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1

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Prostaglandin F2α activates phospholipase D independently from activation of protein kinase C in osteoblast-like cells (1994)

Kozawa, Osamu ; Suzuki, Atsushi ; Kotoyori, Jun ; [et al.]

New York, N.Y. : Wiley-Blackwell

Journal of Cellular Biochemistry 55 (1994), S. 373-379

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ISSN: 0730-2312

Keywords: prostaglandin F2α ; phospholipase D ; protein kinase C ; pertussis toxin ; GTP-binding protein ; osteoblast ; Life and Medical Sciences ; Cell & Developmental Biology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Chemistry and Pharmacology , Medicine

Notes: We previously reported that prostaglandin F2α (PGF2α) receptor is coupled to pertussis toxin (PTX)-sensitive GTP-binding protein (G protein) in osteoblast-like MC3T3-E1 cells [Miwa et al. (1990): Biochem Biophys Res Commun 171:1229-1235]. In the present study, we examined the effect of PGF2α on the activation of phosphatidylcholine-hydrolyzing phospholipase D in MC3T3-E1 cells. PGF2α stimulated the formation of choline in a dose-dependent manner in the range between 10 nM and 10 μM. The formation of choline was stimulated by 12-O-tetradecanoylphorbol-13-acetate (TPA), a protein kinase C (PKC)-activating phorbol ester. 4α-Phorbol 12,13-didecanoate, a PKC-nonactivating phorbol ester, had little effect on choline formation. The formation of choline stimulated by a combination of PGF2α and TPA was additive. Staurosporine, an inhibitor for protein kinases, which inhibited the effect of TPA on choline formation, dose-dependently enhanced the formation of choline induced by PGF2α. NaF, an activator of G protein, stimulated the formation of choline. The formation of choline stimulated by a combination of PGF2α and NaF was not additive. NaF-induced formation of choline was dose-dependently enhanced by staurosporine. PTX dose-dependently inhibited the PGF2α-induced formation of choline. These results strongly suggest that PGF2α activates phospholipase D independently from the activation of PKC in osteoblast-like cells and PTX-sensitive G protein is involved in the PGF2α-induced phospholipase D activation. © 1994 Wiley-Liss, Inc.

Additional Material: 7 Ill.

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URL: http://dx.doi.org/10.1002/jcb.240550315

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2

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Protein kinase C activation amplifies prostaglandin F2α-induced prostaglandin E2 synthesis in osteoblast-like cells (1992)

Tokuda, Haruhiko ; Oiso, Yutaka ; Kozawa, Osamu

New York, N.Y. : Wiley-Blackwell

Journal of Cellular Biochemistry 48 (1992), S. 262-268

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ISSN: 0730-2312

Keywords: protein kinase C ; prostaglandin ; arachidonic acid ; phospholipase A ; osteoblast ; Life and Medical Sciences ; Cell & Developmental Biology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Chemistry and Pharmacology , Medicine

Notes: In cloned osteoblast-like cells, MC3T3-E1, prostaglandin F2α (PGF2α) stimulated arachidonic acid (AA) release in a dose-dependent manner in the range between 1 nM and 10 μM. 12-O-tetradecanoylphorbol-13-acetate (TPA), a protein kinase C (PKC) activator, which by itself had little effect on AA release, markedly amplified the release of AA stimulated by PGF2α in a dose-dependent manner, 4 α-phorbol 12, 13-didecanoate, a phorbol ester which is inactive for PKC, showed little effect on the PGF2α-induced AA release. 1-oleoyl-2-acetylglycerol (OAG), a specific activator for PKC, mimicked TPA by enhancement of the AA release induced by PGF2α. H-7, a PKC inhibitor, markedly suppressed the effect of OAG on PGF2α-induced AA release. Quinacrine, a phospholipase A2 inhibitor, showed partial inhibitory effect on PGF2α-induced AA release, while it suppressed the amplification by OAG of PGF2α-induced AA release almost to the control level. Furthermore, TPA enhanced the AA release induced by melittin, known as a phospholipase A2 activator. On the other hand, TPA inhibited the formation of inositol triphosphate stimulated by PGF2α. Under the same condition, PGF2α indeed stimulated prostaglandin E2 (PGE2) synthesis and TPA markedly amplified the PGF2α-induced PGE2 synthesis as well as AA release. These results indicate that the activation of PKC amplifies PGF2α-induced both AA release and PGE2 synthesis through the potentiation of phospholipase A2 activity in osteoblast-like cells.

