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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.

Type of Medium: Electronic Resource

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

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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.

Type of Medium: Electronic Resource

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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CBFa(AML/PEBP2)-related elements in the TGF-β type I receptor promoter and expression with osteoblast differentiation (1998)

Ji, Changhua ; Casinghino, Sandra ; Chang, David J. ; [et al.]

New York, N.Y. : Wiley-Blackwell

Journal of Cellular Biochemistry 69 (1998), S. 353-363

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ISSN: 0730-2312

Keywords: AML/CBF/PEBP2 ; CBFa1 ; differentiation ; osteoblasts ; regulatory elements ; transforming growth factor-β ; receptor ; Life and Medical Sciences ; Cell & Developmental Biology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Chemistry and Pharmacology , Medicine

Notes: Organization of the transforming growth factor-β (TGF-β) type I receptor (TRI) promoter predicts constitutive transcription, although its activity increases with differentiation status in cultured osteoblasts. Several sequences in the rat TRI promoter comprise cis-acting elements for CBFa (AML/PEBP2α) transcription factors. By gel mobility shift and immunological analyses, a principal osteoblast-derived nuclear factor that binds to these sites is CBFa1(AML-3/PEBP2αA). Rat CBFa1 levels parallel expression of the osteoblast phenotype and increase under conditions that promote mineralized bone nodule formation in vitro. Fusion of CBFa binding sequence from the TRI promoter to enhancer-free transfection vector increases reporter gene expression in cells that possess abundant CBFa1, and overexpression of CBFa increase the activity of transfected native TRI promoter/reporter plasmid. Consequently, phenotype-restricted use of cis-acting elements for CBFa transcription factors can contribute to the high levels of TRI that parallel osteoblast differentiation and to the potent effects of TGF-β on osteoblast function. J. Cell. Biochem. 69:353-363. © 1998 Wiley-Liss, Inc.

Additional Material: 7 Ill.

Type of Medium: Electronic Resource

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Identification of subnanometre surface layers on polymer films by surface-enhanced infrared transmission spectroscopy (1992)

Nishikawa, Yuji ; Ito, Yoshiaki ; Yamakami, Noriko ; [et al.]

Chichester [u.a.] : Wiley-Blackwell

Surface and Interface Analysis 18 (1992), S. 481-486

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ISSN: 0142-2421

Keywords: Chemistry ; Polymer and Materials Science

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Physics

Notes: Identification of subnanometre surface layers on polymer films, which are only analysable by x-ray photoelectron spectroscopy (XPS) or secondary ion mass spectrometry (SIMS), have been demonstrated by the use of transmission surface-enhanced infrared absorption (SEIRA) spectroscopy with the use of silver island films: 1.0 nm thick polydimethylsiloxane (PDMS) or 0.5 nm thick polymethylphenylsiloxane (PMPHS) surface layers, which are semisolid materials, on polyethyleneterephthalate (PET) films were successfully identifiable with the use of transmission SEIRA by measuring the PDMS or PMPHS that was transferred onto the silver-deposited BaF2 substrates under pressure. This approach completely eliminates strong spectral interference from PET films by measuring the transferred surface layer and greatly improves the signal-to-noise ratio of the surface layer absorption with the use of silver island films. The detection limit of PDMS surface layers on PET films is ∼0.2 nm. The present method gives a considerable amount of information about surfaces, such as chemical composition and chemical structure. This is a highly promising method for analysiing subnanometre surface layers which consist of liquid or semisolid materials, such as oil, lubricant, plasticizer and surface-active agent on polymer materials.

Additional Material: 7 Ill.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1002/sia.740180704

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