Function of Ca2+ influx in phospholipase D activation induced by prostaglandin F in osteoblast-like cells: Involvement of tyrosine kinase

O. Kozawa, A. Suzuki, Y. Watanabe, J. Shinoda, Y. Oiso

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

We previously reported that prostaglandin F (PGF) induces Ca2+ influx from the extracellular space via protein tyrosine kinase in osteoblast-like MC3T3-E1 cells and that PGF stimulates phosphatidylcholine-hydrolyzing phospholipase D in these cells (6, 12). In this study, we examined the relationship between the tyrosine kinase-regulated Ca2+ influx by PGF and the activation of phospholipase D in MC3T3-E1 cells. The depletion of extracellular Ca2+ by [ethylenebis(oxyethylenenitrilo)]tetraacetic acid (EGTA) markedly reduced the PGF-induced formation of choline. Genistein, an inhibitor of protein tyrosine kinases, which by itself had little effect on choline formation, significantly suppressed the formation of choline induced by PGF in a dose-dependent manner. Tyrphostin, an inhibitor of protein tyrosine kinases chemically distinct from genistein, also suppressed the PGF-induced formation of choline. Sodium orthovanadate, an inhibitor of protein tyrosine phosphatases, significantly enhanced the PGF-induced formation of choline. These results strongly suggest that the phospholipase D activation by PGF is dependent on extracellular Ca2+ in osteoblast-like cells and that protein tyrosine kinase is involved in the activation of phospholipase D.

Original languageEnglish
Pages (from-to)319-323
Number of pages5
JournalProstaglandins, Leukotrienes and Essential Fatty Acids
Volume52
Issue number5
DOIs
Publication statusPublished - 05-1995
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Clinical Biochemistry
  • Cell Biology

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