Stimulation of phospholipase A2 activity in human platelets by trypsin and collagen

Thomas M. Chiang, Andrew Kang, John N. Fain

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

Type I collagen enhanced human platelet phospholipase A2 activity whether added to platelet-rich plasma or washed platelets. The stimulatory effect of type I collagen on platelet membrane phospholipase A2 activity was also observed in a cell-free system utilizing platelet membranes. The release of arachidonic acid was enhanced by types I and III but not by type V collagen. The activation of platelet phospholipase A2 by type I collagen was inhibited by soybean trypsin inhibitor and mimicked by trypsin. However, type I collagen addition was not associated with any detectable changes in platelet membrane proteins while trypsin altered many proteins. These results point to acid soluble phospholipase A2 activity of platelets as an enzyme activated by type I collagen.

Original languageEnglish (US)
Pages (from-to)47-52
Number of pages6
JournalArchives of Biochemistry and Biophysics
Volume284
Issue number1
DOIs
StatePublished - Jan 1 1991

Fingerprint

Phospholipases A2
Platelets
Human Activities
Trypsin
Collagen Type I
Collagen
Blood Platelets
Collagen Type V
Platelet-Rich Plasma
Trypsin Inhibitors
Membranes
Cell-Free System
Platelet Activation
Soybeans
Arachidonic Acid
Membrane Proteins
Acids
Chemical activation
Enzymes
Plasmas

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology

Cite this

Stimulation of phospholipase A2 activity in human platelets by trypsin and collagen. / Chiang, Thomas M.; Kang, Andrew; Fain, John N.

In: Archives of Biochemistry and Biophysics, Vol. 284, No. 1, 01.01.1991, p. 47-52.

Research output: Contribution to journalArticle

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