Prostaglandin F(2α) stimulates interleukin-6 synthesis via activation of PKC in osteoblast-like cells

Osamu Kozawa, Atsushi Suzuki, Haruhiko Tokuda, Toshihiko Uematsu

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Abstract

In previous studies, we reported that prostaglandin F(2α) (PGF(2α)) stimulates phosphoinositide hydrolysis by phospholipase C and phosphatidylcholine hydrolysis by phospholipase D in osteoblast-like MC3T3- E1 cells. In the present study, we examined the effect of PGF(2α) on synthesis of interleukin-6 (IL-6) and the involvement of protein kinase C (PKC) activation in the IL-6 synthesis in these cells. PGF(2α) significantly stimulated IL-6 synthesis in a dose-dependent manner in the range between 10 nM and 10 μM. A PKC-activating phorbol ester, 12-O-tetradecanoylphorbol-13- acetate (TPA), induced IL-6 synthesis. On the contrary, 4α-phorbol 12,13- didecanoate, a PKC-nonactivating phorbol ester, had no effect. The synthesis of IL-6 stimulated by a combination of PGF(2α) and TPA was not additive. Staurosporine, an inhibitor for protein kinases that suppressed the TPA- induced IL-6 synthesis, significantly inhibited the PGF(2α)-induced IL-6 synthesis. Calphostin C, a highly specific PKC inhibitor, also suppressed the PGF(2α)-stimulated synthesis of IL-6. The effect of PGF(2α) on IL-6 synthesis in PKC-downregulated cells was much weaker than that in intact cells. These results strongly suggest that PGF(2α) induces IL-6 synthesis via PKC activation in osteoblast-like cells.

Original languageEnglish
JournalAmerican Journal of Physiology - Endocrinology and Metabolism
Volume272
Issue number2 35-2
Publication statusPublished - 01-02-1997
Externally publishedYes

Fingerprint

Prostaglandins F
Osteoblasts
Protein Kinase C
Interleukin-6
Tetradecanoylphorbol Acetate
Phorbol Esters
Protein Kinase Inhibitors
Hydrolysis
Phosphoinositide Phospholipase C
Phospholipase D
Staurosporine
Protein C Inhibitor
Phosphatidylcholines
Down-Regulation

All Science Journal Classification (ASJC) codes

  • Endocrinology, Diabetes and Metabolism
  • Physiology
  • Physiology (medical)

Cite this

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title = "Prostaglandin F(2α) stimulates interleukin-6 synthesis via activation of PKC in osteoblast-like cells",
abstract = "In previous studies, we reported that prostaglandin F(2α) (PGF(2α)) stimulates phosphoinositide hydrolysis by phospholipase C and phosphatidylcholine hydrolysis by phospholipase D in osteoblast-like MC3T3- E1 cells. In the present study, we examined the effect of PGF(2α) on synthesis of interleukin-6 (IL-6) and the involvement of protein kinase C (PKC) activation in the IL-6 synthesis in these cells. PGF(2α) significantly stimulated IL-6 synthesis in a dose-dependent manner in the range between 10 nM and 10 μM. A PKC-activating phorbol ester, 12-O-tetradecanoylphorbol-13- acetate (TPA), induced IL-6 synthesis. On the contrary, 4α-phorbol 12,13- didecanoate, a PKC-nonactivating phorbol ester, had no effect. The synthesis of IL-6 stimulated by a combination of PGF(2α) and TPA was not additive. Staurosporine, an inhibitor for protein kinases that suppressed the TPA- induced IL-6 synthesis, significantly inhibited the PGF(2α)-induced IL-6 synthesis. Calphostin C, a highly specific PKC inhibitor, also suppressed the PGF(2α)-stimulated synthesis of IL-6. The effect of PGF(2α) on IL-6 synthesis in PKC-downregulated cells was much weaker than that in intact cells. These results strongly suggest that PGF(2α) induces IL-6 synthesis via PKC activation in osteoblast-like cells.",
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Prostaglandin F(2α) stimulates interleukin-6 synthesis via activation of PKC in osteoblast-like cells. / Kozawa, Osamu; Suzuki, Atsushi; Tokuda, Haruhiko; Uematsu, Toshihiko.

In: American Journal of Physiology - Endocrinology and Metabolism, Vol. 272, No. 2 35-2, 01.02.1997.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Prostaglandin F(2α) stimulates interleukin-6 synthesis via activation of PKC in osteoblast-like cells

AU - Kozawa, Osamu

AU - Suzuki, Atsushi

AU - Tokuda, Haruhiko

AU - Uematsu, Toshihiko

PY - 1997/2/1

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N2 - In previous studies, we reported that prostaglandin F(2α) (PGF(2α)) stimulates phosphoinositide hydrolysis by phospholipase C and phosphatidylcholine hydrolysis by phospholipase D in osteoblast-like MC3T3- E1 cells. In the present study, we examined the effect of PGF(2α) on synthesis of interleukin-6 (IL-6) and the involvement of protein kinase C (PKC) activation in the IL-6 synthesis in these cells. PGF(2α) significantly stimulated IL-6 synthesis in a dose-dependent manner in the range between 10 nM and 10 μM. A PKC-activating phorbol ester, 12-O-tetradecanoylphorbol-13- acetate (TPA), induced IL-6 synthesis. On the contrary, 4α-phorbol 12,13- didecanoate, a PKC-nonactivating phorbol ester, had no effect. The synthesis of IL-6 stimulated by a combination of PGF(2α) and TPA was not additive. Staurosporine, an inhibitor for protein kinases that suppressed the TPA- induced IL-6 synthesis, significantly inhibited the PGF(2α)-induced IL-6 synthesis. Calphostin C, a highly specific PKC inhibitor, also suppressed the PGF(2α)-stimulated synthesis of IL-6. The effect of PGF(2α) on IL-6 synthesis in PKC-downregulated cells was much weaker than that in intact cells. These results strongly suggest that PGF(2α) induces IL-6 synthesis via PKC activation in osteoblast-like cells.

AB - In previous studies, we reported that prostaglandin F(2α) (PGF(2α)) stimulates phosphoinositide hydrolysis by phospholipase C and phosphatidylcholine hydrolysis by phospholipase D in osteoblast-like MC3T3- E1 cells. In the present study, we examined the effect of PGF(2α) on synthesis of interleukin-6 (IL-6) and the involvement of protein kinase C (PKC) activation in the IL-6 synthesis in these cells. PGF(2α) significantly stimulated IL-6 synthesis in a dose-dependent manner in the range between 10 nM and 10 μM. A PKC-activating phorbol ester, 12-O-tetradecanoylphorbol-13- acetate (TPA), induced IL-6 synthesis. On the contrary, 4α-phorbol 12,13- didecanoate, a PKC-nonactivating phorbol ester, had no effect. The synthesis of IL-6 stimulated by a combination of PGF(2α) and TPA was not additive. Staurosporine, an inhibitor for protein kinases that suppressed the TPA- induced IL-6 synthesis, significantly inhibited the PGF(2α)-induced IL-6 synthesis. Calphostin C, a highly specific PKC inhibitor, also suppressed the PGF(2α)-stimulated synthesis of IL-6. The effect of PGF(2α) on IL-6 synthesis in PKC-downregulated cells was much weaker than that in intact cells. These results strongly suggest that PGF(2α) induces IL-6 synthesis via PKC activation in osteoblast-like cells.

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