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Volumn 29, Issue 5, 1997, Pages 815-828

Effect of sphingomyelin and its metabolites on the activity of human recombinant PLC δ1

Author keywords

Ganglioside; Kinetics; Phospholipase C 1 expression; Purification

Indexed keywords

CALCIUM ION; CERAMIDE; GANGLIOSIDE GM1; PHOSPHOLIPASE C; RECOMBINANT ENZYME; SPERMINE; SPHINGOMYELIN;

EID: 0030862727     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1357-2725(97)00014-9     Document Type: Article
Times cited : (13)

References (66)
  • 1
    • 0028965283 scopus 로고
    • Stimulation of cyclic adenosine 3′,5′-monophosphate-dependent protein kinase with brain gangliosides
    • Arakane F., Fukunaga K., Satake M., Miyazaki K., Okamura H. and Miyamoto E. (1995) Stimulation of cyclic adenosine 3′,5′-monophosphate-dependent protein kinase with brain gangliosides. Neurochem. Int. 26, 187-193.
    • (1995) Neurochem. Int. , vol.26 , pp. 187-193
    • Arakane, F.1    Fukunaga, K.2    Satake, M.3    Miyazaki, K.4    Okamura, H.5    Miyamoto, E.6
  • 2
    • 0026726492 scopus 로고
    • Interleukin-1-mediated PGE2 production and sphingomyelin metabolism. Evidence for the regulation of cyclooxygenase gene expression by sphingosine and ceramide
    • Ballou L. R., Chao C. P., Holness M. A., Barker S. C. and Raghow R. (1992) Interleukin-1-mediated PGE2 production and sphingomyelin metabolism. Evidence for the regulation of cyclooxygenase gene expression by sphingosine and ceramide. J. Biol. Chem. 267, 20044-20050.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20044-20050
    • Ballou, L.R.1    Chao, C.P.2    Holness, M.A.3    Barker, S.C.4    Raghow, R.5
  • 3
    • 0028357208 scopus 로고
    • Thrombin-mediated phosphoinositide hydrolysis in Chinese hamster ovary cells overexpressing phospholipase C-δ1
    • Banno Y., Okano Y. and Nozawa Y. (1994) Thrombin-mediated phosphoinositide hydrolysis in Chinese hamster ovary cells overexpressing phospholipase C-δ1. J. Biol. Chem. 269, 15846-15852.
    • (1994) J. Biol. Chem. , vol.269 , pp. 15846-15852
    • Banno, Y.1    Okano, Y.2    Nozawa, Y.3
  • 4
    • 0023687758 scopus 로고
    • Molecular cloning and complete amino-acid sequence of form-I phosphoinositide-specific phospholipase C
    • Bennett C. F., Balcarek J. M., Varrichio A. and Crooke S. (1988) Molecular cloning and complete amino-acid sequence of form-I phosphoinositide-specific phospholipase C. Nature 334, 268-270.
    • (1988) Nature , vol.334 , pp. 268-270
    • Bennett, C.F.1    Balcarek, J.M.2    Varrichio, A.3    Crooke, S.4
  • 5
    • 0026497034 scopus 로고
    • βγ-subunit activation of G-protein-regulated phospholipase C
    • Boyer J. L., Waldo G. L. and Harden T. K. (1992) βγ-subunit activation of G-protein-regulated phospholipase C. J. Biol. Chem. 267, 25451-25456.
    • (1992) J. Biol. Chem. , vol.267 , pp. 25451-25456
    • Boyer, J.L.1    Waldo, G.L.2    Harden, T.K.3
  • 6
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 7
    • 0021186166 scopus 로고
    • Ganglioside-mediated modulation of cell growth, growth factor binding, and receptor phosphorylation
    • Bremer E. G., Hakomori S., Bowen-Pope D. F., Raines E. and Ross R. (1984) Ganglioside-mediated modulation of cell growth, growth factor binding, and receptor phosphorylation. J. Biol. Chem. 259, 6818-6825.
