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Volumn 99, Issue 8, 1997, Pages 1831-1841

1,25 dihydroxyvitamin D3 stimulates phospholipase C-γ in rat colonocytes: Role of c-Src in PLC-γ activation

Author keywords

1,25 dihydroxycholecalciferol; basolateral membrane; nonreceptor tyrosine kinase; vitamin D deficiency

Indexed keywords

CALCITRIOL; CALCIUM ION; PHOSPHOLIPASE C; PROTEIN KINASE C; PROTEIN TYROSINE KINASE; SECOSTEROID;

EID: 0030962467     PISSN: 00219738     EISSN: None     Source Type: Journal    
DOI: 10.1172/JCI119350     Document Type: Article
Times cited : (70)

References (46)
  • 1
    • 0025323383 scopus 로고
    • 3 stimulates membrane phosphoinositide turnover, activates protein kinase C, and increases cytosolic calcium in rat colonie epithelium
    • 3 stimulates membrane phosphoinositide turnover, activates protein kinase C, and increases cytosolic calcium in rat colonie epithelium. J. Clin. Invest. 85:1296-1303.
    • (1990) J. Clin. Invest. , vol.85 , pp. 1296-1303
    • Wall, R.K.1    Baum, C.L.2    Sitrin, M.D.3    Brasitus, T.A.4
  • 2
    • 0026652456 scopus 로고
    • Effect of vitamin D status on the rapid actions of 1,25-dihydroxycholecalciferol in rat colonic membranes
    • Wali, R.K., C.L. Baum, M.D. Sitrin, M.J.G. Bolt, P.K. Dudeja, and T.A. Brasitus. 1992. Effect of vitamin D status on the rapid actions of 1,25-dihydroxycholecalciferol in rat colonic membranes. Am. J. Physiol. 262:945-953.
    • (1992) Am. J. Physiol. , vol.262 , pp. 945-953
    • Wali, R.K.1    Baum, C.L.2    Sitrin, M.D.3    Bolt, M.J.G.4    Dudeja, P.K.5    Brasitus, T.A.6
  • 3
    • 0026807007 scopus 로고
    • Differential effect of 1,25-dihydroxycholecalciferol on phosphoinositide turn-over in the antipodal plasma membranes of colonie epithelial cells
    • Wali, R.K., M.J.G. Bolt, X.-Y. Tien, T.A. Brasitus, and M.D. Sitrin. 1992. Differential effect of 1,25-dihydroxycholecalciferol on phosphoinositide turn-over in the antipodal plasma membranes of colonie epithelial cells. Biochem. Biophys. Res. Commun. 187:1128-1134.
    • (1992) Biochem. Biophys. Res. Commun. , vol.187 , pp. 1128-1134
    • Wali, R.K.1    Bolt, M.J.G.2    Tien, X.-Y.3    Brasitus, T.A.4    Sitrin, M.D.5
  • 8
    • 0030055211 scopus 로고    scopus 로고
    • 3 stimulates expression and translocation of protein kinase Cα and Cδ via a nongenomic mechanism and rapidly induces phosphorylation of a 33-kDa protein in acute promyelocytic NB4 cells
    • 3 stimulates expression and translocation of protein kinase Cα and Cδ via a nongenomic mechanism and rapidly induces phosphorylation of a 33-kDa protein in acute promyelocytic NB4 cells. J. Biol. Chem. 271:16090-16096.
    • (1996) J. Biol. Chem. , vol.271 , pp. 16090-16096
    • Berry, D.M.1    Antochi, R.2    Bhatia, M.3    Meckling-Gill, K.A.4
  • 10
    • 0027324224 scopus 로고
    • In vitro tyrosine phosphorylation of PLC-γ1 and PLC-γ2 by src-family protein tyrosine kinases
    • Liao, F., H.S. Shin, and S.G. Rhee. 1993. In vitro tyrosine phosphorylation of PLC-γ1 and PLC-γ2 by src-family protein tyrosine kinases. Biochem. Biophys. Res. Commun. 191:1028-1033.
    • (1993) Biochem. Biophys. Res. Commun. , vol.191 , pp. 1028-1033
    • Liao, F.1    Shin, H.S.2    Rhee, S.G.3
  • 11
    • 0025935178 scopus 로고
    • Dietary calcium and vitamin D modulate 1,2-dimethylhydrazine-induced colonic carcinogenesis in the rat
    • Sitrin, M.D., A.G. Halline, C. Abrahams, and T.A. Brasitus. 1991. Dietary calcium and vitamin D modulate 1,2-dimethylhydrazine-induced colonic carcinogenesis in the rat. Cancer Res. 51:5608-5613.
