Linked Life Data

17200681

Source:http://linkedlifedata.com/resource/pubmed/id/17200681

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2007-2-8
pubmed:abstractText
The nitric oxide (NO) and cyclooxygenase (COX) pathways share a number of similarities. NO is the mediator generated from the NO synthase (NOS) pathway and COX converts arachidonic acid to prostaglandins (PGs), prostacyclin, and thromboxane A2. Two major forms of NOS and COX have been identified to date. The constitutive isoforms of these enzymes play an important role in the regulation of several physiological states. On the other hand, in an inflammatory setting, the inducible isoforms of these enzymes are induced in a variety of cells resulting in the production of large amounts NO and PGs, which play pathological roles in several disease states. An important link between the NOS and COX pathways was made by our group when we demonstrated that NO activates the COX enzymes, an event leading to overt production of PGs, suggesting that COX enzymes represent important endogenous 'receptor' targets for modulating the multifaceted roles of NO. More importantly, mechanistic studies of how NO activates the COX enzymes have been undertaken and additional pathways through which NO modulates PG production unraveled. The purpose of this article is to cover the advances, which have occurred over the years and in particular to summarize experimental data that outline how the discovery that NO modulates PG production has impacted and extended our understanding of these two systems in physiopathological events.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0085-2538
pubmed:author
pubmed:issnType
Print
pubmed:volume
71
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
290-7
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Molecular mechanisms involved in the reciprocal regulation of cyclooxygenase and nitric oxide synthase enzymes.
pubmed:affiliation
Department of Clinical and Experimental Medicine and Pharmacology, University of Messina, Messina, Italy.
pubmed:publicationType
Journal Article, Review