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[PMID]:26151307
[Au] Autor:Mori A; Namekawa R; Hasebe M; Saito M; Sakamoto K; Nakahara T; Ishii K
[Ad] Endereço:Department of Molecular Pharmacology, Kitasato University School of Pharmaceutical Sciences, 5-9-1 Shirokane, Minato-ku, Tokyo 108-8641, Japan.
[Ti] Título:Involvement of prostaglandin I(2) in nitric oxide-induced vasodilation of retinal arterioles in rats.
[So] Source:Eur J Pharmacol;764:249-55, 2015 Oct 05.
[Is] ISSN:1879-0712
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The soluble guanylyl cyclase/cGMP system plays an important role in the vasodilator response to nitric oxide (NO) in various vascular beds. However, in rat retinal arterioles, the cyclooxygenase-1/cAMP-mediated pathway contributes to the vasodilator effects of NO, although the specific prostanoid involved remains to be elucidated. In the present study, we investigated the role of prostaglandin I2 and its receptor (prostanoid IP receptor) system in NO-induced vasodilation of rat retinal arterioles in vivo. Fundus images were captured using a digital camera that was equipped with a special objective lens. Changes in diameter of retinal arterioles were assessed. The NO donor (±)-(E)-4-ethyl-2-[(E)-hydroxyimino]-5-nitro-3-hexenamide (NOR3) increased the diameter of retinal arterioles but decreased systemic blood pressure in a dose-dependent manner. Treatment of rats with indomethacin, a non-selective cyclooxygenase inhibitor, markedly attenuated the retinal vasodilator, but not depressor responses to NOR3. The prostanoid IP receptor antagonist 4,5-dihydro-N-[4-[[4-(1-methylethoxy)phenyl]methyl]phenyl]-1H-imadazol-2-amine (CAY10441), and the prostaglandin I2 synthase inhibitor 9α,11α-azoprosta-5Z,13E-dien-1-oic acid (U-51605), both showed similar preventive effects against the NOR3-induced retinal vasodilator response. Neither CAY10441 nor U-51605 showed any significant effects on the depressor response to NOR3. NOR3 enhanced the release of prostaglandin I2 from cultured human retinal microvascular endothelial cells and the NOR3-induced prostaglandin I2 release was almost completely abolished by the cyclooxygenase-1 inhibitor SC-560, but not by the cyclooxygenase-2 inhibitor NS-398. However, NOR3 did not increase the release of prostaglandin I2 from human intestinal microvascular endothelial cells. These results suggest that NO exerts its dilatory effect via cyclooxygenase-1/prostaglandin I2/prostanoid IP receptor signaling mechanisms in the retinal vasculature.
[Mh] Termos MeSH primário: Arteríolas/fisiologia
Epoprostenol/fisiologia
Vasos Retinianos/fisiologia
[Mh] Termos MeSH secundário: Animais
Arteríolas/efeitos dos fármacos
Compostos de Benzil/farmacologia
Células Cultivadas
Ciclo-Oxigenase 1/fisiologia
Inibidores de Ciclo-Oxigenase/farmacologia
Células Endoteliais/metabolismo
Seres Humanos
Hidroxilaminas/farmacologia
Imidazóis/farmacologia
Masculino
Óxido Nítrico/fisiologia
Doadores de Óxido Nítrico/farmacologia
Nitrobenzenos/farmacologia
Prostaglandinas H/farmacologia
Pirazóis/farmacologia
Ratos Wistar
Receptores de Prostaglandina/antagonistas & inibidores
Receptores de Prostaglandina/fisiologia
Vasos Retinianos/efeitos dos fármacos
Sulfonamidas/farmacologia
Vasodilatação/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 ((2-(4-(4-isopropoxybenzyl)-phenylamino) imidazoline)); 0 (Benzyl Compounds); 0 (Cyclooxygenase Inhibitors); 0 (Hydroxylamines); 0 (Imidazoles); 0 (Nitric Oxide Donors); 0 (Nitrobenzenes); 0 (Prostaglandins H); 0 (Pyrazoles); 0 (Receptors, Prostaglandin); 0 (SC 560); 0 (Sulfonamides); 0 (ethyl-2-(hydroxyamino)-5-nitro-3-hexenamide); 123653-11-2 (N-(2-cyclohexyloxy-4-nitrophenyl)methanesulfonamide); 31C4KY9ESH (Nitric Oxide); 64192-56-9 (azo analog I); DCR9Z582X0 (Epoprostenol); EC 1.14.99.1 (Cyclooxygenase 1)
[Em] Mês de entrada:1607
[Cu] Atualização por classe:151009
[Lr] Data última revisão:
151009
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150708
[St] Status:MEDLINE


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[PMID]:22442685
[Au] Autor:Schröder R; Xue L; Konya V; Martini L; Kampitsch N; Whistler JL; Ulven T; Heinemann A; Pettipher R; Kostenis E
[Ad] Endereço:Molecular-, Cellular- and Pharmacobiology Section, Institute for Pharmaceutical Biology, University of Bonn, Bonn, Germany.