    • (1991) Cancer Res. , vol.51 , pp. 5608-5613
    • Sitrin, M.D.1    Halline, A.G.2    Abrahams, C.3    Brasitus, T.A.4
  • 13
    • 0015716692 scopus 로고
    • A rapid, sensitive and specific method for the determination of protein in dilute solution
    • Schaffner, W., and C. Weissmann. 1973. A rapid, sensitive and specific method for the determination of protein in dilute solution. Anal. Biochem. 56: 502-514.
    • (1973) Anal. Biochem. , vol.56 , pp. 502-514
    • Schaffner, W.1    Weissmann, C.2
  • 14
    • 0021223457 scopus 로고
    • Protein-lipid interactions in antipodal plasma membranes of rat colonocyles
    • Brasitus, T.A., and R.S. Keresztes. 1984. Protein-lipid interactions in antipodal plasma membranes of rat colonocyles. Biochim. Biophys. Acta. 773: 290-300.
    • (1984) Biochim. Biophys. Acta. , vol.773 , pp. 290-300
    • Brasitus, T.A.1    Keresztes, R.S.2
  • 15
    • 0026635622 scopus 로고
    • CHELATOR: An improved method for computing metal ion concentrations in physiological solutions
    • Schoenmakers, T.J.M., G.J. Visser, G. Flik, and A.P.R. Theuvenet. 1992. CHELATOR: An improved method for computing metal ion concentrations in physiological solutions. BioTechniques. 12:870-879.
    • (1992) BioTechniques , vol.12 , pp. 870-879
    • Schoenmakers, T.J.M.1    Visser, G.J.2    Flik, G.3    Theuvenet, A.P.R.4
  • 17
    • 0025878284 scopus 로고
    • Polyproline affinity method for purification of platelet profilin and modification with pyrene-maleimide
    • Janmey, P.A. 1991. Polyproline affinity method for purification of platelet profilin and modification with pyrene-maleimide. Methods Enzymol. 196: 92-99.
    • (1991) Methods Enzymol. , vol.196 , pp. 92-99
    • Janmey, P.A.1
  • 20
    • 0017613305 scopus 로고
    • Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis
    • Cleveland, D.W., S.G. Fischer, M.W. Kirschner, and U.K. Laemmli. 1977. Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis. J. Biol. Chem. 252:1102-1106.
    • (1977) J. Biol. Chem. , vol.252 , pp. 1102-1106
    • Cleveland, D.W.1    Fischer, S.G.2    Kirschner, M.W.3    Laemmli, U.K.4
  • 23
    • 0022081671 scopus 로고
    • c-src kinase by middle T antigen binding or by dephosphorylation
    • c-src kinase by middle T antigen binding or by dephosphorylation. EMBO (Eur. Mol. Biol Organ.) J. 4: 1471-1477.
    • (1985) EMBO (Eur. Mol. Biol Organ.) J. , vol.4 , pp. 1471-1477
    • Courtneidge, S.A.1
  • 26
    • 0029079038 scopus 로고
    • Src phosphorylation of the epidermal growth factor receptor at novel sites mediates receptor interaction with Src and P85α
    • Stover, D.R., M. Becker, J. Liebetanz, and N.B. Lydon. 1995. Src phosphorylation of the epidermal growth factor receptor at novel sites mediates receptor interaction with Src and P85α. J. Biol. Chem. 270:15591-15597.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15591-15597
    • Stover, D.R.1    Becker, M.2    Liebetanz, J.3    Lydon, N.B.4
  • 30
    • 0028979441 scopus 로고
    • 3 upregulates the phosphatidylinositol signaling pathway in human keratinocytes by increasing phospholipase C levels
    • 3 upregulates the phosphatidylinositol signaling pathway in human keratinocytes by increasing phospholipase C levels. J. Clin. Invest. 96:602-609.
    • (1995) J. Clin. Invest. , vol.96 , pp. 602-609
    • Pillai, S.1    Bikle, D.D.2    Su, M.-J.3    Ratnam, A.4    Abe, J.5
  • 32
    • 0028175956 scopus 로고