Additional Material: 8 Ill.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1002/jcb.240480306

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Glucocorticoid amplifies vasopressin-induced phosphoinositide hydrolysis in aortic smooth muscle cells (1995)

Watanabe, Yasuko ; Tokuda, Haruhiko ; Suzuki, Atsushi ; [et al.]

New York, N.Y. : Wiley-Blackwell

Journal of Cellular Biochemistry 57 (1995), S. 522-529

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ISSN: 0730-2312

Keywords: glucocorticoid ; vasopressin ; angiotensin II ; phosphoinositide ; protein kinase C ; aortic smooth muscle cells ; Life and Medical Sciences ; Cell & Developmental Biology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Chemistry and Pharmacology , Medicine

Notes: It has been reported that glucocorticoid modifies phosphoinositide (PI) hydrolysis stimulated by vasoactive agents in vascular smooth muscle cells. In the present study, we investigated the point at which glucocorticoid affects vasopressin-induced PI hydrolysis in primary cultured rat aortic smooth muscle cells. The pretreatment with dexamethasone significantly amplified the formation of inositol trisphosphate (IP3) induced by vasopressin in a dose-dependent manner in a range of 1 pM to 10 nM. The effect of dexamethasone was dependent on the time of pretreatment up to 8 h. Dexamethasone had little effect on the number of vasopressin receptor and its affinity to vasopressin. The pretreatment with dexamethasone also amplified the formation of IP3 induced by NaF, a GTP-binding protein activator, or angiotensin II. 12-O-Tetradecanoylphorbol-13-acetate, a protein kinase C (PKC)-activating phorbol ester, significantly reduced the dexamethasone-induced enhancement of IP3 formation stimulated by vasopressin, angiotensin II or NaF. 4α-Phorbol-12, 13-didecanoate, a PKC-nonactivating phorbol ester, had little effect on the enhancement by dexamethasone. These results strongly suggest that glucocorticoid amplifies vasopressin-induced PI hydrolysis at a point downstream from GTP-binding protein in primary cultured rat aortic smooth muscle cells, and that the activation of PKC has a negative feedback effect on the amplification by glucocorticoid of vasopressin-induced PI hydrolysis.

Additional Material: 7 Ill.

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URL: http://dx.doi.org/10.1002/jcb.240570317

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Vasopressin induces arachidonic acid release through pertussis toxin-sensitive GTP-binding protein in aortic smooth muscle cells: Independence from phosphoinositide hydrolysis (1993)

Ito, Yoshiaki ; Kozawa, Osamu ; Tokuda, Haruhiko ; [et al.]

New York, N.Y. : Wiley-Blackwell

Journal of Cellular Biochemistry 53 (1993), S. 169-175

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ISSN: 0730-2312

Keywords: arachidonic acid ; phospholipase A2 ; phosphoinositide ; phospholipase C ; GTP-binding protein ; pertussis toxin ; Life and Medical Sciences ; Cell & Developmental Biology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Chemistry and Pharmacology , Medicine

Notes: We previously reported that pertussis toxin (PTX) had little effect on arginine vasopressin-induced formation of inositol trisphosphate (IP3) in rat aortic smooth muscle cells [Kondo et al.: Biochemical and Biophysical Research Communications 161:677-682, 1989]. In the present study, we investigated the mechanism of vasopressin-induced arachidonic acid release in rat aortic smooth muscle cells. Vasopressin stimulated both the release of arachidonic acid and the formation of IP3 dose dependently in the range between 10 pM and 1 μM. The effect of vasopressin on arachidonic acid release was more potent than that on the formation of IP3. Quinacrine, a phospholipase A2 inhibitor, significantly suppressed the vasopressin-induced arachidonic acid release but had little effect on the formation of inositol phosphates. NaF, a GTP-binding protein activator, mimicked vasopressin by stimulating the arachidonic acid release. The arachidonic acid release stimulated by a combination of vasopressin and NaF was not additive. PTX partially but significantly suppressed the vasopressin-induced arachidonic acid release. In the cell membranes, PTX catalyzed ADP-ribosylation of a protein with an Mr of about 40,000. Pretreatment of membranes with 0.1 μM vasopressin in the presence of 2.5 mM MgCl2 and 100 μM GTP markedly attenuated this PTX-catalyzed ADP-ribosylation of the protein in a time-dependent manner. These results strongly suggest that PTX-sensitive GTP-binding protein is involved in the coupling of vasopressin receptor to phospholipase A2 in primary cultured rat aortic smooth muscle cells.