[Ti] Título:PGH1, the precursor for the anti-inflammatory prostaglandins of the 1-series, is a potent activator of the pro-inflammatory receptor CRTH2/DP2.
[So] Source:PLoS One;7(3):e33329, 2012.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Prostaglandin H(1) (PGH(1)) is the cyclo-oxygenase metabolite of dihomo-γ-linolenic acid (DGLA) and the precursor for the 1-series of prostaglandins which are often viewed as "anti-inflammatory". Herein we present evidence that PGH(1) is a potent activator of the pro-inflammatory PGD(2) receptor CRTH2, an attractive therapeutic target to treat allergic diseases such as asthma and atopic dermatitis. Non-invasive, real time dynamic mass redistribution analysis of living human CRTH2 transfectants and Ca(2+) flux studies reveal that PGH(1) activates CRTH2 as PGH(2), PGD(2) or PGD(1) do. The PGH(1) precursor DGLA and the other PGH(1) metabolites did not display such effect. PGH(1) specifically internalizes CRTH2 in stable CRTH2 transfectants as assessed by antibody feeding assays. Physiological relevance of CRTH2 ligation by PGH(1) is demonstrated in several primary human hematopoietic lineages, which endogenously express CRTH2: PGH(1) mediates migration of and Ca(2+) flux in Th2 lymphocytes, shape change of eosinophils, and their adhesion to human pulmonary microvascular endothelial cells under physiological flow conditions. All these effects are abrogated in the presence of the CRTH2 specific antagonist TM30089. Together, our results identify PGH(1) as an important lipid intermediate and novel CRTH2 agonist which may trigger CRTH2 activation in vivo in the absence of functional prostaglandin D synthase.
[Mh] Termos MeSH primário: Células Endoteliais/metabolismo
Prostaglandinas H/metabolismo
Receptores Imunológicos/agonistas
Receptores Imunológicos/metabolismo
Receptores de Prostaglandina/agonistas
Receptores de Prostaglandina/metabolismo
Células Th2/metabolismo
[Mh] Termos MeSH secundário: Sinalização do Cálcio/genética
Feminino
Células HEK293
Seres Humanos
Hipersensibilidade/tratamento farmacológico
Hipersensibilidade/genética
Hipersensibilidade/metabolismo
Oxirredutases Intramoleculares/genética
Oxirredutases Intramoleculares/metabolismo
Lipocalinas/genética
Lipocalinas/metabolismo
Masculino
Prostaglandinas H/genética
Receptores Imunológicos/genética
Receptores de Prostaglandina/genética
[Pt] Tipo de publicação:CLINICAL TRIAL; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Lipocalins); 0 (Prostaglandins H); 0 (Receptors, Immunologic); 0 (Receptors, Prostaglandin); 0 (prostaglandin D2 receptor); EC 5.3.- (Intramolecular Oxidoreductases); EC 5.3.99.2 (prostaglandin R2 D-isomerase)
[Em] Mês de entrada:1207
[Cu] Atualização por classe:150225
[Lr] Data última revisão:
150225
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120324
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0033329


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[PMID]:22159626
[Au] Autor:Ma D; Assumpção TC; Li Y; Andersen JF; Ribeiro J; Francischetti IM
[Ad] Endereço:Section of Vector Biology, Laboratory of Malaria and Vector Research, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Rockville, Maryland 20852, USA.
[Ti] Título:Triplatin, a platelet aggregation inhibitor from the salivary gland of the triatomine vector of Chagas disease, binds to TXA(2) but does not interact with glycoprotein PVI.
[So] Source:Thromb Haemost;107(1):111-23, 2012 Jan.
[Is] ISSN:0340-6245
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Salivary glands from haematophagous animals express a notable diversity of negative modulators of platelet function. Triplatin is an inhibitor of collagen-induced platelet aggregation which has been described as an antagonist of glycoprotein VI (GPVI). Because triplatin displays sequence homology to members of the lipocalin family of proteins, we investigated whether triplatin mechanism of action could be explained by interaction with pro-haemostatic prostaglandins. Our results demonstrate that triplatin inhibits platelet aggregation induced by low doses of collagen, thromboxane A2 (TXA(2)) mimetic (U46619), and arachidonic acid (AA). On the other hand, it does not inhibit platelet aggregation by convulxin, PMA, or low-dose ADP. Isothermal titration calorimetry (ITC) revealed that triplatin binds AA, cTXA(2), TXB(2), U46619 or prostaglandin (PG)H(2) mimetic (U51605). Consistent with its ligand specificity, triplatin induces relaxation of rat aorta contracted with U46619. Triplatin also interacts with PGF(2α) and PGJ(2), but not with leukotrienes, AA or biogenic amines. Surface plasmon resonance experiments failed to demonstrate interaction of triplatin with GPVI; it also did to inhibit platelet adhesion to fibrillar or soluble collagen. Because triplatin displays sequence similarity to apolipoprotein D (ApoD) - a lipocalin associated with high-density lipoprotein, ApoD was tested as a putative TXA(2)-binding molecule. ITC failed to demonstrate binding of ApoD to all prostanoids described above, or to AA. Furthermore, ApoD was devoid of inhibitory properties towards platelets activation by AA, collagen, or U46619. In conclusion, triplatin mechanism of action has been elucidated without ambiguity as a novel TXA(2)- and PGF(2α)- binding protein. It conceivably blocks platelet aggregation and vasoconstriction, thus contributing to successful blood feeding at the vector-host interface.