    • v-src monoclonal antibody inhibits activation of phospholipase C in platelets. A new mechanism for platelet-activating factor responses
    • v-src monoclonal antibody inhibits activation of phospholipase C in platelets. A new mechanism for platelet-activating factor responses. J. Biol. Chem. 269:9123-9127.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9123-9127
    • Dhar, A.1    Shukla, S.D.2
  • 37
    • 0021910430 scopus 로고
    • Dietary vitamin D and calcium and risk of colorectal cancer: A 19 year prospective study in men
    • Garland, C., R.B. Shekelle, E. Barrett-Connor, M.H. Criqui, A.H. Rossof, and O. Paul. 1985. Dietary vitamin D and calcium and risk of colorectal cancer: a 19 year prospective study in men. Lancet. i:307-309.
    • (1985) Lancet , vol.1 , pp. 307-309
    • Garland, C.1    Shekelle, R.B.2    Barrett-Connor, E.3    Criqui, M.H.4    Rossof, A.H.5    Paul, O.6
  • 38
    • 0027172209 scopus 로고
    • The Src family tyrosine kinases are required for platelet-derived growth factor-mediated signal transduction in NIH 3T3 cells
    • Twamley-Stein, G.M., R. Pepperkok, W. Ansorge, and S.A. Courtneidge. 1993. The Src family tyrosine kinases are required for platelet-derived growth factor-mediated signal transduction in NIH 3T3 cells. Proc. Natl. Acad. Sci. USA. 90:7696-7700.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7696-7700
    • Twamley-Stein, G.M.1    Pepperkok, R.2    Ansorge, W.3    Courtneidge, S.A.4
  • 39
    • 0028795721 scopus 로고
    • DNA synthesis induced by some but not all growth factors requires Src family protein tyrosine kinases
    • Roche, S., M. Koegl, M.V. Barone, M.F. Roussel, and S.A. Courtneidge. 1995. DNA synthesis induced by some but not all growth factors requires Src family protein tyrosine kinases. Mol. Cell. Biol. 15:1102-1109.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1102-1109
    • Roche, S.1    Koegl, M.2    Barone, M.V.3    Roussel, M.F.4    Courtneidge, S.A.5
  • 42
    • 0025931499 scopus 로고
    • Signal transduction by nerve growth factor and fibroblast growth factor in PC12 cells requires a sequence of src and ras actions
    • Kremer, N.E., G. D'Arcangelo, S.M. Thomas, M. DeMarco, J.S. Brugge, and S. Halegoua. 1991. Signal transduction by nerve growth factor and fibroblast growth factor in PC12 cells requires a sequence of src and ras actions. J. Cell Biol. 115:809-819.
    • (1991) J. Cell Biol. , vol.115 , pp. 809-819
    • Kremer, N.E.1    D'Arcangelo, G.2    Thomas, S.M.3    DeMarco, M.4    Brugge, J.S.5    Halegoua, S.6
  • 44
    • 0023956395 scopus 로고
    • c-src alters a selective morphogenetic property of epithelial cells in vitro without a mitogenic effect
    • c-src alters a selective morphogenetic property of epithelial cells in vitro without a mitogenic effect. Mol. Cell. Biol. 8:632-646.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 632-646
    • Warren, S.L.1    Handel, L.M.2    Nelson, W.J.3
  • 45
    • 0028877919 scopus 로고
    • Tyrosine phosphorylation of focal adhesion kinase at sites in the catalytic domain regulates kinase activity: A role for Src family kinases
    • Calalb, M.B., T.R. Polte, and S.K. Hanks. 1995. Tyrosine phosphorylation of focal adhesion kinase at sites in the catalytic domain regulates kinase activity: a role for Src family kinases. Mol. Cell. Biol. 15:954-963.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 954-963
    • Calalb, M.B.1    Polte, T.R.2    Hanks, S.K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.