The activities of acyl-CoA hydrolase in lysate and subcellular fractions of human blood platelets in relation to activities of acyl-CoA:1-acyl-lysophospholipid acyltransferase.
The activities of acyl-CoA hydrolase (EC 3.1.2.2.) and acyl-CoA:1-acyl- lysophospholipid acyltransferase (EC 2.3.1.23) have been studied in subcellular fractions of human platelets. The acyl-CoA:1-acyl-lysophospholipid acyltransferase activity was higher in the 'dense-tubular-system-enriched' fraction than in the 'light-mitochondrial' fraction, using endogenously acyl-CoAs formed from labelled fatty acids, ATP, CoA and various lysophospholipids. No activity was found in the 'particle-free' fraction. No difference in specificities was observed between the incorporation of various fatty acids into different lysoPLs in the subcellular fractions compared with the platelet lysates. Generally, arachidonic, linoleic and eicosapentaenoic acids were better substrates for the acyl-CoA:1-acyl-lysophospholipid acyltransferases than oleic, docosahexaenoic and palmitic acids. The opposite was observed with the acyl-CoA hydrolase activity, palmitoyl-CoA was the substrate giving the highest activity, and eicosapentaenoyl-CoA and arachidonoyl-CoA the lowest. About 85% of the hydrolase activity was detected in the 'particle-free' fraction, with each of the six acyl-CoA derivatives tested.
Bakken
A M
AM
Department of Clinical Biology, University of Bergen, University Hospital Haukeland, Norway.
Farstad
M
M
Osmundsen
H
H
D008243:1-Acylglycerophosphocholine O-Acyltransferase / Q000378:metabolism*; D001792:Blood Platelets / Q000201:enzymology*; D006801:Humans; D066298:In Vitro Techniques; D019787:Linoleic Acid; D008041:Linoleic Acids / Q000378:metabolism; D010170:Palmitoyl-CoA Hydrolase / Q000378:metabolism*; D010743:Phospholipids / Q000378:metabolism; D013347:Subcellular Fractions / Q000201:enzymology
D008041:Linoleic Acids; D010743:Phospholipids; D019787:Linoleic Acid; D008243:1-Acylglycerophosphocholine O-Acyltransferase; D010170:Palmitoyl-CoA Hydrolase