    • (1984) J. Biol. Chem. , vol.259 , pp. 6818-6825
    • Bremer, E.G.1    Hakomori, S.2    Bowen-Pope, D.F.3    Raines, E.4    Ross, R.5
  • 9
    • 0026676806 scopus 로고
    • Isozyme-selective stimulation of phospholipase C-β2 by G protein βγ-subunits
    • Camps M., Carozzi A., Schnabel P., Scheer A., Parker P. J. and Gierschik P. (1992) Isozyme-selective stimulation of phospholipase C-β2 by G protein βγ-subunits. Nature 360, 684-689.
    • (1992) Nature , vol.360 , pp. 684-689
    • Camps, M.1    Carozzi, A.2    Schnabel, P.3    Scheer, A.4    Parker, P.J.5    Gierschik, P.6
  • 10
    • 0023654642 scopus 로고
    • Ganglioside-modulated protein phosphorylation. Partial purification and characterization of a ganglioside-stimulated protein kinase in brain
    • Chan K. F. (1987a) Ganglioside-modulated protein phosphorylation. Partial purification and characterization of a ganglioside-stimulated protein kinase in brain. J. Biol. Chem. 262, 5248-5255.
    • (1987) J. Biol. Chem. , vol.262 , pp. 5248-5255
    • Chan, K.F.1
  • 11
    • 0023654021 scopus 로고
    • Ganglioside-modulated protein phosphorylation in myelin
    • Chan K. F. (1987b) Ganglioside-modulated protein phosphorylation in myelin. J. Biol. Chem. 262, 2415-2422.
    • (1987) J. Biol. Chem. , vol.262 , pp. 2415-2422
    • Chan, K.F.1
  • 12
    • 0023901368 scopus 로고
    • Ganglioside-modulated protein phosphorylation. Partial purification and characterization of a ganglioside-inhibited protein kinase in brain
    • Chan K. F. (1988) Ganglioside-modulated protein phosphorylation. Partial purification and characterization of a ganglioside-inhibited protein kinase in brain. J. Biol. Chem. 263, 568-574.
    • (1988) J. Biol. Chem. , vol.263 , pp. 568-574
    • Chan, K.F.1
  • 13
    • 0024464077 scopus 로고
    • Ganglioside-modulated protein phosphorylation in muscle. Activation of phosphorylase b kinase by gangliosides
    • Chan K. F. (1989) Ganglioside-modulated protein phosphorylation in muscle. Activation of phosphorylase b kinase by gangliosides. J. Biol. Chem. 264, 18632-18637.
    • (1989) J. Biol. Chem. , vol.264 , pp. 18632-18637
    • Chan, K.F.1
  • 14
    • 0025349216 scopus 로고
    • Myelin basic protein: Interaction with calmodulin and gangliosides
    • Chan K. F. J., Robb N. D. and Chen W. H. (1990) Myelin basic protein: interaction with calmodulin and gangliosides. J. Neurosci. Res. 25, 533-544.
    • (1990) J. Neurosci. Res. , vol.25 , pp. 533-544
    • Chan, K.F.J.1    Robb, N.D.2    Chen, W.H.3
  • 15
    • 0026101732 scopus 로고
    • Ganglioside-binding proteins in skeletal and cardiac muscle
    • Chan K. F. J. and Liu Y. (1991) Ganglioside-binding proteins in skeletal and cardiac muscle. Glycobiology 1, 193-203.
    • (1991) Glycobiology , vol.1 , pp. 193-203
    • Chan, K.F.J.1    Liu, Y.2
  • 16
    • 0028937157 scopus 로고
    • Cloning and identification of amino acid residues of human phospholipase Cδ1 essential for catalysis
    • Cheng H.-F., Jiang M.-J., Chen C.-L., Liu S.-M., Wong L.-P., Lomasney J. W. and King K. (1995) Cloning and identification of amino acid residues of human phospholipase Cδ1 essential for catalysis. J. Biol. Chem. 270, 5495-5505.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5495-5505
    • Cheng, H.-F.1    Jiang, M.-J.2    Chen, C.-L.3    Liu, S.-M.4    Wong, L.-P.5    Lomasney, J.W.6    King, K.7
  • 17
    • 0026468420 scopus 로고
    • Inositol-lipid-specific phospholipase C isoenzymes and their differential regulation by receptors
    • Cockcroft S. and Thomas G. M. H. (1992) Inositol-lipid-specific phospholipase C isoenzymes and their differential regulation by receptors. Biochem. J. 288, 1-14.
