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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5-6
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pubmed:dateCreated |
1985-9-24
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pubmed:abstractText |
The fatty acyl specificity of phospholipase A1 and A2 in homogenates of mouse bone marrow-derived macrophages was determined using phosphatidylcholine and phosphatidylethanolamine of different acyl chain composition. Phosphatidylcholine with arachidonoyl at position 2 was cleaved preferentially by an alkaline phospholipase A2 (pH-optimum 9.0) leading to selective liberation of arachidonic acid. In contrast, phosphatidylcholines with oleoyl or linoleoyl at position 2 were degraded mainly by an acid phospholipase A1 (pH-optimum 4-5) resulting in a conservation of these fatty acids esterified in lysophosphatides. Substrate kinetics of the alkaline phospholipase A2 revealed a 30 fold higher affinity (Km = 3.8 X 10(-7) M) for 1-acyl-2-arachidonoyl-glycerophosphocholine compared to 1-acyl-2-oleoyl-glycerophosphocholine. The kinetic data were not influenced by endogenous lipids indicating that exogenous substrates do not equilibrate with cellular lipids. These results are suitable to explain a selective liberation of arachidonic acid from a mixture of phospholipids.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:issn |
0341-0382
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
40
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
356-63
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pubmed:dateRevised |
2009-6-8
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pubmed:meshHeading |
pubmed-meshheading:4024704-Animals,
pubmed-meshheading:4024704-Bone Marrow,
pubmed-meshheading:4024704-Cells, Cultured,
pubmed-meshheading:4024704-Deoxycholic Acid,
pubmed-meshheading:4024704-Enzyme Activation,
pubmed-meshheading:4024704-Female,
pubmed-meshheading:4024704-Hydrogen-Ion Concentration,
pubmed-meshheading:4024704-Kinetics,
pubmed-meshheading:4024704-L Cells (Cell Line),
pubmed-meshheading:4024704-Lysophospholipase,
pubmed-meshheading:4024704-Macrophages,
pubmed-meshheading:4024704-Mice,
pubmed-meshheading:4024704-Mice, Inbred C57BL,
pubmed-meshheading:4024704-Phospholipases,
pubmed-meshheading:4024704-Phospholipases A,
pubmed-meshheading:4024704-Phospholipases A1,
pubmed-meshheading:4024704-Phospholipases A2,
pubmed-meshheading:4024704-Substrate Specificity
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pubmed:articleTitle |
Acyl chain specificity and kinetic properties of phospholipase A1 and A2 of bone marrow-derived macrophages.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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