Additional Material: 7 Ill.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1002/jcb.240530210

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Effects of vitamin D3 on signaling by prostaglandin E2 in osteoblast-like cells (1993)

Tokuda, Haruhiko ; Kotoyori, Jun ; Suzuki, Atsushi ; [et al.]

New York, N.Y. : Wiley-Blackwell

Journal of Cellular Biochemistry 52 (1993), S. 220-226

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ISSN: 0730-2312

Keywords: vitamin D3 ; prostaglandin E2 ; cAMP ; phosphoinositide ; GTP-binding protein ; osteoblast ; Life and Medical Sciences ; Cell & Developmental Biology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Chemistry and Pharmacology , Medicine

Notes: We investigated the effects of vitamin D3 on the signaling pathways by prostaglandin E2 (PGE2) in osteoblast-like MC3T3-E1 cells. The pretreatment with 1,25-dihydroxyvitamin D3 (1,25-(OH)2D3), an active form of vitamin D3, significantly inhibited cAMP accumulation induced by 10 μM PGE2 in a dose-dependent manner in the range between 1 pM and 1 nM. This effect of 1,25-(OH)2D3 was dependent on the time of pretreatment up to 8 h. 1,25-(OH)2D3 also inhibited the cAMP accumulation induced by NaF, a GTP-binding protein activator, or forskolin which directly activates adenylate cyclase. On the other hand, 1,25-(OH)2D3 significantly inhibited PGE2-induced IP3 formation in a dose-dependent manner between 10 pM and 1 nM. However, 1,25-(OH)2D3 had little effect on NaF-induced IP3 formation. The pretreatment with 24,25-dihydroxyvitamin D3, an inactive form of vitamin D3, affected neither cAMP accumulation nor IP3 formation induced by PGE2. These results strongly suggest that 1,25-(OH)2D3 modulates the signaling by PGE2 in osteoblast-like cells as follows: the inhibitory effect on the cAMP production is exerted at a point downstream from adenylate cyclase and the inhibitory effect on the phosphoinositide hydrolysis is exerted at the point between the PGE2 receptor and GTP-binding protein, probably Gi2.

Additional Material: 6 Ill.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1002/jcb.240520213

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Protein kinase C activation by interleukin (IL)-1 limits IL-1-induced IL-6 synthesis in osteoblast-like cells: Involvement of phosphatidylcholine-specific phospholipase C (1997)

Kozawa, Osamu ; Suzuki, Atsushi ; Tokuda, Haruhiko ; [et al.]

New York, N.Y. : Wiley-Blackwell

Journal of Cellular Biochemistry 67 (1997), S. 103-111

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ISSN: 0730-2312

Keywords: interleukin-1 ; interleukin-6 ; protein kinase C ; phosphatidylcholine ; phospholipase C ; osteoblast ; Life and Medical Sciences ; Cell & Developmental Biology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Chemistry and Pharmacology , Medicine

Notes: We investigated the regulatory mechanism of interleukin-6 (IL-6) synthesis induced by interleukin-1 (IL-1) in osteoblast-like MC3T3-E1 cells. IL-1 stimulated the secretion of IL-6 in a dose-dependent manner in the range between 0.1 and 100 ng/ml. Staurosporine and calphostin C, inhibitors of protein kinase C (PKC), significantly enhanced the IL-1-induced secretion of IL-6. The stimulative effect of IL-1 was markedly amplified in PKC down-regulated MC3T3-E1 cells. IL-1 produced diacylglycerol in MC3T3-E1 cells. IL-1 had little effect on the formation of inositol phosphates and choline. On the contrary, IL-1 significantly stimulated the formation of phosphocholine dose-dependently. D-609, an inhibitor of phosphatidylcholine-specific phospholipase C, suppressed the IL-1-induced diacylglycerol production. The IL-1-induced IL-6 secretion was significantly enhanced by D-609. These results indicate that IL-1 activates PKC via phosphatidylcholine-specific phospholipase C in osteoblast-like cells, and the PKC activation then limits IL-6 synthesis induced by IL-1 itself. J. Cell. Biochem. 67:103-111, 1997. © 1997 Wiley-Liss, Inc.