    • (1992) Biochem. J. , vol.288 , pp. 1-14
    • Cockcroft, S.1    Thomas, G.M.H.2
  • 18
    • 0026560014 scopus 로고
    • Tumor necrosis factor-α activates the sphingomyelin signal transduction pathway in a cell-free system
    • Dressler K. A., Mathias S. and Kolesnic R. N. (1992) Tumor necrosis factor-α activates the sphingomyelin signal transduction pathway in a cell-free system. Science 255, 1715-1718.
    • (1992) Science , vol.255 , pp. 1715-1718
    • Dressler, K.A.1    Mathias, S.2    Kolesnic, R.N.3
  • 19
    • 0027461517 scopus 로고
    • Structural requirements of phosphatidylinositol-specific phospholipase C δ1 for enzyme activity
    • Ellis M. V., Carne A. and Katan M. (1993) Structural requirements of phosphatidylinositol-specific phospholipase C δ1 for enzyme activity. Eur. J. Biochem. 213, 339-347.
    • (1993) Eur. J. Biochem. , vol.213 , pp. 339-347
    • Ellis, M.V.1    Carne, A.2    Katan, M.3
  • 20
    • 0029924329 scopus 로고    scopus 로고
    • Crystal structure of a mammalian phosphoinositide-specific phospholipase Cδ
    • Essen L.-O., Perisic O., Cheung R., Katan M. and Williams R. L. (1996) Crystal structure of a mammalian phosphoinositide-specific phospholipase Cδ. Nature 380, 595-602.
    • (1996) Nature , vol.380 , pp. 595-602
    • Essen, L.-O.1    Perisic, O.2    Cheung, R.3    Katan, M.4    Williams, R.L.5
  • 21
    • 0024201809 scopus 로고
    • Computer programs for calculating total from specified free or free from spcecified total concentrations in aqueous solutions containing multiple metals and ligands
    • (Edited by Fleisher S. and Fleisher B.), Academic Press, New York
    • Fabiato A. (1988) Computer programs for calculating total from specified free or free from spcecified total concentrations in aqueous solutions containing multiple metals and ligands. In Methods in Enzymology (Edited by Fleisher S. and Fleisher B.), Vol. 157, pp. 378-417. Academic Press, New York.
    • (1988) Methods in Enzymology , vol.157 , pp. 378-417
    • Fabiato, A.1
  • 22
    • 0024297332 scopus 로고
    • Purification of a phospholipase C from rat liver cytosol that acts on phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 4-phosphate
    • Fukui T., Lutz R. J. and Lowenstein J. M. (1988) Purification of a phospholipase C from rat liver cytosol that acts on phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 4-phosphate. J. Biol. Chem. 263, 17730-17737.
    • (1988) J. Biol. Chem. , vol.263 , pp. 17730-17737
    • Fukui, T.1    Lutz, R.J.2    Lowenstein, J.M.3
  • 23
    • 0015859264 scopus 로고
    • External labeling of cell surface galactose and galactosamine in glycolipid and glycoprotein of human erythrocytes
    • Gahmberg C. T. and Hakomori S. I. (1973) External labeling of cell surface galactose and galactosamine in glycolipid and glycoprotein of human erythrocytes. J. Biol. Chem. 248, 4311-4317.
    • (1973) J. Biol. Chem. , vol.248 , pp. 4311-4317
    • Gahmberg, C.T.1    Hakomori, S.I.2
  • 24
    • 0028787055 scopus 로고
    • The pleckstrin homology domain of phospholipase C-δ1 binds with high affinity to phosphatidylinositol 4,5-bisphosphate in bilayer membranes
    • Garcia P., Gupta R., Shah S., Morris A. J., Rudge S. A., Scarlata S., Petrova V., McLaughlin S. and Rebecchi M. J. (1995) The pleckstrin homology domain of phospholipase C-δ1 binds with high affinity to phosphatidylinositol 4,5-bisphosphate in bilayer membranes. Biochemistry 34, 16228-16234.
