Ca2+ effect on ATP-independent lysophospholipid transacylases is indissociable from Ca2+ effect on phospholipase A2 activity in rat platelet sonicates

Biochim Biophys Acta. 1988 Nov 4;963(1):127-30. doi: 10.1016/0005-2760(88)90345-1.

Abstract

CoA-dependent transacylation and phospholipid hydrolysis were studied in parallel experiments using rat platelet sonicates. The decrease observed in palmitoyllyso-sn-glycero-3-phosphocholine (palmitoyllyso-GPC) transcylation as a function of Ca2+ concentration was found to be correlated with appearance of endogenous lysoderivatives. We also demonstrated that endogenously produced acyllyso-sn-glycero-3-phosphoethanolamine (acyllyso-GPE) induced CoA-dependent arachidonate transfer from diacyl-GPC. These results further argue for a two-step arachidonate release from diacyl-GPC when platelets are stimulated with thrombin.

MeSH terms

  • Acyltransferases / blood*
  • Adenosine Triphosphate / metabolism*
  • Animals
  • Blood Platelets / enzymology*
  • Calcium / pharmacology*
  • Lysophospholipase / blood*
  • Multienzyme Complexes / blood*
  • Phospholipases / blood*
  • Phospholipases A / blood*
  • Phospholipases A2
  • Rats

Substances

  • Multienzyme Complexes
  • Adenosine Triphosphate
  • Acyltransferases
  • Phospholipases
  • Phospholipases A
  • Phospholipases A2
  • Lysophospholipase
  • lysophospholipase-transacylase
  • Calcium