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

Involvement of tyrosine kinase

O. Kozawa, Atsushi 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 - 01-01-1995
Externally publishedYes

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Phospholipase D
Dinoprost
Osteoblasts
Protein-Tyrosine Kinases
Chemical activation
Choline
Genistein
Tyrphostins
Protein Tyrosine Phosphatases
Vanadates
Egtazic Acid
Extracellular Space
Phosphatidylcholines
Sodium
Acids

All Science Journal Classification (ASJC) codes

  • Clinical Biochemistry
  • Cell Biology

Cite this

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title = "Function of Ca2+ influx in phospholipase D activation induced by prostaglandin F2α in osteoblast-like cells: Involvement of tyrosine kinase",
abstract = "We previously reported that prostaglandin F2α (PGF2α) induces Ca2+ influx from the extracellular space via protein tyrosine kinase in osteoblast-like MC3T3-E1 cells and that PGF2α 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 PGF2α and the activation of phospholipase D in MC3T3-E1 cells. The depletion of extracellular Ca2+ by [ethylenebis(oxyethylenenitrilo)]tetraacetic acid (EGTA) markedly reduced the PGF2α-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 PGF2α in a dose-dependent manner. Tyrphostin, an inhibitor of protein tyrosine kinases chemically distinct from genistein, also suppressed the PGF2α-induced formation of choline. Sodium orthovanadate, an inhibitor of protein tyrosine phosphatases, significantly enhanced the PGF2α-induced formation of choline. These results strongly suggest that the phospholipase D activation by PGF2α is dependent on extracellular Ca2+ in osteoblast-like cells and that protein tyrosine kinase is involved in the activation of phospholipase D.",
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Function of Ca2+ influx in phospholipase D activation induced by prostaglandin F in osteoblast-like cells : Involvement of tyrosine kinase. / Kozawa, O.; Suzuki, Atsushi; Watanabe, Y.; Shinoda, J.; Oiso, Y.

In: Prostaglandins, Leukotrienes and Essential Fatty Acids, Vol. 52, No. 5, 01.01.1995, p. 319-323.

Research output: Contribution to journalArticle

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AU - Suzuki, Atsushi

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