Thrombin triggers the de novo expression of an inducible NO synthase in porcine aortic valve endothelial cells
The nitric oxide (NO) production by porcine aortic valve endothelial cells was estimated in cusps incubated at 37°C by measuring their cyclic GMP content and the nitrite levels of the incubation medium. After a stabilization period, incubations for 5 min with acetylcholine, bradykinin, ADP and bovin...
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Veröffentlicht in: | European journal of pharmacology 1995-10, Vol.291 (2), p.67-72 |
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creator | De Meyer, Erwin Van Hove, Cor E. Feng, Xiao Jie Rampart, Marc Herman, Arnold G. |
description | The nitric oxide (NO) production by porcine aortic valve endothelial cells was estimated in cusps incubated at 37°C by measuring their cyclic GMP content and the nitrite levels of the incubation medium. After a stabilization period, incubations for 5 min with acetylcholine, bradykinin, ADP and bovine thrombin resulted in a receptor-mediated increase in cyclic GMP which could be blocked by EGTA,
N-ω-
nitro-
L-
arginine
methyl ester (L-NAME) and N
G-monomethyl-
L-arginine (L-NMMA). Incubation with lipopolysaccharide (endotoxin) from
E. coli O111:B4 or bovine thrombin for 5 h, dose-dependently increased nitrite production as well as cyclic GMP content. The elevated nitrite production was completely abolished in the presence of the protein synthesis inhibitor cycloheximide, was reduced by more than 50% by dexamethasone but was not affected by EGTA. L-NMMA dose-dependently reduced the increased nitrite production and cyclic GMP content. These results suggest that besides the presence of a constitutive NO synthase in porcine aortic valve endothelial cells thrombin, like lipopolysaccharide, triggers the de novo expression of an inducible Ca
2+-independent NO synthase. |
doi_str_mv | 10.1016/0922-4106(95)90126-4 |
format | Article |
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N-ω-
nitro-
L-
arginine
methyl ester (L-NAME) and N
G-monomethyl-
L-arginine (L-NMMA). Incubation with lipopolysaccharide (endotoxin) from
E. coli O111:B4 or bovine thrombin for 5 h, dose-dependently increased nitrite production as well as cyclic GMP content. The elevated nitrite production was completely abolished in the presence of the protein synthesis inhibitor cycloheximide, was reduced by more than 50% by dexamethasone but was not affected by EGTA. L-NMMA dose-dependently reduced the increased nitrite production and cyclic GMP content. These results suggest that besides the presence of a constitutive NO synthase in porcine aortic valve endothelial cells thrombin, like lipopolysaccharide, triggers the de novo expression of an inducible Ca
2+-independent NO synthase.</description><identifier>ISSN: 0922-4106</identifier><identifier>ISSN: 0014-2999</identifier><identifier>DOI: 10.1016/0922-4106(95)90126-4</identifier><identifier>PMID: 8566177</identifier><language>eng</language><publisher>Amsterdam: Elsevier B.V</publisher><subject>Animals ; Aorta - drug effects ; Aorta - enzymology ; Aortic valve cusp ; Arginine - analogs & derivatives ; Arginine - pharmacology ; Biological and medical sciences ; Blood vessels and receptors ; Cyclic GMP ; Cyclic GMP - metabolism ; Endothelium, Vascular - drug effects ; Endothelium, Vascular - enzymology ; Enzyme Inhibitors - pharmacology ; Enzyme-Linked Immunosorbent Assay ; Fundamental and applied biological sciences. Psychology ; NG-Nitroarginine Methyl Ester ; Nitric oxide (NO) ; Nitric Oxide Synthase - biosynthesis ; Nitric Oxide Synthase - metabolism ; Nitric oxide synthase, constitutive ; Nitric oxide synthase, inducible ; porcine ; Swine ; Thrombin ; Thrombin - pharmacology ; Vertebrates: cardiovascular system</subject><ispartof>European journal of pharmacology, 1995-10, Vol.291 (2), p.67-72</ispartof><rights>1995</rights><rights>1996 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c386t-f64d22e5a591e0e7f6efd685f7b7462000838ff2b1608e86d11d1c773c64d773</citedby><cites>FETCH-LOGICAL-c386t-f64d22e5a591e0e7f6efd685f7b7462000838ff2b1608e86d11d1c773c64d773</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,777,781,27905,27906</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=2912482$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8566177$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>De Meyer, Erwin</creatorcontrib><creatorcontrib>Van Hove, Cor E.