan >> is a nonbiphenyl nontetrazole angiotensin II type 1 receptor ([[ AT1 ]]) antagonist, which acts to decrease total peripheral resistance.


The putative << alpha 1L-adrenoceptor >> antagonist [[ JTH-601 ]], but not the alpha 1B-adrenoceptor antagonist chloroethylclonidine (10 microM) antagonized noradrenaline-induced contractions of SMA.


The putative alpha 1L-adrenoceptor antagonist JTH-601, but not the << alpha 1B-adrenoceptor >> antagonist [[ chloroethylclonidine ]] (10 microM) antagonized noradrenaline-induced contractions of SMA.


The potency of the selective alpha 1D-adrenoceptor antagonist BMY 7378 against noradrenaline (pA2 = 6.16 +/- 0.13) and of the selective alpha 1A-adrenoceptor antagonist RS-17053 against noradrenaline (pKB = 8.35 +/- 0.10) and against the selective << alpha 1A-adrenoceptor >> agonist [[ A-61603 ]] (pKB = 8.40 +/- 0.09) were too low to account for alpha 1D- and alpha 1A-adrenoceptor involvement.


The potency of the selective << alpha 1D-adrenoceptor >> antagonist [[ BMY 7378 ]] against noradrenaline (pA2 = 6.16 +/- 0.13) and of the selective alpha 1A-adrenoceptor antagonist RS-17053 against noradrenaline (pKB = 8.35 +/- 0.10) and against the selective alpha 1A-adrenoceptor agonist A-61603 (pKB = 8.40 +/- 0.09) were too low to account for alpha 1D- and alpha 1A-adrenoceptor involvement.