    • (1995) Biochemistry , vol.34 , pp. 16228-16234
    • Garcia, P.1    Gupta, R.2    Shah, S.3    Morris, A.J.4    Rudge, S.A.5    Scarlata, S.6    Petrova, V.7    McLaughlin, S.8    Rebecchi, M.J.9
  • 25
    • 0031106172 scopus 로고    scopus 로고
    • Phospholipase isoforms δ1 and δ3 from human fibroblast. High yield expression in E. Coli, simple purification
    • Ghosh S., Pawelczyk T. and Lowenstein J. M. (1997) Phospholipase isoforms δ1 and δ3 from human fibroblast. High yield expression in E. coli, simple purification. Prot. Exp Purification 9, 262-278.
    • (1997) Prot. Exp Purification , vol.9 , pp. 262-278
    • Ghosh, S.1    Pawelczyk, T.2    Lowenstein, J.M.3
  • 28
    • 0028853289 scopus 로고
    • A dual functional signal mediator showing RhoGAP and phospholipase C-δ stimulating activities
    • Homma Y. and Emori Y. (1995) A dual functional signal mediator showing RhoGAP and phospholipase C-δ stimulating activities. EMBO J. 14, 286-291.
    • (1995) EMBO J. , vol.14 , pp. 286-291
    • Homma, Y.1    Emori, Y.2
  • 29
    • 0028070326 scopus 로고
    • Identification of arachidonic acid as a mediator of sphingomyelin hydrolysis in responce to tumor necrosis factor α
    • Jayadev S., Linardic C. M. and Hannun Y. A. (1994) Identification of arachidonic acid as a mediator of sphingomyelin hydrolysis in responce to tumor necrosis factor α. J. Biol. Chem. 269, 5757-5763.
    • (1994) J. Biol. Chem. , vol.269 , pp. 5757-5763
    • Jayadev, S.1    Linardic, C.M.2    Hannun, Y.A.3
  • 30
    • 0019434731 scopus 로고
    • Corticotropin-(1-24)-tetracosapeptide affects protein phosphorylation and polyphosphoinositide metabolism in rat brain
    • Jolles J., Zwiers H., Dekker A., Wirtz K. W. A. and Gipsen W. H. (1981) Corticotropin-(1-24)-tetracosapeptide affects protein phosphorylation and polyphosphoinositide metabolism in rat brain. Biochem. J. 194, 283-291.
    • (1981) Biochem. J. , vol.194 , pp. 283-291
    • Jolles, J.1    Zwiers, H.2    Dekker, A.3    Wirtz, K.W.A.4    Gipsen, W.H.5
  • 31
    • 0003048378 scopus 로고
    • (Edited by Work T. S. and Work E.), Elsevier, New York
    • Kates M. (1972) Techniques of Lipidology (Edited by Work T. S. and Work E.), pp. 355-356. Elsevier, New York
    • (1972) Techniques of Lipidology , pp. 355-356
    • Kates, M.1
  • 32
    • 0025247881 scopus 로고
    • Tyrosine residues in bovine phospholipase C-γ phosphorylated by the epidermal growth factor receptor in vitro
    • Kim J. W., Sim S. S., Kim U.-H., Nishibe S., Wahl M. I., Carpenter G. and Rhee S. G. (1990) Tyrosine residues in bovine phospholipase C-γ phosphorylated by the epidermal growth factor receptor in vitro. J. Biol. Chem. 265, 3940-3943.
    • (1990) J. Biol. Chem. , vol.265 , pp. 3940-3943
    • Kim, J.W.1    Sim, S.S.2    Kim, U.-H.3    Nishibe, S.4    Wahl, M.I.5    Carpenter, G.6    Rhee, S.G.7
  • 33
    • 0026007737 scopus 로고
    • Identification of sphingomyelin turnover as an effector mechanism for the action of tumor necrosis factor α and γ-interferon. Specific role in cell differentiation
    • Kim M.-Y., Linardic C. and Hannun Y. (1991) Identification of sphingomyelin turnover as an effector mechanism for the action of tumor necrosis factor α and γ-interferon. Specific role in cell differentiation. J. Biol. Chem. 266, 484-489.
