메뉴 건너뛰기




Volumn 40, Issue 3, 1998, Pages 564-572

Identification of phospholipase C β isoforms and their location in cultured vascular smooth muscle cells of pig, human and rat

Author keywords

Confocal microscopy; Human; Intracellular localisation; Phospholipase C; Pig; Rat; Vascular smooth muscle cell cultures

Indexed keywords

ISOENZYME; PHOSPHOLIPASE C;

EID: 0032402404     PISSN: 00086363     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0008-6363(98)00193-X     Document Type: Article
Times cited : (19)

References (38)
  • 1
    • 0030995012 scopus 로고    scopus 로고
    • Regulation of phosphoinositide-specific phospholipase C isoenzymes
    • Rhee S.G., Bae Y.S. Regulation of phosphoinositide-specific phospholipase C isoenzymes. J Biol Chem. 272:1997;15045-15048.
    • (1997) J Biol Chem , vol.272 , pp. 15045-15048
    • Rhee, S.G.1    Bae, Y.S.2
  • 2
    • 0029743335 scopus 로고    scopus 로고
    • Phospholipase C isoforms in vascular smooth muscle and their regulation by G-proteins
    • Blayney L.M., Gapper P.W., Newby A.C. Phospholipase C isoforms in vascular smooth muscle and their regulation by G-proteins. Br J Pharmacol. 118:1996;1003-1011.
    • (1996) Br J Pharmacol , vol.118 , pp. 1003-1011
    • Blayney, L.M.1    Gapper, P.W.2    Newby, A.C.3
  • 3
    • 0029936331 scopus 로고    scopus 로고
    • Regulation of phosphoinositide phospholipases by hormones, neurotransmitters and other agonists linked to G-proteins
    • Exton J.H. Regulation of phosphoinositide phospholipases by hormones, neurotransmitters and other agonists linked to G-proteins. Ann Rev Pharmacol Toxicol. 36:1996;481-509.
    • (1996) Ann Rev Pharmacol Toxicol , vol.36 , pp. 481-509
    • Exton, J.H.1
  • 4
    • 0031022712 scopus 로고    scopus 로고
    • CCK, carbachol, and bombesin activate distinct PLC-13 isoenzymes via Gq/11 in rat pancreatic acinar membranes
    • Piper A., Stryjek-Kaminska D., Klengel R., Zeuzem S. CCK, carbachol, and bombesin activate distinct PLC-13 isoenzymes via Gq/11 in rat pancreatic acinar membranes. Am J Physiol. 272:1997;G135-G140.
    • (1997) Am J Physiol , vol.272
    • Piper, A.1    Stryjek-Kaminska, D.2    Klengel, R.3    Zeuzem, S.4
  • 7
    • 0030978912 scopus 로고    scopus 로고
    • Phospholipase C β and membrane action of calcitrol and estradiol
    • Le Mellay V., Grosse B., Lieberherr M. Phospholipase C β and membrane action of calcitrol and estradiol. J Biol Chem. 272:1997;11902-11907.
    • (1997) J Biol Chem , vol.272 , pp. 11902-11907
    • Le Mellay, V.1    Grosse, B.2    Lieberherr, M.3
  • 8
    • 0027936892 scopus 로고
    • Membrane organization in G-protein mechanisms
    • Neubig R.R. Membrane organization in G-protein mechanisms. FASEB J. 8:1994;939-946.
    • (1994) FASEB J , vol.8 , pp. 939-946
    • Neubig, R.R.1
  • 9
    • 0027337113 scopus 로고
    • Phosphoinositidase C isoforms are specifically localized in the nuclear matrix and the cytoskeleton of Swiss 3T3 cells
    • Zini N., Martelli A.M., Cocco L., Manzoli F.A., Maraldi N.M. Phosphoinositidase C isoforms are specifically localized in the nuclear matrix and the cytoskeleton of Swiss 3T3 cells. Exp Cell Res. 208:1993;257-269.
    • (1993) Exp Cell Res , vol.208 , pp. 257-269
    • Zini, N.1    Martelli, A.M.2    Cocco, L.3    Manzoli, F.A.4    Maraldi, N.M.5
  • 10
    • 0025925359 scopus 로고
    • c-src, phospholipase C, inositol lipid and diacylglycerol kinases with the cytoskeletons of thrombin-stimulated platelets
    • c-src, phospholipase C, inositol lipid and diacylglycerol kinases with the cytoskeletons of thrombin-stimulated platelets. J Biol Chem. 266:1991;15705-15709.
    • (1991) J Biol Chem , vol.266 , pp. 15705-15709
    • Grondin, P.1    Plantavid, M.2    Sultan, C.3    Breton, M.4    Mauco, G.5    Chap, H.6
  • 11
    • 0026705818 scopus 로고
    • Discrete subcellular localization of phosphoinositidase C β, γ, and δ in PC12 rat pheochromocytoma cells
