Cross-talk regulation between cyclic AMP production and phosphoinositide hydrolysis induced by prostaglandin E2 in osteoblast-like cells

Kozawa, Osamu; Tokuda, Harukuni; Miwa, Masaichi; Kotoyori, Jun; Oiso, Yutaka

doi:10.1016/0014-4827(92)90158-5

Cited by 162 publications

(87 citation statements)

References 19 publications

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“…We previously reported that PGE2 stimulates cAMP accumulation dose dependently in the range between 1 nM and 10 µM in MC3T3-E1 cells and that cAMP accumulation reaches a peak at 5 min and decreases thereafter [17]. As shown in the previous study, 10 µM PGE2 caused a significant increase in cAMP accumulation, while bradykinin had little effect on cAMP accumulation in MC3T3-E1 cells (Table 1).…”

Section: Effect Of Bradykinin On Camp Accumulation In Mc3t3-e1 Cells:supporting

confidence: 65%

“…We have also demonstrated that both PGE2-induced cAMP production and Ca2+ influx are autoregulated due to the activation of protein kinase C, resulting from PI hydrolysis [17,18]. In the present study, we compared the intracellular signaling systems of two bone resorbing agents, PGE2 and bradykinin [2,3], in these cells.…”

Section: Discussionmentioning

confidence: 80%

“…Moreover, in recent studies [17,18], we have demonstrated that PGE2 induces PI hydrolysis, cAMP production and Ca2+ influx in these cells, and these dose-dependencies are different to one another. We have also shown that both PGE2-induced cAMP production and Ca2+ influx are autoregulated due to the activation of protein kinase C, resulting from PI hydrolysis in these cells [17,18]. However, the details of intracellular signaling of various bone resorbing agents has not yet been clarified.…”

Section: Bradykininmentioning

confidence: 83%

“…We previously reported that PGE2, known as a potent bone resorbing agent [11], induces Ca2+ influx in addition to cAMP production and PI hydrolysis in osteoblast-like MC3T3-E1 cells [16][17][18], and the dose-dependent curves of PGE2-induced PI hydrolysis, cAMP production and Ca2+influx are different to one another [16][17][18]. We have also demonstrated that both PGE2-induced cAMP production and Ca2+ influx are autoregulated due to the activation of protein kinase C, resulting from PI hydrolysis [17,18].…”

Section: Discussionmentioning

confidence: 99%

“…We previously showed that PGE2 stimulates PI hydrolysis in a dose-dependent manner in the range between 1 nM and 10 µM in MC3T3-E1 cells [17]. The maximum effect of PGE2 is observed at 10 pM and ECM on the inositol trisphosphate formation by PGE2 is 0.8 µM.…”

Section: Effect Of Bradykinin On Camp Accumulation In Mc3t3-e1 Cells:mentioning

confidence: 94%

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Intracellular Signaling Mechanism of Bradykinin in Osteoblast-Like Cells: Comparison with Prostaglandin E2.

et al. 1994

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Section: Effect Of Bradykinin On Camp Accumulation In Mc3t3-e1 Cells:supporting

confidence: 65%

Section: Discussionmentioning

confidence: 80%

Section: Bradykininmentioning

confidence: 83%

Section: Discussionmentioning

confidence: 99%

Section: Effect Of Bradykinin On Camp Accumulation In Mc3t3-e1 Cells:mentioning

confidence: 94%

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Intracellular Signaling Mechanism of Bradykinin in Osteoblast-Like Cells: Comparison with Prostaglandin E2.