[Mh] Termos MeSH primário: Inibidores da Agregação de Plaquetas/farmacologia
Glicoproteínas da Membrana de Plaquetas/química
Glândulas Salivares/metabolismo
Proteínas e Peptídeos Salivares/uso terapêutico
Tromboxano A2/metabolismo
[Mh] Termos MeSH secundário: Ácido 15-Hidroxi-11 alfa,9 alfa-(epoximetano)prosta-5,13-dienoico/farmacologia
Aminas/química
Animais
Ácido Araquidônico/metabolismo
Cavalos
Seres Humanos
Ligantes
Modelos Biológicos
Agregação Plaquetária/efeitos dos fármacos
Prostaglandinas H/farmacologia
Ligação Proteica
Serpentes
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., INTRAMURAL
[Nm] Nome de substância:
0 (Amines); 0 (Ligands); 0 (Platelet Aggregation Inhibitors); 0 (Platelet Membrane Glycoproteins); 0 (Prostaglandins H); 0 (Salivary Proteins and Peptides); 0 (platelet membrane glycoprotein VI); 0 (triplatin, Triatoma infestans); 27YG812J1I (Arachidonic Acid); 57576-52-0 (Thromboxane A2); 64192-56-9 (azo analog I); 76898-47-0 (15-Hydroxy-11 alpha,9 alpha-(epoxymethano)prosta-5,13-dienoic Acid)
[Em] Mês de entrada:1205
[Cu] Atualização por classe:161025
[Lr] Data última revisão:
161025
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:111214
[St] Status:MEDLINE
[do] DOI:10.1160/TH11-10-0685


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[PMID]:21511721
[Au] Autor:Kang HJ; Hwang SJ; Yoon JA; Jun JH; Lim HJ; Yoon TK; Song H
[Ad] Endereço:Laboratory of Reproductive Biology & Infertility, Cheil General Hospital & Women's Healthcare Center, Kwandong University College of Medicine, Seoul, Korea.
[Ti] Título:Activation of peroxisome proliferators-activated receptor δ (PPARδ) promotes blastocyst hatching in mice.
[So] Source:Mol Hum Reprod;17(10):653-60, 2011 Oct.
[Is] ISSN:1460-2407
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Prostaglandins participate in a variety of female reproductive processes, including ovulation, fertilization, embryo implantation and parturition. In particular, maternal prostacyclin (PGI(2)) is critical for embryo implantation and the action of PGI(2) is not mediated via its G-protein-coupled membrane receptor, IP, but its nuclear receptor, peroxisome-proliferator-activated receptor δ (PPARδ). Recently, several studies have shown that PGI(2) enhances blastocyst development and/or hatching rate in vitro, and subsequently implantation and live birth rates in mice. However, the mechanism by which PGI(2) improves preimplantation embryo development in vitro remains unclear. Using molecular, pharmacologic and genetic approaches, we show that PGI(2)-induced PPARδ activation accelerates blastocyst hatching in mice. mRNAs for PPARδ, retinoid X receptor (heterodimeric partners of PPARδ) and PGI(2) synthase (PGIS) are temporally induced after zygotic gene activation, and their expression reaches maximum levels at the blastocyst stage, suggesting that functional complex of PPARδ can be formed in the blastocyst. Carbaprostacyclin (a stable analogue of PGI(2)) and GW501516 (a PPARδ selective agonist) significantly accelerated blastocyst hatching but did not increase total cell number of cultured blastocysts. Whereas U51605 (a PGIS inhibitor) interfered with blastocyst hatching, GW501516 restored U51605-induced retarded hatching. In contrast to the improvement of blastocyst hatching by PPARδ agonists, PPAR antagonists significantly inhibited blastocyst hatching. Furthermore, deletion of PPARδ at early stages of preimplantation mouse embryos caused delay of blastocyst hatching, but did not impair blastocyst development. Taken together, PGI(2)-induced PPARδ activation accelerates blastocyst hatching in mice.
