Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1989-7-18
pubmed:abstractText
The phospholipase activities of cell-free extracts of human lung were studied using sn-2-arachidonoyl phospholipids. Samples of human lung obtained during surgery were homogenized and separated by centrifugation into three fractions: P1, containing mitochondrial and lysosomal marker enzymes; P2, with microsomal enzymes; and S2, with cytosolic enzymes. The highest phospholipase activities were in the microsomal fraction, using any of the three substrates, [14C]arachidonoylphosphatidylcholine (PC), [14C]arachidonoylphosphatidylethanolamine (PE) and [14C]arachidonoylphosphatidylinositol (PI). From PC and PE, only free arachidonic acid was formed, suggesting the presence of a phospholipase A2 (PLA2)-like activity. From PI, two metabolites were produced, diacylglycerol and arachidonic acid, suggesting the presence of a PI-specific PLC activity. Rates of hydrolysis were highest for PI, followed by PE and then PC. Hydrolysis of [14C]arachidonoyl-PC was compared to that of [14C]oleoyl-PC and found to be similarly distributed and of comparable velocity. The distribution and relative activities of phospholipases in rat lung homogenates were very similar to those in human lung.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
8
pubmed:volume
1003
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
189-95
pubmed:dateRevised
2009-9-29
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Phospholipases A2 and C of human lung; subcellular distribution and substrate selectivity.
pubmed:affiliation
Department of Pharmacology, Hunterian Institute, Royal College of Surgeons, London, U.K.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't