Effect of prostaglandin F on Ca 2+ influx in osteoblast‐like cells: Function of tyrosine kinase

Atsushi Suzuki, Osamu Kozawa, Hidehiko Saito, Yutaka Oiso

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

We previously reported that pertussis toxin–sensitive GTP‐binding protein is involved in prostaglandin F (PGF )‐induced phosphoinositide (PI) hydrolysis in osteoblast‐like MC3T3‐E1 cells [Miwa et al. (1990): Biochem Biophys Res Commun 171:1229–1235]. In the present study, we investigated the mechanism of PGF ‐induced Ca 2+ influx in MC3T3‐E1 cells. PGF ‐induced formation of total inositol phosphates (IPs) was markedly reduced by the depletion of extracellular Ca 2+ with EGTA. On the other hand, the depletion of extracellular Ca 2+ had little effect on PGF ‐induced inositol 1,4,5‐trisphosphate formation. PGF stimulated 45 Ca 2+ influx dose dependently, attaining a maximum effect at 10 nM. Dose of PGF above 10 nM caused less than maximal stimulation. Genistein, an inhibitor of protein tyrosine kinase, which by itself had little effect on 45 Ca 2+ influx, significantly suppressed the PGF ‐induced 45 Ca 2+ influx in a dose‐dependent manner in the range between 1 μg/ml and 0.1 mg/ml. Sodium orthovanadate, an inhibitor of protein tyrosine phosphatases, enhanced the PGF ‐induced 45 Ca 2+ influx. Genistein also suppressed the PGF ‐induced total IPs formation dose dependently in the range between 1 μg/ml and 0.1 mg/ml. However, it had little effect on the PGF ‐induced inositol 1,4,5‐trisphosphate formation. The pretreatment with pertussis toxin had little effect on the PGF ‐induced 45 Ca 2+ influx. These results strongly suggest that PGF stimulates Ca 2+ mobilization from extracellular space and PI hydrolysis via independent pathways in osteoblast‐like cells, and the PGF ‐induced Ca 2+ influx is regulated by protein tyrosine kinase, resulting in the promotion of PI hydrolysis.

Original languageEnglish
Pages (from-to)487-493
Number of pages7
JournalJournal of Cellular Biochemistry
Volume54
Issue number4
DOIs
Publication statusPublished - 01-01-1994
Externally publishedYes

Fingerprint

Prostaglandins F
Protein-Tyrosine Kinases
Phosphatidylinositols
Hydrolysis
Inositol Phosphates
Genistein
Inositol
Protein Tyrosine Phosphatases
Vanadates
Whooping Cough
Egtazic Acid
Pertussis Toxin
Extracellular Space
Sodium

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

@article{6d93ee84e3c949cc96001d475736ad71,
title = "Effect of prostaglandin F 2α on Ca 2+ influx in osteoblast‐like cells: Function of tyrosine kinase",
abstract = "We previously reported that pertussis toxin–sensitive GTP‐binding protein is involved in prostaglandin F 2α (PGF 2α )‐induced phosphoinositide (PI) hydrolysis in osteoblast‐like MC3T3‐E1 cells [Miwa et al. (1990): Biochem Biophys Res Commun 171:1229–1235]. In the present study, we investigated the mechanism of PGF 2α ‐induced Ca 2+ influx in MC3T3‐E1 cells. PGF 2α ‐induced formation of total inositol phosphates (IPs) was markedly reduced by the depletion of extracellular Ca 2+ with EGTA. On the other hand, the depletion of extracellular Ca 2+ had little effect on PGF 2α ‐induced inositol 1,4,5‐trisphosphate formation. PGF 2α stimulated 45 Ca 2+ influx dose dependently, attaining a maximum effect at 10 nM. Dose of PGF 2α above 10 nM caused less than maximal stimulation. Genistein, an inhibitor of protein tyrosine kinase, which by itself had little effect on 45 Ca 2+ influx, significantly suppressed the PGF 2α ‐induced 45 Ca 2+ influx in a dose‐dependent manner in the range between 1 μg/ml and 0.1 mg/ml. Sodium orthovanadate, an inhibitor of protein tyrosine phosphatases, enhanced the PGF 2α ‐induced 45 Ca 2+ influx. Genistein also suppressed the PGF 2α ‐induced total IPs formation dose dependently in the range between 1 μg/ml and 0.1 mg/ml. However, it had little effect on the PGF 2α ‐induced inositol 1,4,5‐trisphosphate formation. The pretreatment with pertussis toxin had little effect on the PGF 2α ‐induced 45 Ca 2+ influx. These results strongly suggest that PGF 2α stimulates Ca 2+ mobilization from extracellular space and PI hydrolysis via independent pathways in osteoblast‐like cells, and the PGF 2α ‐induced Ca 2+ influx is regulated by protein tyrosine kinase, resulting in the promotion of PI hydrolysis.",
author = "Atsushi Suzuki and Osamu Kozawa and Hidehiko Saito and Yutaka Oiso",
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Effect of prostaglandin F on Ca 2+ influx in osteoblast‐like cells : Function of tyrosine kinase. / Suzuki, Atsushi; Kozawa, Osamu; Saito, Hidehiko; Oiso, Yutaka.