[Mh] Termos MeSH primário: Blastocisto/fisiologia
Implantação do Embrião
Desenvolvimento Embrionário
PPAR delta/metabolismo
[Mh] Termos MeSH secundário: Anilidas/farmacologia
Animais
Benzamidas/farmacologia
Inibidores das Enzimas do Citocromo P-450
Sistema Enzimático do Citocromo P-450/biossíntese
Sistema Enzimático do Citocromo P-450/genética
Implantação do Embrião/efeitos dos fármacos
Desenvolvimento Embrionário/efeitos dos fármacos
Epoprostenol/análogos & derivados
Epoprostenol/metabolismo
Epoprostenol/farmacologia
Feminino
Oxirredutases Intramoleculares/antagonistas & inibidores
Oxirredutases Intramoleculares/biossíntese
Oxirredutases Intramoleculares/genética
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Endogâmicos ICR
Camundongos Knockout
PPAR delta/antagonistas & inibidores
Gravidez
Prostaglandinas H/farmacologia
Piridinas/farmacologia
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Receptores X Retinoide/biossíntese
Receptores X Retinoide/genética
Tiazóis/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (2-chloro-5-nitrobenzanilide); 0 (Anilides); 0 (Benzamides); 0 (Cytochrome P-450 Enzyme Inhibitors); 0 (GW 501516); 0 (PPAR delta); 0 (Prostaglandins H); 0 (Pyridines); 0 (RNA, Messenger); 0 (Retinoid X Receptors); 0 (T 0070907); 0 (Thiazoles); 64192-56-9 (azo analog I); 69552-46-1 (carboprostacyclin); 9035-51-2 (Cytochrome P-450 Enzyme System); DCR9Z582X0 (Epoprostenol); EC 5.3.- (Intramolecular Oxidoreductases); EC 5.3.99.4 (prostacyclin synthetase)
[Em] Mês de entrada:1201
[Cu] Atualização por classe:141120
[Lr] Data última revisão:
141120
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:110423
[St] Status:MEDLINE
[do] DOI:10.1093/molehr/gar030


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[PMID]:20041722
[Au] Autor:Zagol-Ikapitte I; Amarnath V; Bala M; Roberts LJ; Oates JA; Boutaud O
[Ad] Endereço:Departments of Pharmacology, Pathology, and Medicine, Vanderbilt University, Nashville, Tennessee 37232-6602, USA.
[Ti] Título:Characterization of scavengers of gamma-ketoaldehydes that do not inhibit prostaglandin biosynthesis.
[So] Source:Chem Res Toxicol;23(1):240-50, 2010 Jan.
[Is] ISSN:1520-5010
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Expression of cyclooxygenase-2 (COX-2) is associated with the development of many pathologic conditions. The product of COX-2, prostaglandin H(2) (PGH(2)), can spontaneously rearrange to form reactive gamma-ketoaldehydes called levuglandins (LGs). This gamma-ketoaldehyde structure confers a high degree of reactivity on the LGs, which rapidly form covalent adducts with primary amines of protein residues. Formation of LG adducts of proteins has been demonstrated in pathologic conditions (e.g., increased levels in the hippocampus in Alzheimer's disease) and during physiologic function (platelet activation). On the basis of knowledge that lipid modification of proteins is known to cause their translocation and to alter their function, we hypothesize that modification of proteins by LG could have functional consequences. Testing this hypothesis requires an experimental approach that discriminates between the effects of protein modification by LG and the effects of cyclooxygenase-derived prostanoids acting through their G-protein coupled receptors. To achieve this goal, we have synthesized and evaluated a series of scavengers that react with LG with a potency more than 2 orders of magnitude greater than that with the epsilon-amine of lysine. A subset of these scavengers are shown to block the formation of LG adducts of proteins in cells without inhibiting the catalytic activity of the cyclooxygenases. Ten of these selective scavengers did not produce cytotoxicity. These results demonstrate that small molecules can scavenge LGs in cells without interfering with the formation of prostaglandins. They also provide a working hypothesis for the development of pharmacologic agents that could be used in experimental animals in vivo to assess the pathophysiological contribution of levuglandins in diseases associated with cyclooxygenase up-regulation.
[Mh] Termos MeSH primário: Aminas/química
Prostaglandinas H/química
Prostaglandinas/biossíntese
[Mh] Termos MeSH secundário: Aminas/síntese química
Plaquetas/metabolismo
Linhagem Celular Tumoral
Ciclo-Oxigenase 2/química
Ciclo-Oxigenase 2/metabolismo
Células Hep G2
Seres Humanos
Prostaglandinas H/metabolismo
Piridoxamina/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Amines); 0 (Prostaglandins); 0 (Prostaglandins H); 6466NM3W93 (Pyridoxamine); EC 1.14.99.1 (Cyclooxygenase 2)
[Em] Mês de entrada:1003
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:100101
[St] Status:MEDLINE
[do] DOI:10.1021/tx900407a


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[PMID]:18771909
[Au] Autor:Pakrasi PL; Jain AK
[Ad] Endereço:Embryo Physiology Laboratory, Center of Advanced Study, Department of Zoology, Banaras Hindu University, Varanasi 221005, India. pakrasi@bhu.ac.in
[Ti] Título:Cyclooxygenase-2-derived endogenous prostacyclin reduces apoptosis and enhances embryo viability in mouse.