    • Mazzoni M., Bertagnolo V., Neri L.M.et al. Discrete subcellular localization of phosphoinositidase C β, γ, and δ in PC12 rat pheochromocytoma cells. Biochem Biophys Res Commun. 187:1992;114-120.
    • (1992) Biochem Biophys Res Commun , vol.187 , pp. 114-120
    • Mazzoni, M.1    Bertagnolo, V.2    Neri, L.M.3
  • 12
    • 0028303835 scopus 로고
    • Phosphoinositide signaling in nuclei of friend cells: Phospholipase C β down-regulation is related to cell differentiation
    • Martelli A.M., Billi A., Gilmour R.S.et al. Phosphoinositide signaling in nuclei of friend cells: Phospholipase C β down-regulation is related to cell differentiation. Cancer Res. 54:1994;2536-2540.
    • (1994) Cancer Res , vol.54 , pp. 2536-2540
    • Martelli, A.M.1    Billi, A.2    Gilmour, R.S.3
  • 14
    • 0027282799 scopus 로고
    • Immunocytochemical analysis of phosphatidylinositol-specific phospholipase-C in PC12-cells - Predominance of the δ isoform during neural differentiation
    • Neri L.M., Milani D., Marchisio M.et al. Immunocytochemical analysis of phosphatidylinositol-specific phospholipase-C in PC12-cells - Predominance of the δ isoform during neural differentiation. Histochemistry. 100:1993;121-129.
    • (1993) Histochemistry , vol.100 , pp. 121-129
    • Neri, L.M.1    Milani, D.2    Marchisio, M.3
  • 16
    • 0022568961 scopus 로고
    • Expression of smooth muscle-specific cx isoactin in cultured vascular smooth muscle cells: Relationship between growth and cytodifferentiation
    • Owens G.K., Loeb A., Gordon D., Thompson M.M. Expression of smooth muscle-specific cx isoactin in cultured vascular smooth muscle cells: relationship between growth and cytodifferentiation. J Cell Biol. 102:1986;343-352.
    • (1986) J Cell Biol , vol.102 , pp. 343-352
    • Owens, G.K.1    Loeb, A.2    Gordon, D.3    Thompson, M.M.4
  • 17
    • 0024462447 scopus 로고
    • A novel 58-kDa protein associates with the Golgi apparatus and microtubules
    • Bloom G.S., Brashear T.A. A novel 58-kDa protein associates with the Golgi apparatus and microtubules. J Biol Chem. 264:1989;16083-16092.
    • (1989) J Biol Chem , vol.264 , pp. 16083-16092
    • Bloom, G.S.1    Brashear, T.A.2
  • 19
    • 0030600130 scopus 로고    scopus 로고
    • And they are still moving. Dynamic properties of caveoli
    • Kurchalia T.V., Parton R.G. And they are still moving. Dynamic properties of caveoli. FEBS Lett. 389:1996;52-54.
    • (1996) FEBS Lett , vol.389 , pp. 52-54
    • Kurchalia, T.V.1    Parton, R.G.2
  • 20
    • 0025340170 scopus 로고
    • Serum-induced proliferation of rabbit aortic smooth muscle cells from the contractile state is inhibited by 8-Br-cAMP but not 8-Br-cGMP
    • Southgate K.M., Newby A.C. Serum-induced proliferation of rabbit aortic smooth muscle cells from the contractile state is inhibited by 8-Br-cAMP but not 8-Br-cGMP. Atherosclerosis. 82:1990;113-123.
    • (1990) Atherosclerosis , vol.82 , pp. 113-123
    • Southgate, K.M.1    Newby, A.C.2
  • 21
    • 0030740575 scopus 로고    scopus 로고
    • 5-Hydroxytryptamine, angiotensin and bradykinin transiently increase intracellular calcium concentrations and PKC-alpha activity, but do not induce mitogenesis in human vascular smooth muscle cells
    • Assender J.W., Irenius E., Fredholin B.B. 5-Hydroxytryptamine, angiotensin and bradykinin transiently increase intracellular calcium concentrations and PKC-alpha activity, but do not induce mitogenesis in human vascular smooth muscle cells. Acta Physiol Scand. 160:1997;207-217.
    • (1997) Acta Physiol Scand , vol.160 , pp. 207-217
    • Assender, J.W.1    Irenius, E.2    Fredholin, B.B.3
  • 22
    • 0030888799 scopus 로고    scopus 로고
    • Inhibition of myocardial crossbridge cycling by hypoxic endothelial cells: A potential mechanism for matching oxygen supply and demand
    • Shah A., Mebazaa A., Yang Z.et al. Inhibition of myocardial crossbridge cycling by hypoxic endothelial cells: a potential mechanism for matching oxygen supply and demand. Circ Res. 80:1997;688-698.
