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  • 1
    Electronic Resource
    Electronic Resource
    Cyclic AMP stimulates45Ca-accumulation via synthesis of insulin-like growth factor-I in cultures of osteoblast-like cells (1992)
    Springer
    Journal of bone and mineral metabolism 10 (1992), S. 1-5 
    Details
    ISSN: 1435-5604
    Keywords: Calcium ; Cyclic AMP ; Insulin-like growth factor-I ; Osteoblast
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The effects of cAMP on insulin-like growth factor-I (IGF-I) secretion and45Ca-accumulation into extracellular matrix were investigated in cloned osteoblast-like MC3T3-E1 cells cultured for 7 weeks, which was considered to be long enough to develop calcification. Dibutyryl cAMP stimulated IGF-I secretion dose dependently in the range between 0.1 mM and 3 mM. Dibutyryl cAMP also stimulated accumulation of45Ca into sodium dodecyl sulfate-insoluble, EDTA-extractable materials in cultures of these cells dose dependently between 0.1 mM and 3 mM. The patterns of both stimulations were similar. The dibutyryl cAMP-stimulated IGF-I secretion preceded the45Ca-accumulation. Antibodies to IGF-I suppressed the dibutyryl cAMP-stimulated45Ca-accumulation almost to the control level. Taking account of our previous report that exogenous IGF-I stimulates45Ca-accumulation in cultures of these cells, the present results suggest that cAMP stimulates45Ca-accumulation via synthesis of IGF-I in osteoblast-like cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02378976
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  • 2
    Electronic Resource
    Electronic Resource
    Triiodothyronine stimulates45Ca-accumulation via synthesis of insulin-like growth factor-I in cultures of osteoblast-like cells (1993)
    Springer
    Journal of bone and mineral metabolism 11 (1993), S. 1-6 
    Details
    ISSN: 1435-5604
    Keywords: Calcium ; Triiodothyronine ; Insulin-like growth factor-I ; Osteoblast
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract We examined the effects of triiodothyronine (T3) on45Ca-accumulation into extracellular matrix in osteoblast-like MC3T3-El cells cultured for 7-week period, which was considered to be long enough to develop calcification. T3 increased45Ca-accumulation into sodium dodecyl sulfate-insoluble, EDTA-extractable materials cultures of MC3T3-El cells in a dose-dependent manner in the range between 10 pM and 10 nM. Contrary to the stimulatory effect on45Ca-accumulation, T3 inhibited DNA synthesis in MC3T3-El cells dose dependently between 10 pM and 10 nM. T3 stimulated the secretion of insulin-like growth factor-I (IGF-I) dose dependently between 0.1 nM and 10 nM in MC3T3-El cells cultured for 7 weeks. Antibodies to IGF-I suppressed the45Ca-accumulation induced by T3 almost to the control level. These results strongly suggest that T3 stimulates45Ca-accumulation via synthesis of IGF-I in osteoblast-like cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02383527
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  • 3
    Electronic Resource
    Electronic Resource
    Vasopressin induces arachidonic acid release through pertussis toxin-sensitive GTP-binding protein in aortic smooth muscle cells: Independence from phosphoinositide hydrolysis (1993)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 53 (1993), S. 169-175 
    Details
    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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  • 4
    Electronic Resource
    Electronic Resource
    Effects of vitamin D3 on signaling by prostaglandin E2 in osteoblast-like cells (1993)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 52 (1993), S. 220-226 
    Details
    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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  • 5
    Electronic Resource
    Electronic Resource
    Prostaglandin F2α activates phospholipase D independently from activation of protein kinase C in osteoblast-like cells (1994)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 55 (1994), S. 373-379 
    Details
    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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  • 6
    Electronic Resource
    Electronic Resource
    Glucocorticoid amplifies vasopressin-induced phosphoinositide hydrolysis in aortic smooth muscle cells (1995)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 57 (1995), S. 522-529 
    Details
    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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