[So] Source:Prostaglandins Leukot Essent Fatty Acids;79(1-2):27-33, 2008 Jul-Aug.
[Is] ISSN:0952-3278
[Cp] País de publicação:Scotland
[La] Idioma:eng
[Ab] Resumo:The role of prostaglandins (PGs) in apoptosis in preimplantation mice embryo development is reported in this study. It is known that apoptosis plays a very important role in normal mice embryo development. Very few reports are available on this subject. Embryos (6-8 cells) were cultured in the presence of a selective cyclooxygenase (COX)1 inhibitor (SC560), a selective COX2 inhibitor (NS398) and a selective prostacyclin synthase (PGIS) inhibitor (U51605) in a 48-h culture. In another experiment, culture media were supplemented with prostaglandin E2 (PGE2) and prostaglandin I2 (PGI2 or prostacyclin) analogues. The apoptosis was evaluated by detection of active caspase-3. It was strongly detected in the presence of selective COX-2 and PGIS inhibitors, which can be decreased by a PGI2 analogue. In our embryo transfer experiment, the implantation rate decreased with exposure to either the COX2 or the PGIS inhibitor which is increased further after PGI2 supplementation. The level of PGI2 is also higher at the 8-16-cell stage, compaction and blastocyst stage than PGE2. All these results indicate that COX2-derived PGI2 plays an important role in preimplantation embryo development and acts as an antiapopetic factor in in vitro culture.
[Mh] Termos MeSH primário: Apoptose/efeitos dos fármacos
Blastocisto/efeitos dos fármacos
Blastocisto/metabolismo
Ciclo-Oxigenase 2/metabolismo
Epoprostenol/fisiologia
Nitrobenzenos/farmacologia
Prostaglandinas H/farmacologia
Pirazóis/farmacologia
Sulfonamidas/farmacologia
[Mh] Termos MeSH secundário: Animais
Blastocisto/citologia
Caspase 3/biossíntese
Caspase 3/metabolismo
Inibidores de Caspase
Ciclo-Oxigenase 2/efeitos dos fármacos
Inibidores das Enzimas do Citocromo P-450
Sistema Enzimático do Citocromo P-450
Técnicas de Cultura Embrionária/métodos
Implantação do Embrião/efeitos dos fármacos
Transferência Embrionária
Desenvolvimento Embrionário/efeitos dos fármacos
Epoprostenol/biossíntese
Feminino
Oxirredutases Intramoleculares/antagonistas & inibidores
Masculino
Camundongos
Camundongos Endogâmicos
Gravidez
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Caspase Inhibitors); 0 (Cytochrome P-450 Enzyme Inhibitors); 0 (Nitrobenzenes); 0 (Prostaglandins H); 0 (Pyrazoles); 0 (SC 560); 0 (Sulfonamides); 123653-11-2 (N-(2-cyclohexyloxy-4-nitrophenyl)methanesulfonamide); 64192-56-9 (azo analog I); 9035-51-2 (Cytochrome P-450 Enzyme System); DCR9Z582X0 (Epoprostenol); EC 1.14.99.1 (Cyclooxygenase 2); EC 3.4.22.- (Casp3 protein, mouse); EC 3.4.22.- (Caspase 3); EC 5.3.- (Intramolecular Oxidoreductases); EC 5.3.99.4 (prostacyclin synthetase)
[Em] Mês de entrada:0812
[Cu] Atualização por classe:151119
[Lr] Data última revisão:
151119
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:080906
[St] Status:MEDLINE
[do] DOI:10.1016/j.plefa.2008.07.006


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[PMID]:18032380
[Au] Autor:Li YC; Chiang CW; Yeh HC; Hsu PY; Whitby FG; Wang LH; Chan NL
[Ad] Endereço:Institute of Biochemistry, College of Life Sciences, National Chung Hsing University, Taichung City 402, Taiwan.
[Ti] Título:Structures of prostacyclin synthase and its complexes with substrate analog and inhibitor reveal a ligand-specific heme conformation change.
[So] Source:J Biol Chem;283(5):2917-26, 2008 Feb 01.