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Tiludronate inhibits interleukin-6 synthesis in osteoblasts: Inhibition of phospholipase D activation in MC3T3-E1 cells (1998)

Tokuda, Haruhiko ; Kozawa, Osamu ; Harada, Atsushi ; [et al.]

New York, N.Y. : Wiley-Blackwell

Journal of Cellular Biochemistry 69 (1998), S. 252-259

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ISSN: 0730-2312

Keywords: bisphosphonate ; prostaglandin F2α ; interleukin-6 ; phospholipase D ; osteoblast ; Life and Medical Sciences ; Cell & Developmental Biology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Chemistry and Pharmacology , Medicine

Notes: In previous studies, we have reported that PGF2α stimulates phosphoinositide hydrolysis by phospholipase C and phosphatidylcholine hydrolysis by phospholipase D through heterotrimeric GTP-binding protein in osteoblast-like MC3T3-E1 cells, and that PGF2α and PGE1 induce interleukin-6 (IL-6) synthesis via activation of protein kinase C and protein kinase A, respectively. In the present study, we investigated the effect of tiludronate, a bisphosphonate known to inhibit bone resorption, on the PGF2α- and PGE1-induced IL-6 synthesis in these cells. Tiludronate significantly suppressed the PGF2α-induced IL-6 secretion in a dose-dependent manner in the range between 0.1 and 30 μM. However, the IL-6 secretion induced by PGE1 or (Bu)2cAMP was hardly affected by tiludronate. The choline formation induced by PGF2α was reduced by tiludronate dose-dependently in the range between 0.1 and 30 μM. On the contrary, tiludronate had no effect on PGF2α-induced formation of inositol phosphates. Tiludronate suppressed the choline formation induced by NaF, known as an activator of heterotrimeric GTP-binding protein. However, tiludronate had little effect on the formation of choline induced by TPA, a protein kinase C activator. Tiludronate significantly inhibited the NaF-induced IL-6 secretion in human osteoblastic osteosarcoma Saos-2 cells. These results strongly suggest that tiludronate inhibits PGF2α-induced IL-6 synthesis via suppression of phosphatidylcholine-hydrolyzing phospholipase D activation in osteoblasts, and that the inhibitory effect is exerted at the point between heterotrimeric GTP-binding protein and phospholipase D. J. Cell. Biochem. 69:252-259, 1998. © 1998 Wiley-Liss, Inc.

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Sphingosine modulates interleukin-6 synthesis in osteoblasts (1998)

Kozawa, Osamu ; Tokuda, Haruhiko ; Matsuno, Hiroyuki ; [et al.]

New York, N.Y. : Wiley-Blackwell

Journal of Cellular Biochemistry 70 (1998), S. 338-345

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ISSN: 0730-2312

Keywords: sphingosine ; interleukin-6 ; osteoblast ; Life and Medical Sciences ; Cell & Developmental Biology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Chemistry and Pharmacology , Medicine

Notes: We previously reported that prostaglandin (PG)E1 and PGF2α induce the synthesis of interleukin-6 (IL-6) via activation of protein kinase (PK)A and PKC, respectively, in osteoblast-like MC3T3-E1 cells. In addition, we have shown that basic fibroblast growth factor (bFGF) elicits IL-6 synthesis through intracellular Ca2+ mobilization in these cells and that tumor necrosis factor-α (TNF) induces IL-6 synthesis through sphingosine 1-phosphate produced by sphingomyelin hydrolysis. In the present study, among sphingomyelin metabolites, we examined the effect of sphingosine on IL-6 synthesis induced by various agonists in MC3T3-E1 cells. Sphingosine inhibited the IL-6 synthesis induced by PGF2α or 12-O-tetradecanoylphorbol-13-acetate, an activator of PKC. Sphingosine suppressed the PGE1-induced IL-6 synthesis. The IL-6 synthesis induced by cholera toxin, forskolin, or dibutyryl cAMP was inhibited by sphingosine. Sphingosine inhibited the IL-6 synthesis induced by bFGF or A23187. However, sphingosine did not affect the IL-6 synthesis induced by interleukin-1. On the contrary, sphingosine enhanced the TNF-induced IL-6 synthesis. DL-threo-Dihydrosphingosine, an inhibitor of sphingosine kinase, reduced the enhancement by sphingosine as well as the TNF-effect. These results indicate that sphingosine modulates the IL-6 synthesis stimulated by various agonists in osteoblasts. J. Cell. Biochem. 70:338-345. © 1998 Wiley-Liss, Inc.

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