Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1988-8-1
pubmed:abstractText
Phospholipid metabolism was studied in rat myocardial slices that were incubated under normoxia or hypoxia for up to 24 hours. Phospholipid degradation was prominent in hypoxic myocardium, particularly phosphatidylcholine, which markedly decreased after 24 hours of hypoxia. In contrast, lysophosphatidylcholine increased. The mechanism of phospholipid degradation in hypoxic myocardium was studied. The highest activity for phospholipase A2 among subcellular fractions was found in microsomal fraction. In hypoxic myocardium, this phospholipase A2 activity markedly increased and had substrate specificity toward phosphatidylcholine and phosphatidylethanolamine. Phosphatidylcholine was slightly hydrolyzed in control myocardium, but it was markedly hydrolyzed in hypoxic myocardium. Phospholipase C activity was found in cytosol and had a high substrate specificity toward phosphatidylinositol. In hypoxic myocardium, its activity gradually decreased during hypoxic incubation. Prostacyclin biosynthesis was also determined. The synthesis of prostacyclin in hypoxic myocardial microsomes did not increase. These results suggest that hypoxia causes phospholipid degradation and activates phospholipase A2 activity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0009-7330
pubmed:author
pubmed:issnType
Print
pubmed:volume
62
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1175-81
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Prostacyclin biosynthesis and phospholipase activity in hypoxic rat myocardium.
pubmed:affiliation
Department of Cardiovascular Medicine, Hokkaido University, School of Medicine, Sapporo, Japan.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't