[Is] ISSN:0021-9258
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Prostacyclin synthase (PGIS) is a cytochrome P450 (P450) enzyme that catalyzes production of prostacyclin from prostaglandin H(2). PGIS is unusual in that it catalyzes an isomerization rather than a monooxygenation, which is typical of P450 enzymes. To understand the structural basis for prostacyclin biosynthesis in greater detail, we have determined the crystal structures of ligand-free, inhibitor (minoxidil)-bound and substrate analog U51605-bound PGIS. These structures demonstrate a stereo-specific substrate binding and suggest features of the enzyme that facilitate isomerization. Unlike most microsomal P450s, where large substrate-induced conformational changes take place at the distal side of the heme, conformational changes in PGIS are observed at the proximal side and in the heme itself. The conserved and extensive heme propionate-protein interactions seen in all other P450s, which are largely absent in the ligand-free PGIS, are recovered upon U51605 binding accompanied by water exclusion from the active site. In contrast, when minoxidil binds, the propionate-protein interactions are not recovered and water molecules are largely retained. These findings suggest that PGIS represents a divergent evolution of the P450 family, in which a heme barrier has evolved to ensure strict binding specificity for prostaglandin H(2), leading to a radical-mediated isomerization with high product fidelity. The U51605-bound structure also provides a view of the substrate entrance and product exit channels.
[Mh] Termos MeSH primário: Sistema Enzimático do Citocromo P-450/química
Oxirredutases Intramoleculares/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Clonagem Molecular
Cristalografia por Raios X
Inibidores das Enzimas do Citocromo P-450
Sistema Enzimático do Citocromo P-450/genética
Sistema Enzimático do Citocromo P-450/metabolismo
Inibidores Enzimáticos/farmacologia
Epoprostenol/biossíntese
Heme/química
Oxirredutases Intramoleculares/antagonistas & inibidores
Oxirredutases Intramoleculares/genética
Oxirredutases Intramoleculares/metabolismo
Ligantes
Minoxidil/farmacologia
Modelos Biológicos
Modelos Moleculares
Dados de Sequência Molecular
Prostaglandinas H/metabolismo
Conformação Proteica
Proteínas Recombinantes/antagonistas & inibidores
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Homologia de Sequência de Aminoácidos
Eletricidade Estática
Especificidade por Substrato
Termodinâmica
Peixe-Zebra/genética
Peixe-Zebra/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cytochrome P-450 Enzyme Inhibitors); 0 (Enzyme Inhibitors); 0 (Ligands); 0 (Prostaglandins H); 0 (Recombinant Proteins); 42VZT0U6YR (Heme); 5965120SH1 (Minoxidil); 64192-56-9 (azo analog I); 9035-51-2 (Cytochrome P-450 Enzyme System); DCR9Z582X0 (Epoprostenol); EC 5.3.- (Intramolecular Oxidoreductases); EC 5.3.99.4 (prostacyclin synthetase)
[Em] Mês de entrada:0804
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:071123
[St] Status:MEDLINE


  8 / 639 MEDLINE  
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[PMID]:17328923
[Au] Autor:Pakrasi PL; Jain AK
[Ad] Endereço:Embryo Physiology Laboratory, Department of Zoology, Banaras Hindu University, Varanasi 221005, India. pakrasi@bhu.ac.in
[Ti] Título:Evaluation of cyclooxygenase 2 derived endogenous prostacyclin in mouse preimplantation embryo development in vitro.
[So] Source:Life Sci;80(16):1503-7, 2007 Mar 27.
[Is] ISSN:0024-3205
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Cyclooxygenase (COX) plays an important role in prostaglandin (PG) synthesis and has two isoforms, COX1 and COX2. PGI synthase (PGIS) catalyzes the isomeization of PGH(2) to prostacyclin (PGI(2)). It is reported that COX2 derived PGI2(2) plays a critical role in blastocyst implantation and decidualization and PGI2 mediates its function via PPARdelta receptor. It is also known that cyclooxygenase derived prostaglandins play an important role in mouse blastocyst hatching in vitro. In this study we hypothesized that COX2 derived PGI2 plays an important role in preimplantation embryonic development by increasing the cell number. To examine this hypothesis, 8-cell stage mouse embryos were cultured in the presence of selective inhibitors of COX1 (SC560), COX2 (NS398) and PGIS (U51605) respectively. COX2 and PGIS inhibitor significantly reduced the blastocyst development and presence of PGI2 analogue along with these inhibitors restored the blastocyst development by increasing the total number of embryonic cells. Our immunohistochemical analysis showed that COX1 is expressed at 2-cell, 8-cell, compaction and blastocyst stage whereas COX2 expression starts from eight cell stage embryos. PGIS and PPARdelta expression starts at 2-cell stage of development. Our results suggest that PGI(2) may affect blastomeres number via the so called hypothesis of PPARdelta nuclear receptor in autocrine manner.