et al. 1994

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Protein kinase C activation inhibits stress‐induced synthesis of heat shock protein 27 in osteoblast‐like cells: Function of arachidonic acid

et al. 1996

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Exposure of osteoblast-like MC3T3-E1 cells to sodium arsenite (arsenite) increased the level of heat shock protein 27 (hsp27). The effect of arsenite was dose-dependent in the range of 50 to 200 microM. Arsenite also stimulated arachidonic acid release dose-dependently in the range between 50 and 200 microM in these cells. Both indomethacin, an inhibitor of cyclooxygenase, and nordihydroguaiaretic acid, a lipoxygenase inhibitor, significantly enhanced the arsenite-induced accumulation of hsp27. Melittin, an activator of phospholipase A2, significantly enhanced the arsenite-induced accumulation of hsp27. 12-O-Tetradecanoylphorbol-13-acetate (TPA), a protein kinase C (PKC)-activating phorbol ester, inhibited the arsenite-induced accumulation of hsp27. In contrast, 4 alpha-phorbol 12,13-didecanoate (4 alpha-PDD), a PKC-nonactivating phorbol ester, had little effect. TPA suppressed the arsenite-induced arachidonic acid release, but 4 alpha-PDD had little effect. Arsenite no longer affected cAMP accumulation, inositol phosphates formation nor the formation of choline and phosphocholine in these cells. These results suggest that the response to stress of hsp27 is coupled with the metabolic activity of the arachidonic acid cascade, and the activation of PKC inhibits the induction of hsp27 through the suppression of arachidonic acid release in osteoblast-like cells.

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Protein kinases A and C positively regulate G protein-dependent activation of phosphatidylinositol-specific phospholipase C by tumor necrosis factor-alpha in MC3T3-E1 osteoblasts

Rapuano

Bockman

1997

J. Cell. Biochem.

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The role(s) of protein kinases in the regulation of G protein-dependent activation of phosphatidylinositol-specific phospholipase C by tumor necrosis factor-alpha was investigated in the osteoblast cell line MC3T3-E1. We have previously reported the stimulatory effects of tumor necrosis factor-alpha and A1F4-, an activator of G proteins, on this phospholipase pathway documented by a decrease in mass of PI and release of diacylglycerol. In this study, we further explored the mechanism(s) by which the tumor necrosis factor or A1F4(-)-promoted breakdown of phosphatidylinositol and the polyphosphoinositides by phospholipase C is regulated. Tumor necrosis factor-alpha was found to elicit a 4-5-fold increase in the formation of [3H]inositol-1,4-phosphate and [3H]inositol-1,4,5-phosphate; and a 36% increase in [3H]inositol-1-phosphate within 5 min in prelabeled cells. [3H]inositol-4-phosphate, a metabolite of [3H]inositol-1,4-phosphate and [3H]inositol-1,4,5-phosphate, was found to be the predominant phosphoinositol product of tumor necrosis factor-alpha and A1F4(-)-activated phospholipase C hydrolysis after 30 min. In addition, the preincubation of cells with pertussis toxin decreased the tumor necrosis factor-induced release of inositol phosphates by 53%. Inhibitors of protein kinase C, including Et-18-OMe and H-7, dramatically decreased the formation of [3H]inositol phosphates stimulated by either tumor necrosis factor-alpha or A1F4- by 90-100% but did not affect basal formation. The activation of cAMP-dependent protein kinase, or protein kinase A, by the treatment of cells with forskolin or 8-BrcAMP augmented basal, tumor necrosis factor-alpha and A1F4(-)-induced [3H]inositol phosphate formation. Therefore, we report that protein kinases can regulate tumor necrosis factor-alpha-initiated signalling at the cell surface in osteoblasts through effects on the coupling between receptor, G-protein and phosphatidylinositol-specific phospholipase C.

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Cross-talk regulation between cyclic AMP production and phosphoinositide hydrolysis induced by prostaglandin E2 in osteoblast-like cells

Cited by 162 publications

References 19 publications

Intracellular Signaling Mechanism of Bradykinin in Osteoblast-Like Cells: Comparison with Prostaglandin E2.

Intracellular Signaling Mechanism of Bradykinin in Osteoblast-Like Cells: Comparison with Prostaglandin E2.

Protein kinase C activation inhibits stress‐induced synthesis of heat shock protein 27 in osteoblast‐like cells: Function of arachidonic acid

Protein kinases A and C positively regulate G protein-dependent activation of phosphatidylinositol-specific phospholipase C by tumor necrosis factor-alpha in MC3T3-E1 osteoblasts

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