    • (1991) J. Biol. Chem. , vol.266 , pp. 484-489
    • Kim, M.-Y.1    Linardic, C.2    Hannun, Y.3
  • 35
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 36
    • 0028986998 scopus 로고
    • 2 hydrolysis and regulation of phospholipase C isozymes
    • 2 hydrolysis and regulation of phospholipase C isozymes. Curr. Biol. 7, 183-189.
    • (1995) Curr. Biol. , vol.7 , pp. 183-189
    • Lee, S.B.1    Rhee, S.G.2
  • 37
    • 0001275961 scopus 로고    scopus 로고
    • Molecular cloning, splice variants, expression, and purification of phospholipase C-δ4
    • Lee S B. and Rhee S. G. (1996) Molecular cloning, splice variants, expression, and purification of phospholipase C-δ4. J. Biol. Chem. 271, 25-31.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25-31
    • Lee, S.B.1    Rhee, S.G.2
  • 38
    • 0026659880 scopus 로고
    • Brefeldin A promotes hydrolysis of sphingomyelin
    • Linardic C. M., Jayadev S. and Hannun Y. A. (1992) Brefeldin A promotes hydrolysis of sphingomyelin. J. Biol. Chem. 267, 14909-14911.
    • (1992) J. Biol. Chem. , vol.267 , pp. 14909-14911
    • Linardic, C.M.1    Jayadev, S.2    Hannun, Y.A.3
  • 39
    • 0027978352 scopus 로고
    • Identification of distinct pool of sphingomyelin involved in the sphingomyelin cycle
    • Linardic C. M. and Hannun Y. A. (1994) Identification of distinct pool of sphingomyelin involved in the sphingomyelin cycle. J. Biol. Chem. 269, 23530-23537.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23530-23537
    • Linardic, C.M.1    Hannun, Y.A.2
  • 40
    • 0027461121 scopus 로고
    • Activation of the sphingomyelin signaling pathway in intact EL4 cells in a cell-free system by IL-1β
    • Mathias S., Younnes A., Kan C.-C., Orlow I., Joseph C. and Kolesnick R. N. (1993) Activation of the sphingomyelin signaling pathway in intact EL4 cells in a cell-free system by IL-1β. Science 259, 519-522.
    • (1993) Science , vol.259 , pp. 519-522
    • Mathias, S.1    Younnes, A.2    Kan, C.-C.3    Orlow, I.4    Joseph, C.5    Kolesnick, R.N.6
  • 42
    • 0024392485 scopus 로고
    • A novel inositol phospholipid-specific phospholipase C. Rapid purification and characterization
    • Meldrum E., Katan M. and Parker P. (1989) A novel inositol phospholipid-specific phospholipase C. Rapid purification and characterization. Eur. J. Biochem. 182, 673-677.
    • (1989) Eur. J. Biochem. , vol.182 , pp. 673-677
    • Meldrum, E.1    Katan, M.2    Parker, P.3
  • 43
    • 0030042239 scopus 로고    scopus 로고
    • Ceramide inhibits IgE-mediated activation of phospholipase D, but not of phospholipase C, in rat basophilic leukemia cells
    • Nakamura Y., Nakashima S., Ojio K., Banno Y., Miyata H. and Nozawa Y. (1996) Ceramide inhibits IgE-mediated activation of phospholipase D, but not of phospholipase C, in rat basophilic leukemia cells. J. Immunol. 156, 256-262.
    • (1996) J. Immunol. , vol.156 , pp. 256-262
    • Nakamura, Y.1    Nakashima, S.2    Ojio, K.3    Banno, Y.4    Miyata, H.5    Nozawa, Y.6
  • 46
    • 0028329918 scopus 로고
    • Release of proteins and peptides from fusion proteins using a recombinant plant virus proteinase
    • Parks T. D., Leuther K. K., Howard E. D., Johnston S. A. and Dougherty W. G. (1994) Release of proteins and peptides from fusion proteins using a recombinant plant virus proteinase. Anal. Biochem. 216, 413-417.