[Mh] Termos MeSH primário: Blastocisto/metabolismo
Proliferação Celular/efeitos dos fármacos
Ciclo-Oxigenase 2/metabolismo
Desenvolvimento Embrionário/fisiologia
Epoprostenol/metabolismo
[Mh] Termos MeSH secundário: Animais
Inibidores de Ciclo-Oxigenase/farmacologia
Desenvolvimento Embrionário/efeitos dos fármacos
Epoprostenol/antagonistas & inibidores
Epoprostenol/biossíntese
Imuno-Histoquímica
Camundongos
Nitrobenzenos/farmacologia
Prostaglandinas H/farmacologia
Pirazóis/farmacologia
Sulfonamidas/farmacologia
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cyclooxygenase Inhibitors); 0 (Nitrobenzenes); 0 (Prostaglandins H); 0 (Pyrazoles); 0 (SC 560); 0 (Sulfonamides); 123653-11-2 (N-(2-cyclohexyloxy-4-nitrophenyl)methanesulfonamide); 64192-56-9 (azo analog I); DCR9Z582X0 (Epoprostenol); EC 1.14.99.1 (Cyclooxygenase 2)
[Em] Mês de entrada:0706
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:070303
[St] Status:MEDLINE


  9 / 639 MEDLINE  
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[PMID]:17126320
[Au] Autor:Gluais P; Vanhoutte PM; Félétou M
[Ad] Endereço:Institut de Recherches Servier, 92150 Suresnes, France.
[Ti] Título:Mechanisms underlying ATP-induced endothelium-dependent contractions in the SHR aorta.
[So] Source:Eur J Pharmacol;556(1-3):107-14, 2007 Feb 05.
[Is] ISSN:0014-2999
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:In mature spontaneously hypertensive (SHR) and Wistar-Kyoto (WKY) rats, acetylcholine, the calcium ionophore A 23187 and ATP release endothelium-derived contracting factor (EDCF), cyclooxygenase (COX) derivatives that activate thromboxane-endoperoxide (TP) receptors on vascular smooth muscle. The EDCFs released by acetylcholine have been identified as prostacyclin and prostaglandin (PG) H(2) while in response to A 23187 thromboxane A(2), along with the two other prostaglandins, contributes to the endothelium-dependent contractions. The purpose of the present study was to identify the EDCFs produced by ATP. Isometric tension and the release of prostaglandins were measured in isolated aortic rings of WKY rats and SHR. ATP produced the endothelium-dependent release of prostacyclin, thromboxane A(2) and PGE(2) (PGI(2)>>TXA(2)> or =PGE(2)>PGF(2alpha)) in a similar manner in aorta from WKY rats and SHR. In SHR aortas, the release of thromboxane A(2) was significantly larger in response to ATP than to acetylcholine while that to prostacyclin was significantly smaller. The inhibition of cyclooxygenase with indomethacin prevented the release of prostaglandins and the occurrence of endothelium-dependent contractions. The thromboxane synthase inhibitor dazoxiben selectively abolished the ATP-dependent production of thromboxane A(2) and partially inhibited the corresponding endothelium-dependent contractions. U 51605, a non-selective inhibitor of PGI-synthase, reduced the release of prostacyclin elicited by ATP but induced a parallel increase in the production of PGE(2) and PGF(2alpha), suggestive of a PGH(2)-spillover, which was associated with the enhancement of the endothelium-dependent contractions. Thus, in the aorta of SHR, endothelium-dependent contractions elicited by ATP involve the release of thromboxane A(2) and prostacyclin with a possible contribution of PGH(2).
[Mh] Termos MeSH primário: Trifosfato de Adenosina/farmacologia
Aorta Torácica/fisiologia
Endotélio Vascular/fisiologia
Músculo Liso Vascular/fisiologia
[Mh] Termos MeSH secundário: Acetilcolina/metabolismo
Animais
Aorta Torácica/efeitos dos fármacos
Aorta Torácica/metabolismo
Inibidores de Ciclo-Oxigenase/farmacologia
Inibidores das Enzimas do Citocromo P-450
Sistema Enzimático do Citocromo P-450
Dinoprostona/biossíntese
Endotélio Vascular/efeitos dos fármacos
Técnicas In Vitro
Indometacina/farmacologia
Oxirredutases Intramoleculares/antagonistas & inibidores
Masculino
Contração Muscular/efeitos dos fármacos
Músculo Liso Vascular/efeitos dos fármacos
Músculo Liso Vascular/metabolismo
Prostaglandina-Endoperóxido Sintases/metabolismo
Prostaglandinas H/farmacologia
Prostaglandinas I/metabolismo
Ratos
Ratos Endogâmicos SHR
Ratos Endogâmicos WKY
Tromboxano A2/biossíntese
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cyclooxygenase Inhibitors); 0 (Cytochrome P-450 Enzyme Inhibitors); 0 (Prostaglandins H); 0 (Prostaglandins I); 57576-52-0 (Thromboxane A2); 64192-56-9 (azo analog I); 8L70Q75FXE (Adenosine Triphosphate); 9035-51-2 (Cytochrome P-450 Enzyme System); EC 1.14.99.1 (Prostaglandin-Endoperoxide Synthases); EC 5.3.- (Intramolecular Oxidoreductases); EC 5.3.99.4 (prostacyclin synthetase); K7Q1JQR04M (Dinoprostone); N9YNS0M02X (Acetylcholine); XXE1CET956 (Indomethacin)
[Em] Mês de entrada:0704
[Cu] Atualização por classe:151119
[Lr] Data última revisão:
151119
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:061128
[St] Status:MEDLINE


  10 / 639 MEDLINE  
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[PMID]:16597439
[Au] Autor:Myung SC; Keum EM; Park SY; Lee MY; Kim SC
[Ad] Endereço:Department of Urology, Chung-Ang University, College of Medicine, Dongjak Gu, Huksuk Dong 221, Seoul, Korea.