</creatorcontrib><creatorcontrib>Feng, Xiao Jie</creatorcontrib><creatorcontrib>Rampart, Marc</creatorcontrib><creatorcontrib>Herman, Arnold G.</creatorcontrib><title>Thrombin triggers the de novo expression of an inducible NO synthase in porcine aortic valve endothelial cells</title><title>European journal of pharmacology</title><addtitle>Eur J Pharmacol</addtitle><description>The nitric oxide (NO) production by porcine aortic valve endothelial cells was estimated in cusps incubated at 37°C by measuring their cyclic GMP content and the nitrite levels of the incubation medium. After a stabilization period, incubations for 5 min with acetylcholine, bradykinin, ADP and bovine thrombin resulted in a receptor-mediated increase in cyclic GMP which could be blocked by EGTA,
N-ω-
nitro-
L-
arginine
methyl ester (L-NAME) and N
G-monomethyl-
L-arginine (L-NMMA). Incubation with lipopolysaccharide (endotoxin) from
E. coli O111:B4 or bovine thrombin for 5 h, dose-dependently increased nitrite production as well as cyclic GMP content. The elevated nitrite production was completely abolished in the presence of the protein synthesis inhibitor cycloheximide, was reduced by more than 50% by dexamethasone but was not affected by EGTA. L-NMMA dose-dependently reduced the increased nitrite production and cyclic GMP content. These results suggest that besides the presence of a constitutive NO synthase in porcine aortic valve endothelial cells thrombin, like lipopolysaccharide, triggers the de novo expression of an inducible Ca
2+-independent NO synthase.</description><subject>Animals</subject><subject>Aorta - drug effects</subject><subject>Aorta - enzymology</subject><subject>Aortic valve cusp</subject><subject>Arginine - analogs & derivatives</subject><subject>Arginine - pharmacology</subject><subject>Biological and medical sciences</subject><subject>Blood vessels and receptors</subject><subject>Cyclic GMP</subject><subject>Cyclic GMP - metabolism</subject><subject>Endothelium, Vascular - drug effects</subject><subject>Endothelium, Vascular - enzymology</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>Enzyme-Linked Immunosorbent Assay</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>NG-Nitroarginine Methyl Ester</subject><subject>Nitric oxide (NO)</subject><subject>Nitric Oxide Synthase - biosynthesis</subject><subject>Nitric Oxide Synthase - metabolism</subject><subject>Nitric oxide synthase, constitutive</subject><subject>Nitric oxide synthase, inducible</subject><subject>porcine</subject><subject>Swine</subject><subject>Thrombin</subject><subject>Thrombin - pharmacology</subject><subject>Vertebrates: cardiovascular system</subject><issn>0922-4106</issn><issn>0014-2999</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE9rGzEQxXVoSdM03yABHUJpD9tKslZaXQoh9B-E5uK70EqjWGEtOZq1ab595Nr42NPAm_ceMz9Crjj7whlXX5kRopOcqU-m_2wYF6qTb8j5SX5H3iM-McYMN_KMnA29Ulzrc5KXq1rWY8p0runxESrSeQU0AM1lVyj83VRATCXTEqnLNOWw9WmcgP55oPiS55VDaCrdlOpTBupKnZOnOzftgEIOpdVNyU3UwzThB_I2ugnh8jgvyPLH9-Xdr-7-4efvu9v7zi8GNXdRySAE9K43HBjoqCAGNfRRj1oq0f4YFkOMYuSKDTCowHngXuuFb8E2LsjHQ-2mluct4GzXCfcHuAxli1ZrbXopWDPKg9HXglgh2k1Na1dfLGd2T9buEdo9Qmt6-4-slS12fezfjmsIp9ARa9vfHPcOvZtiddknPNmE4UIOotm-HWzQUOwSVIs-QfYQUgU_21DS_-94BRRrl2I</recordid><startdate>19951015</startdate><enddate>19951015</enddate><creator>De Meyer, Erwin</creator><creator>Van Hove, Cor E.</creator><creator>Feng, Xiao Jie</creator><creator>Rampart, Marc</creator><creator>Herman, Arnold G.</creator><general>Elsevier B.V</general><general>Elsevier</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19951015</creationdate><title>Thrombin triggers the de novo expression of an inducible NO synthase in porcine aortic valve endothelial cells</title><author>De Meyer, Erwin ; Van Hove, Cor E. ; Feng, Xiao Jie ; Rampart, Marc ; Herman, Arnold G.