    • (1994) Anal. Biochem. , vol.216 , pp. 413-417
    • Parks, T.D.1    Leuther, K.K.2    Howard, E.D.3    Johnston, S.A.4    Dougherty, W.G.5
  • 47
  • 48
    • 0026970340 scopus 로고
    • Regulation of phospholipase Ca activity by sphingomyelin and sphin gosine
    • Pawelczyk T. and Lowenstein J. M. (1992) Regulation of phospholipase Ca activity by sphingomyelin and sphin gosine. Arch. Biochem. Biophys. 297, 328-333.
    • (1992) Arch. Biochem. Biophys. , vol.297 , pp. 328-333
    • Pawelczyk, T.1    Lowenstein, J.M.2
  • 49
    • 0027310380 scopus 로고
    • Binding of phospholipase Cδ1 to phospholipid vesicles
    • Pawelczyk T. and Lowenstein J. M. (1993a) Binding of phospholipase Cδ1 to phospholipid vesicles. Biochem. J. 291, 693-696.
    • (1993) Biochem. J. , vol.291 , pp. 693-696
    • Pawelczyk, T.1    Lowenstein, J.M.2
  • 50
    • 0027530795 scopus 로고
    • Inhibition of phospholipase Cδ by hexadecylphosphorylcholine and lysophospholipids with antitumor activity
    • Pawelczyk T. and Lowenstein J. M. (1993b) Inhibition of phospholipase Cδ by hexadecylphosphorylcholine and lysophospholipids with antitumor activity. Biochem. Pharmacol. 45, 493-497.
    • (1993) Biochem. Pharmacol. , vol.45 , pp. 493-497
    • Pawelczyk, T.1    Lowenstein, J.M.2
  • 51
    • 0027050183 scopus 로고
    • Phosphoinositide-specific phospholipase C-δ1 binds with high affinity to phospholipid vesicles containig phosphatidylinositol 4,5-bisphosphate
    • Rebecchi M., Peterson A. and McLaughlin S. (1992) Phosphoinositide-specific phospholipase C-δ1 binds with high affinity to phospholipid vesicles containig phosphatidylinositol 4,5-bisphosphate. Biochemistry 31, 12742-12747.
    • (1992) Biochemistry , vol.31 , pp. 12742-12747
    • Rebecchi, M.1    Peterson, A.2    McLaughlin, S.3
  • 53
    • 0002431043 scopus 로고
    • (Edited by Liscovitch M.), RG Landes Company, Austin, TX
    • Rhee S. G. (1994) Signal-activated Phospholipases (Edited by Liscovitch M.), pp. 1-12. RG Landes Company, Austin, TX.
    • (1994) Signal-activated Phospholipases , pp. 1-12
    • Rhee, S.G.1
  • 54
    • 0028833570 scopus 로고
    • Stimulation and binding of myocardial phospholipase C by phosphatidic acid
    • Ross A. H., Sharon Y. B., Kurz T. and Wolf R. A. (1995) Stimulation and binding of myocardial phospholipase C by phosphatidic acid. Am. J. Physiol. 269, C349-C358.
    • (1995) Am. J. Physiol. , vol.269
    • Ross, A.H.1    Sharon, Y.B.2    Kurz, T.3    Wolf, R.A.4
  • 55
    • 0016162296 scopus 로고
    • Measurement of inorganic orthophosphate in biological materials: Extraction properties of butyl acetate
    • Sanui H. (1974) Measurement of inorganic orthophosphate in biological materials: extraction properties of butyl acetate. Anal. Biochem. 60, 489-504.
    • (1974) Anal. Biochem. , vol.60 , pp. 489-504
    • Sanui, H.1
  • 57
    • 0017878781 scopus 로고
    • A model for ganglioside behaviour in cell membranes
    • Sharom F. J. and Grant C. W. (1978) A model for ganglioside behaviour in cell membranes. Biochim. Biophys. Acta 507, 208-212.