[Ti] Título:Vasomotor action of insulin on the rabbit normal cavernous smooth muscle.
[So] Source:Eur J Pharmacol;536(1-2):142-7, 2006 Apr 24.
[Is] ISSN:0014-2999
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Investigations on the effects of insulin on the normal vasculature have produced conflicting results. This study was aimed at establishing the vasomotor actions of insulin on normal cavernous smooth muscle. Insulin produced dose-dependent (10(-10)-10(-5) M) relaxation of the norepinephrine-precontracted strips of cavernosum, and of Bay K8644 [methyl-1,4-dihydro-2,6-dimethyl-3-nitro-4-2(trifluoromethylphenyl)pyridine-5-carboxylate]-precontracted strips. Endothelial denudation or indomethacin (10 microM) pre-treatment significantly reduced these insulin-induced relaxations, whereas NG-nitro-L-arginine methyl ester (L-NAME, 5 mM) did not. Moreover, the pre-treatment of the cavernosum strips with a prostacyclin synthesis inhibitor [9,11-diazo-15-deoxy-prostaglandin H2 (U-51605), 10 microM] significantly reduced insulin-induced response, whereas pretreatment with a cyclooxygenase-2 (COX-2) inhibitor (NS-398, 10 microM) did not. In addition, responses to insulin were not inhibited by K+ channel blockers, i.e., tetraethylammonium (TEA, 10 mM) or 4-aminopyridine (4-AP, 10 microM). Moreover, L-type Ca2+ currents were reduced by prostacyclin (2 microM) but not by insulin (10 microM). We conclude that insulin induces the endothelium-dependent relaxation of cavernous smooth muscles and that this relaxation response may emanate from the direct inhibition of L-type Ca2+ channels by prostacyclin.
[Mh] Termos MeSH primário: Insulina/farmacologia
Relaxamento Muscular/efeitos dos fármacos
Músculo Liso Vascular/efeitos dos fármacos
[Mh] Termos MeSH secundário: Éster Metílico do Ácido 3-Piridinacarboxílico, 1,4-Di-Hidro-2,6-Dimetil-5-Nitro-4-(2-(Trifluormetil)fenil)/farmacologia
4-Aminopiridina/farmacologia
Animais
Canais de Cálcio/fisiologia
Relação Dose-Resposta a Droga
Endotélio Vascular/fisiologia
Técnicas In Vitro
Indometacina/farmacologia
Masculino
Potenciais da Membrana/efeitos dos fármacos
Contração Muscular/efeitos dos fármacos
Músculo Liso Vascular/fisiologia
Norepinefrina/farmacologia
Pênis/irrigação sanguínea
Pênis/efeitos dos fármacos
Pênis/fisiologia
Bloqueadores dos Canais de Potássio/farmacologia
Canais de Potássio/fisiologia
Prostaglandinas/farmacologia
Prostaglandinas H/farmacologia
Coelhos
Tetraetilamônio/farmacologia
Vasoconstritores/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Calcium Channels); 0 (Insulin); 0 (Potassium Channel Blockers); 0 (Potassium Channels); 0 (Prostaglandins); 0 (Prostaglandins H); 0 (Vasoconstrictor Agents); 64192-56-9 (azo analog I); 66-40-0 (Tetraethylammonium); 71145-03-4 (3-Pyridinecarboxylic acid, 1,4-dihydro-2,6-dimethyl-5-nitro-4-(2-(trifluoromethyl)phenyl)-, Methyl ester); BH3B64OKL9 (4-Aminopyridine); X4W3ENH1CV (Norepinephrine); XXE1CET956 (Indomethacin)
[Em] Mês de entrada:0607
[Cu] Atualização por classe:141120
[Lr] Data última revisão:
141120
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:060407
[St] Status:MEDLINE



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