Effect of prostaglandin F on Ca2+ 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 Ca2+ influx in MC3T3‐E1 cells. PGF‐induced formation of total inositol phosphates (IPs) was markedly reduced by the depletion of extracellular Ca2+ with EGTA. On the other hand, the depletion of extracellular Ca2+ had little effect on PGF‐induced inositol 1,4,5‐trisphosphate formation. PGF stimulated 45Ca2+ 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 45Ca2+ influx, significantly suppressed the PGF‐induced 45Ca2+ 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 45Ca2+ 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 45Ca2+ influx. These results strongly suggest that PGF stimulates Ca2+ mobilization from extracellular space and PI hydrolysis via independent pathways in osteoblast‐like cells, and the PGF‐induced Ca2+ 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 - 04-1994

Fingerprint

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

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

@article{6d93ee84e3c949cc96001d475736ad71,
title = "Effect of prostaglandin F2α on Ca2+ influx in osteoblast‐like cells: Function of tyrosine kinase",
abstract = "We previously reported that pertussis toxin–sensitive GTP‐binding protein is involved in prostaglandin F2α (PGF2α)‐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 PGF2α‐induced Ca2+ influx in MC3T3‐E1 cells. PGF2α‐induced formation of total inositol phosphates (IPs) was markedly reduced by the depletion of extracellular Ca2+ with EGTA. On the other hand, the depletion of extracellular Ca2+ had little effect on PGF2α‐induced inositol 1,4,5‐trisphosphate formation. PGF2α stimulated 45Ca2+ influx dose dependently, attaining a maximum effect at 10 nM. Dose of PGF2α above 10 nM caused less than maximal stimulation. Genistein, an inhibitor of protein tyrosine kinase, which by itself had little effect on 45Ca2+ influx, significantly suppressed the PGF2α‐induced 45Ca2+ 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 PGF2α‐induced 45Ca2+ influx. Genistein also suppressed the PGF2α‐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 PGF2α‐induced inositol 1,4,5‐trisphosphate formation. The pretreatment with pertussis toxin had little effect on the PGF2α‐induced 45Ca2+ influx. These results strongly suggest that PGF2α stimulates Ca2+ mobilization from extracellular space and PI hydrolysis via independent pathways in osteoblast‐like cells, and the PGF2α‐induced Ca2+ 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",
year = "1994",
month = "4",
doi = "10.1002/jcb.240540416",
language = "English",
volume = "54",
pages = "487--493",
journal = "Journal of Cellular Biochemistry",
issn = "0730-2312",
publisher = "Wiley-Liss Inc.",
number = "4",

}

Effect of prostaglandin F on Ca2+ 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, 04.1994, p. 487-493.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Effect of prostaglandin F2α on Ca2+ influx in osteoblast‐like cells

T2 - Function of tyrosine kinase

AU - Suzuki, Atsushi

AU - Kozawa, Osamu

AU - Saito, Hidehiko

AU - Oiso, Yutaka

PY - 1994/4

Y1 - 1994/4

N2 - We previously reported that pertussis toxin–sensitive GTP‐binding protein is involved in prostaglandin F2α (PGF2α)‐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 PGF2α‐induced Ca2+ influx in MC3T3‐E1 cells. PGF2α‐induced formation of total inositol phosphates (IPs) was markedly reduced by the depletion of extracellular Ca2+ with EGTA. On the other hand, the depletion of extracellular Ca2+ had little effect on PGF2α‐induced inositol 1,4,5‐trisphosphate formation. PGF2α stimulated 45Ca2+ influx dose dependently, attaining a maximum effect at 10 nM. Dose of PGF2α above 10 nM caused less than maximal stimulation. Genistein, an inhibitor of protein tyrosine kinase, which by itself had little effect on 45Ca2+ influx, significantly suppressed the PGF2α‐induced 45Ca2+ 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 PGF2α‐induced 45Ca2+ influx. Genistein also suppressed the PGF2α‐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 PGF2α‐induced inositol 1,4,5‐trisphosphate formation. The pretreatment with pertussis toxin had little effect on the PGF2α‐induced 45Ca2+ influx. These results strongly suggest that PGF2α stimulates Ca2+ mobilization from extracellular space and PI hydrolysis via independent pathways in osteoblast‐like cells, and the PGF2α‐induced Ca2+ 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 F2α (PGF2α)‐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 PGF2α‐induced Ca2+ influx in MC3T3‐E1 cells. PGF2α‐induced formation of total inositol phosphates (IPs) was markedly reduced by the depletion of extracellular Ca2+ with EGTA. On the other hand, the depletion of extracellular Ca2+ had little effect on PGF2α‐induced inositol 1,4,5‐trisphosphate formation. PGF2α stimulated 45Ca2+ influx dose dependently, attaining a maximum effect at 10 nM. Dose of PGF2α above 10 nM caused less than maximal stimulation. Genistein, an inhibitor of protein tyrosine kinase, which by itself had little effect on 45Ca2+ influx, significantly suppressed the PGF2α‐induced 45Ca2+ 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 PGF2α‐induced 45Ca2+ influx. Genistein also suppressed the PGF2α‐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 PGF2α‐induced inositol 1,4,5‐trisphosphate formation. The pretreatment with pertussis toxin had little effect on the PGF2α‐induced 45Ca2+ influx. These results strongly suggest that PGF2α stimulates Ca2+ mobilization from extracellular space and PI hydrolysis via independent pathways in osteoblast‐like cells, and the PGF2α‐induced Ca2+ influx is regulated by protein tyrosine kinase, resulting in the promotion of PI hydrolysis.

UR - http://www.scopus.com/inward/record.url?scp=0028273125&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028273125&partnerID=8YFLogxK

U2 - 10.1002/jcb.240540416

DO - 10.1002/jcb.240540416

M3 - Article

C2 - 8014198

AN - SCOPUS:0028273125

VL - 54

SP - 487

EP - 493

JO - Journal of Cellular Biochemistry

JF - Journal of Cellular Biochemistry

SN - 0730-2312

IS - 4

ER -