Predominant inhibition of ganodermic acid S on the thromboxane A2- dependent pathway in human platelets response to collagen

Chen Yi Su, Ming Shi Shiao, Cheng Teh Wang*

*Corresponding author for this work

Research output: Contribution to journalJournal Article peer-review

18 Scopus citations

Abstract

Ganodermic acid S (GAS), a membrane acting agent, exerts multiple effects on human platelet function (C.N. Wang et al. (1991) Biochem. J. 277, 189-197). The study reported how GAS affected the response of human gel- filtered platelets (GFP) to collagen. The agent inhibited cell aggregation by prolonging lag and shape change periods and decreasing the initial cell aggregation rate. However, the inhibitory efficiency was less than its inhibition on GFP response to U46619, a thromboxane (TX) A2 mimetic. In the agent-effect on biochemical events, GAS effectively inhibited Ca2+ mobilization, phosphorylation of myosin light chain, dense granule secretion and TXB2 generation. The inhibitions might originate from blocking Ca2+ mobilization of the TXA2-dependent pathway. GAS partially decreased the phosphorylation of most phosphotyrosine proteins from early activation to the integrin α(IIb)β3-regulated steps. The agent did not affect the phosphorylation of three proteins at the steps regulated by integrin α(IIb)β3. The results suggest that GAS inhibits the collagen response predominantly on the TXA2-dependent signaling, and the tyrosine kinase- dependent pathway in collagen response plays a major role in aggregation.

Original languageEnglish
Pages (from-to)223-234
Number of pages12
JournalBiochimica et Biophysica Acta - Molecular and Cell Biology of Lipids
Volume1437
Issue number2
DOIs
StatePublished - 25 02 1999
Externally publishedYes

Keywords

  • (Human platelet)
  • Aggregation
  • Ca mobilization
  • Collagen
  • Ganodermic acid S
  • Tyrosine phosphorylation

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