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Article: COX-1 and vascular disease

TitleCOX-1 and vascular disease
Authors
Issue Date2009
PublisherNature Publishing Group. The Journal's web site is located at http://www.nature.com/clpt/index.html
Citation
Clinical Pharmacology And Therapeutics, 2009, v. 86 n. 2, p. 212-215 How to Cite?
AbstractSince the discovery of the pivotal role of cyclooxygenase (COX) in the metabolism of arachidonic acid, vascular biologists have been confronted with the duality of this system. Indeed, one substrate (arachidonic acid) transformed by one enzyme (COX) yields end products (endoperoxides) that exist only very briefly before being metabolized to more stable prostanoids by a set of specific downstream synthases that were initially believed to be tissue specific. For instance, platelets contain mainly the synthase that produces thromboxane A 2 (a potent proaggregatory and vasoconstrictor substance), whereas endothelial cells contain mainly the enzyme that generates prostacyclin (an equally potent antiaggregatory and vasodilator substance). The overproduction of thromboxane A 2 by platelets leads to thrombosis; endothelial cells resist vascular occlusion by producing prostacyclin. This duality of the metabolism of arachidonic acid has dominated our thinking about atherothrombosis for decades, and rightfully still does. As scientific understanding progressed, it became evident that two isoforms of COX exist: COX-1 and COX-2. COX-1 was initially considered to be the good, constitutive isoform, whereas COX-2 appeared to be mainly a bad inducible enzyme involved in inflammatory responses. However, more recently, the unexpected events resulting from the widespread use of selective COX-2 inhibitors has suggested that, from a cardiovascular point of view, the products of COX-2 exert a protective role and that this isoform cannot necessarily be regarded as bad. Likewise, evidence has emerged that initiation of the metabolism of arachidonic acid by COX-1 is not necessarily a good thing in terms of vascular protection. This brief review focuses on the potential contribution of endothelial COX-1 to vascular dysfunction. It is based on a number of review articles, to which the reader will be referred in order to identify the original references to the statements made; these references are not cited here because of space limitations.
Persistent Identifierhttp://hdl.handle.net/10722/59550
ISSN
2015 Impact Factor: 7.268
2015 SCImago Journal Rankings: 2.414
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorVanhoutte, PMen_HK
dc.date.accessioned2010-05-31T03:52:32Z-
dc.date.available2010-05-31T03:52:32Z-
dc.date.issued2009en_HK
dc.identifier.citationClinical Pharmacology And Therapeutics, 2009, v. 86 n. 2, p. 212-215en_HK
dc.identifier.issn0009-9236en_HK
dc.identifier.urihttp://hdl.handle.net/10722/59550-
dc.description.abstractSince the discovery of the pivotal role of cyclooxygenase (COX) in the metabolism of arachidonic acid, vascular biologists have been confronted with the duality of this system. Indeed, one substrate (arachidonic acid) transformed by one enzyme (COX) yields end products (endoperoxides) that exist only very briefly before being metabolized to more stable prostanoids by a set of specific downstream synthases that were initially believed to be tissue specific. For instance, platelets contain mainly the synthase that produces thromboxane A 2 (a potent proaggregatory and vasoconstrictor substance), whereas endothelial cells contain mainly the enzyme that generates prostacyclin (an equally potent antiaggregatory and vasodilator substance). The overproduction of thromboxane A 2 by platelets leads to thrombosis; endothelial cells resist vascular occlusion by producing prostacyclin. This duality of the metabolism of arachidonic acid has dominated our thinking about atherothrombosis for decades, and rightfully still does. As scientific understanding progressed, it became evident that two isoforms of COX exist: COX-1 and COX-2. COX-1 was initially considered to be the good, constitutive isoform, whereas COX-2 appeared to be mainly a bad inducible enzyme involved in inflammatory responses. However, more recently, the unexpected events resulting from the widespread use of selective COX-2 inhibitors has suggested that, from a cardiovascular point of view, the products of COX-2 exert a protective role and that this isoform cannot necessarily be regarded as bad. Likewise, evidence has emerged that initiation of the metabolism of arachidonic acid by COX-1 is not necessarily a good thing in terms of vascular protection. This brief review focuses on the potential contribution of endothelial COX-1 to vascular dysfunction. It is based on a number of review articles, to which the reader will be referred in order to identify the original references to the statements made; these references are not cited here because of space limitations.en_HK
dc.languageengen_HK
dc.publisherNature Publishing Group. The Journal's web site is located at http://www.nature.com/clpt/index.htmlen_HK
dc.relation.ispartofClinical Pharmacology and Therapeuticsen_HK
dc.subject.meshBlood Platelets - drug effects - metabolism-
dc.subject.meshCyclooxygenase 1 - metabolism-
dc.subject.meshEndothelium, Vascular - enzymology - metabolism-
dc.subject.meshHypertension - enzymology - metabolism-
dc.subject.meshPlatelet Aggregation Inhibitors - metabolism-
dc.titleCOX-1 and vascular diseaseen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0009-9236&volume=86&issue=2&spage=212&epage=215&date=2009&atitle=COX-1+and+Vascular+Disease-
dc.identifier.emailVanhoutte, PM: vanhoutt@hku.hken_HK
dc.identifier.authorityVanhoutte, PM=rp00238en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1038/clpt.2009.108en_HK
dc.identifier.pmid19553934-
dc.identifier.scopuseid_2-s2.0-67651166598en_HK
dc.identifier.hkuros166660en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-67651166598&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume86en_HK
dc.identifier.issue2en_HK
dc.identifier.spage212en_HK
dc.identifier.epage215en_HK
dc.identifier.isiWOS:000268565100023-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridVanhoutte, PM=7202304247en_HK
dc.identifier.citeulike8154051-

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