In: Journal of Cellular Biochemistry, Vol. 54, No. 4, 01.01.1994, p. 487-493.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Effect of prostaglandin F 2α on Ca 2+ influx in osteoblast‐like cells

T2 - Function of tyrosine kinase

AU - Suzuki, Atsushi

AU - Kozawa, Osamu

AU - Saito, Hidehiko

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N2 - We previously reported that pertussis toxin–sensitive GTP‐binding protein is involved in prostaglandin F 2α (PGF 2α )‐induced phosphoinositide (PI) hydrolysis in osteoblast‐like MC3T3‐E1 cells [Miwa et al. (1990): Biochem Biophys Res Commun 171:1229–1235]. In the present study, we investigated the mechanism of PGF 2α ‐induced Ca 2+ influx in MC3T3‐E1 cells. PGF 2α ‐induced formation of total inositol phosphates (IPs) was markedly reduced by the depletion of extracellular Ca 2+ with EGTA. On the other hand, the depletion of extracellular Ca 2+ had little effect on PGF 2α ‐induced inositol 1,4,5‐trisphosphate formation. PGF 2α stimulated 45 Ca 2+ influx dose dependently, attaining a maximum effect at 10 nM. Dose of PGF 2α above 10 nM caused less than maximal stimulation. Genistein, an inhibitor of protein tyrosine kinase, which by itself had little effect on 45 Ca 2+ influx, significantly suppressed the PGF 2α ‐induced 45 Ca 2+ influx in a dose‐dependent manner in the range between 1 μg/ml and 0.1 mg/ml. Sodium orthovanadate, an inhibitor of protein tyrosine phosphatases, enhanced the PGF 2α ‐induced 45 Ca 2+ influx. Genistein also suppressed the PGF 2α ‐induced total IPs formation dose dependently in the range between 1 μg/ml and 0.1 mg/ml. However, it had little effect on the PGF 2α ‐induced inositol 1,4,5‐trisphosphate formation. The pretreatment with pertussis toxin had little effect on the PGF 2α ‐induced 45 Ca 2+ influx. These results strongly suggest that PGF 2α stimulates Ca 2+ mobilization from extracellular space and PI hydrolysis via independent pathways in osteoblast‐like cells, and the PGF 2α ‐induced Ca 2+ influx is regulated by protein tyrosine kinase, resulting in the promotion of PI hydrolysis.

AB - We previously reported that pertussis toxin–sensitive GTP‐binding protein is involved in prostaglandin F 2α (PGF 2α )‐induced phosphoinositide (PI) hydrolysis in osteoblast‐like MC3T3‐E1 cells [Miwa et al. (1990): Biochem Biophys Res Commun 171:1229–1235]. In the present study, we investigated the mechanism of PGF 2α ‐induced Ca 2+ influx in MC3T3‐E1 cells. PGF 2α ‐induced formation of total inositol phosphates (IPs) was markedly reduced by the depletion of extracellular Ca 2+ with EGTA. On the other hand, the depletion of extracellular Ca 2+ had little effect on PGF 2α ‐induced inositol 1,4,5‐trisphosphate formation. PGF 2α stimulated 45 Ca 2+ influx dose dependently, attaining a maximum effect at 10 nM. Dose of PGF 2α above 10 nM caused less than maximal stimulation. Genistein, an inhibitor of protein tyrosine kinase, which by itself had little effect on 45 Ca 2+ influx, significantly suppressed the PGF 2α ‐induced 45 Ca 2+ influx in a dose‐dependent manner in the range between 1 μg/ml and 0.1 mg/ml. Sodium orthovanadate, an inhibitor of protein tyrosine phosphatases, enhanced the PGF 2α ‐induced 45 Ca 2+ influx. Genistein also suppressed the PGF 2α ‐induced total IPs formation dose dependently in the range between 1 μg/ml and 0.1 mg/ml. However, it had little effect on the PGF 2α ‐induced inositol 1,4,5‐trisphosphate formation. The pretreatment with pertussis toxin had little effect on the PGF 2α ‐induced 45 Ca 2+ influx. These results strongly suggest that PGF 2α stimulates Ca 2+ mobilization from extracellular space and PI hydrolysis via independent pathways in osteoblast‐like cells, and the PGF 2α ‐induced Ca 2+ influx is regulated by protein tyrosine kinase, resulting in the promotion of PI hydrolysis.

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