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c386t-f64d22e5a591e0e7f6efd685f7b7462000838ff2b1608e86d11d1c773c64d773</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Animals</topic><topic>Aorta - drug effects</topic><topic>Aorta - enzymology</topic><topic>Aortic valve cusp</topic><topic>Arginine - analogs & derivatives</topic><topic>Arginine - pharmacology</topic><topic>Biological and medical sciences</topic><topic>Blood vessels and receptors</topic><topic>Cyclic GMP</topic><topic>Cyclic GMP - metabolism</topic><topic>Endothelium, Vascular - drug effects</topic><topic>Endothelium, Vascular - enzymology</topic><topic>Enzyme Inhibitors - pharmacology</topic><topic>Enzyme-Linked Immunosorbent Assay</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>NG-Nitroarginine Methyl Ester</topic><topic>Nitric oxide (NO)</topic><topic>Nitric Oxide Synthase - biosynthesis</topic><topic>Nitric Oxide Synthase - metabolism</topic><topic>Nitric oxide synthase, constitutive</topic><topic>Nitric oxide synthase, inducible</topic><topic>porcine</topic><topic>Swine</topic><topic>Thrombin</topic><topic>Thrombin - pharmacology</topic><topic>Vertebrates: cardiovascular system</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>De Meyer, Erwin</creatorcontrib><creatorcontrib>Van Hove, Cor E.</creatorcontrib><creatorcontrib>Feng, Xiao Jie</creatorcontrib><creatorcontrib>Rampart, Marc</creatorcontrib><creatorcontrib>Herman, Arnold G.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>European journal of pharmacology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>De Meyer, Erwin</au><au>Van Hove, Cor E.</au><au>Feng, Xiao Jie</au><au>Rampart, Marc</au><au>Herman, Arnold G.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Thrombin triggers the de novo expression of an inducible NO synthase in porcine aortic valve endothelial cells</atitle><jtitle>European journal of pharmacology</jtitle><addtitle>Eur J Pharmacol</addtitle><date>1995-10-15</date><risdate>1995</risdate><volume>291</volume><issue>2</issue><spage>67</spage><epage>72</epage><pages>67-72</pages><issn>0922-4106</issn><issn>0014-2999</issn><abstract>The nitric oxide (NO) production by porcine aortic valve endothelial cells was estimated in cusps incubated at 37°C by measuring their cyclic GMP content and the nitrite levels of the incubation medium. After a stabilization period, incubations for 5 min with acetylcholine, bradykinin, ADP and bovine thrombin resulted in a receptor-mediated increase in cyclic GMP which could be blocked by EGTA,
N-ω-
nitro-
L-
arginine
methyl ester (L-NAME) and N
G-monomethyl-
L-arginine (L-NMMA). Incubation with lipopolysaccharide (endotoxin) from
E. coli O111:B4 or bovine thrombin for 5 h, dose-dependently increased nitrite production as well as cyclic GMP content. The elevated nitrite production was completely abolished in the presence of the protein synthesis inhibitor cycloheximide, was reduced by more than 50% by dexamethasone but was not affected by EGTA. L-NMMA dose-dependently reduced the increased nitrite production and cyclic GMP content. These results suggest that besides the presence of a constitutive NO synthase in porcine aortic valve endothelial cells thrombin, like lipopolysaccharide, triggers the de novo expression of an inducible Ca
2+-independent NO synthase.</abstract><cop>Amsterdam</cop><pub>Elsevier B.V</pub><pmid>8566177</pmid><doi>10.1016/0922-4106(95)90126-4</doi><tpages>6</tpages></addata></record> |
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subjects | Animals Aorta - drug effects Aorta - enzymology Aortic valve cusp Arginine - analogs & derivatives Arginine - pharmacology Biological and medical sciences Blood vessels and receptors Cyclic GMP Cyclic GMP - metabolism Endothelium, Vascular - drug effects Endothelium, Vascular - enzymology Enzyme Inhibitors - pharmacology Enzyme-Linked Immunosorbent Assay Fundamental and applied biological sciences. Psychology NG-Nitroarginine Methyl Ester Nitric oxide (NO) Nitric Oxide Synthase - biosynthesis Nitric Oxide Synthase - metabolism Nitric oxide synthase, constitutive Nitric oxide synthase, inducible porcine Swine Thrombin Thrombin - pharmacology Vertebrates: cardiovascular system |
title | Thrombin triggers the de novo expression of an inducible NO synthase in porcine aortic valve endothelial cells |
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