    • (1978) Biochim. Biophys. Acta , vol.507 , pp. 208-212
    • Sharom, F.J.1    Grant, C.W.2
  • 58
    • 0023778244 scopus 로고
    • Inhibition of DNA synthesis in C6 glioma cells following cellular incorporation of GM1 ganglioside and choleragenoid exposure
    • Skaper S. D., Facci L., Favaron M. and Leon A. (1988) Inhibition of DNA synthesis in C6 glioma cells following cellular incorporation of GM1 ganglioside and choleragenoid exposure. J. Neurochem. 51, 688-697.
    • (1988) J. Neurochem. , vol.51 , pp. 688-697
    • Skaper, S.D.1    Facci, L.2    Favaron, M.3    Leon, A.4
  • 59
    • 0025793981 scopus 로고
    • Regulation of polyphosphoinositide-specific phospholipase C activity by purified Gq
    • Smrcka A. V., Helper J. R., Brown K. O. and Sternweis P. C. (1991) Regulation of polyphosphoinositide-specific phospholipase C activity by purified Gq. Science 251, 804-807.
    • (1991) Science , vol.251 , pp. 804-807
    • Smrcka, A.V.1    Helper, J.R.2    Brown, K.O.3    Sternweis, P.C.4
  • 60
    • 0027214868 scopus 로고
    • Regulation of purified subtypes of PLC-β by G protein α and βγ subunits
    • Smrcka A. V. and Sternweis P. C. (1993) Regulation of purified subtypes of PLC-β by G protein α and βγ subunits. J. Biol. Chem. 268, 9667-9674.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9667-9674
    • Smrcka, A.V.1    Sternweis, P.C.2
  • 61
    • 0016372224 scopus 로고
    • Topographical distribution of complex carbohydrates in the erythrocyte membrane
    • Steck T. L. and Dawson G. (1974) Topographical distribution of complex carbohydrates in the erythrocyte membrane. J. Biol. Chem. 249, 2135-2142.
    • (1974) J. Biol. Chem. , vol.249 , pp. 2135-2142
    • Steck, T.L.1    Dawson, G.2
  • 62
    • 0023749072 scopus 로고
    • Cloning and sequence of multiple forms of phospholipase C
    • Such P.-G., Ryu S. H., Moon K. H., Suh H. W. and Rhee S. G. (1988) Cloning and sequence of multiple forms of phospholipase C. Cell 54, 161-169.
    • (1988) Cell , vol.54 , pp. 161-169
    • Such, P.-G.1    Ryu, S.H.2    Moon, K.H.3    Suh, H.W.4    Rhee, S.G.5
  • 63
    • 0025860413 scopus 로고
    • Activation of the β1 isozyme of phospholipase C α subunits of the Gq class of G proteins
    • Taylor S. J., Chae H. Z., Rhee S. G. and Exton J. H. (1991) Activation of the β1 isozyme of phospholipase C α subunits of the Gq class of G proteins. Nature 350, 516-518.
    • (1991) Nature , vol.350 , pp. 516-518
    • Taylor, S.J.1    Chae, H.Z.2    Rhee, S.G.3    Exton, J.H.4
  • 64
    • 0025296838 scopus 로고
    • Stimulation of phospholipase C-γ1 membrane association by epidermal growth factor
    • Todderud G., Wahl M. I., Rhee S. G. and Carpenter G. (1990) Stimulation of phospholipase C-γ1 membrane association by epidermal growth factor. Science 249, 296-298.
    • (1990) Science , vol.249 , pp. 296-298
    • Todderud, G.1    Wahl, M.I.2    Rhee, S.G.3    Carpenter, G.4
  • 65
    • 0018907210 scopus 로고
    • Transbilayer distribution and mobility of phosphatidylcholine in intact erythrocyte membranes. A study with phosphatidylcholine exchange protein
    • Van Meer G., Poorthuis B. J., Wirtz K. W., Op den Kamp J. A. and van Deenen L. L. (1980) Transbilayer distribution and mobility of phosphatidylcholine in intact erythrocyte membranes. A study with phosphatidylcholine exchange protein. Eur. J. Biochem. 103, 283-288.
    • (1980) Eur. J. Biochem. , vol.103 , pp. 283-288
    • Van Meer, G.1    Poorthuis, B.J.2    Wirtz, K.W.3    Op Den Kamp, J.A.4    Van Deenen, L.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.