    • (1997) Circ Res , vol.80 , pp. 688-698
    • Shah, A.1    Mebazaa, A.2    Yang, Z.3
  • 24
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principal of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principal of protein-dye binding. Anal Biochem. 72:1976;248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 27
    • 0023427097 scopus 로고
    • Bovine brain cytosol contains three immunologically distinct forms of inositol phospholipid specific phospholipase C
    • Ryu S.H., Shu P.G., Cho K.S., Lee K.Y., Rhee S.G. Bovine brain cytosol contains three immunologically distinct forms of inositol phospholipid specific phospholipase C. Proc Natl Acad Sci USA. 84:1987;6649-6653.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 6649-6653
    • Ryu, S.H.1    Shu, P.G.2    Cho, K.S.3    Lee, K.Y.4    Rhee, S.G.5
  • 28
    • 0029957272 scopus 로고    scopus 로고
    • The control of inositol lipid hydrolysis
    • Katan M. The control of inositol lipid hydrolysis. Cancer Surv. 27:1996;199-211.
    • (1996) Cancer Surv , vol.27 , pp. 199-211
    • Katan, M.1
  • 30
    • 0026693238 scopus 로고
    • Nuclear localization and signalling activity of phosphoinositidase C β in Swiss 3T3 cells
    • Martelli A.M. Nuclear localization and signalling activity of phosphoinositidase C β in Swiss 3T3 cells. Nature. 358:1992;242-245.
    • (1992) Nature , vol.358 , pp. 242-245
    • Martelli, A.M.1
  • 31
    • 0028177560 scopus 로고
    • Interleukin-1 alpha stimulates nuclear phospholipase-C in human osteosarcoma SaOS-2 cells
    • Marmiroli S., Ognibene A., Bavelloni A.et al. Interleukin-1 alpha stimulates nuclear phospholipase-C in human osteosarcoma SaOS-2 cells. J Biol Chem. 269:1994;13-16.
    • (1994) J Biol Chem. , vol.269 , pp. 13-16
    • Marmiroli, S.1    Ognibene, A.2    Bavelloni, A.3
  • 33
    • 0028860268 scopus 로고
    • Heterotrimeric G proteins: Organizers of transmembrane signals
    • Neer E.J. Heterotrimeric G proteins: Organizers of transmembrane signals. Cell. 80:1995;249-257.
    • (1995) Cell , vol.80 , pp. 249-257
    • Neer, E.J.1
  • 34
    • 0028859279 scopus 로고
    • Protein modules and signalling networks
    • Pawson T. Protein modules and signalling networks. Nature. 373:1995;573-580.
    • (1995) Nature , vol.373 , pp. 573-580
    • Pawson, T.1
  • 35
    • 0026462105 scopus 로고
    • The role of CTP-binding proteins in signal transduction: From the sublimely simple to the conceptually complex
    • Rodbell M. The role of CTP-binding proteins in signal transduction: from the sublimely simple to the conceptually complex. Curr. Top Cell Regul. 32:1992;1-47.
    • (1992) Curr. Top Cell Regul , vol.32 , pp. 1-47
    • Rodbell, M.1
  • 36
    • 0029855514 scopus 로고    scopus 로고
    • Organisation of transmembrane signalling by heterotrimeric G-proteins
    • Offermans S., Simon M.I. Organisation of transmembrane signalling by heterotrimeric G-proteins. Cancer Surv. 27:1996;177-197.
    • (1996) Cancer Surv , vol.27 , pp. 177-197
    • Offermans, S.1    Simon, M.I.2
  • 37
    • 0027443234 scopus 로고
    • Caveolae: Where incoming and outgoing messages meet
    • Anderson R.G.W. Caveolae: Where incoming and outgoing messages meet. Proc Natl Acad Sci USA. 90:1993;10909-10913.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 10909-10913
    • Anderson, R.G.W.1
  • 38
    • 0028113411 scopus 로고
    • Signal transduction of a G-protein-coupled receptor in caveolae: Colocalisation of endothelin and its receptor with caveolin
    • Chun M., Liyanage U.K., Lisante M.P., Lodish H.F. Signal transduction of a G-protein-coupled receptor in caveolae: colocalisation of endothelin and its receptor with caveolin. Proc Natl Acad Sci USA. 91:1994;11728-11732.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 11728-11732
    • Chun, M.1    Liyanage, U.K.2    Lisante, M.P.3    Lodish, H.F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.