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Volumn 75, Issue 2, 2000, Pages 672-682

Up-regulation of cell surface insulin receptor by protein kinase C-α in adrenal chromaffin cells: Involvement of transcriptional and translational events

Author keywords

125I Insulin binding; Insulin receptor; Northern blot; Protein kinase C ; Up regulation; Western blot

Indexed keywords

INSULIN RECEPTOR; PROTEIN KINASE C ACTIVATOR;

EID: 0033914653     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.2000.0750672.x     Document Type: Article
Times cited : (13)

References (80)
  • 1
    • 0033556222 scopus 로고    scopus 로고
    • Simultaneous visualization of the translocation of protein kinase Cα-green fluorescent protein hybrids and intracellular calcium concentrations
    • Almholt K., Arkhammar P. O. G., Thastrup O., and Tullin S. (1999) Simultaneous visualization of the translocation of protein kinase Cα-green fluorescent protein hybrids and intracellular calcium concentrations. Biochem. J. 337, 211-218.
    • (1999) Biochem. J. , vol.337 , pp. 211-218
    • Almholt, K.1    Arkhammar, P.O.G.2    Thastrup, O.3    Tullin, S.4
  • 2
    • 0029758766 scopus 로고    scopus 로고
    • Fusion of insulin receptor ectodomains to immunoglobulin constant domains reproduces high-affinity insulin binding in vitro
    • Bass J., Kurose T., Pashmforoush M., and Steiner D. F. (1996) Fusion of insulin receptor ectodomains to immunoglobulin constant domains reproduces high-affinity insulin binding in vitro. J. Biol. Chem. 271, 19367-19375.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19367-19375
    • Bass, J.1    Kurose, T.2    Pashmforoush, M.3    Steiner, D.F.4
  • 3
    • 0028031151 scopus 로고
    • Glucose-induced translocation of protein kinase C isoforms in rat-1 fibroblasts is paralleled by inhibition of the insulin receptor tyrosine kinase
    • Berti L., Mosthaf L., Kroder G., Kellerer M., Tippmer S., Mushack J., Seffer E., Seedorf K., and Haring H. (1994) Glucose-induced translocation of protein kinase C isoforms in rat-1 fibroblasts is paralleled by inhibition of the insulin receptor tyrosine kinase. J. Biol. Chem. 269, 3381-3386.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3381-3386
    • Berti, L.1    Mosthaf, L.2    Kroder, G.3    Kellerer, M.4    Tippmer, S.5    Mushack, J.6    Seffer, E.7    Seedorf, K.8    Haring, H.9
  • 4
    • 0030763630 scopus 로고    scopus 로고
    • Chloroquine extends the lifetime of the activated insulin receptor complex in endosomes
    • Bevan A. P., Krook A., Tikerpae J., Seabright P. J., Siddle K., and Smith G. D. (1997) Chloroquine extends the lifetime of the activated insulin receptor complex in endosomes. J. Biol. Chem. 272, 26833-26840.
    • (1997) J. Biol. Chem. , vol.272 , pp. 26833-26840
    • Bevan, A.P.1    Krook, A.2    Tikerpae, J.3    Seabright, P.J.4    Siddle, K.5    Smith, G.D.6
  • 5
    • 0030813811 scopus 로고    scopus 로고
    • Vanadate, but not insulin, inhibits insulin receptor gene expression in rat hepatoma cells
    • Bortoli S., Amessou M., Collinet M., Desbuquois B., and Lopez S. (1997) Vanadate, but not insulin, inhibits insulin receptor gene expression in rat hepatoma cells. Endocrinology 138, 4821-4829.
    • (1997) Endocrinology , vol.138 , pp. 4821-4829
    • Bortoli, S.1    Amessou, M.2    Collinet, M.3    Desbuquois, B.4    Lopez, S.5
  • 6
    • 0024521276 scopus 로고
    • Insulin receptor recycling in vascular endothelial cells. Regulation by insulin and phorbol ester
    • Bottaro D. P., Bonner-Weir S., and King G. L. (1989) Insulin receptor recycling in vascular endothelial cells. Regulation by insulin and phorbol ester. J. Biol. Chem. 264, 5916-5923.
    • (1989) J. Biol. Chem. , vol.264 , pp. 5916-5923
    • Bottaro, D.P.1    Bonner-Weir, S.2    King, G.L.3
  • 7
    • 0025348797 scopus 로고
    • Glucose starvation and glycosylation inhibitors reduce insulin receptor gene expression: Characterization and potential mechanism in human cells
    • Briata P., Briata L., and Gherzi R. (1990) Glucose starvation and glycosylation inhibitors reduce insulin receptor gene expression: characterization and potential mechanism in human cells. Biochem. Biophys. Res. Commun. 169, 397-405.
    • (1990) Biochem. Biophys. Res. Commun. , vol.169 , pp. 397-405
    • Briata, P.1    Briata, L.2    Gherzi, R.3
  • 8
    • 0030048931 scopus 로고    scopus 로고
    • Human diabetes associated with defects in nuclear regulatory proteins for the insulin receptor gene
    • Brunetti A., Brunetti L., Foti D., Accili D., and Goldfine I. D. (1996) Human diabetes associated with defects in nuclear regulatory proteins for the insulin receptor gene. J. Clin. Invest. 97, 258-262.
    • (1996) J. Clin. Invest. , vol.97 , pp. 258-262
    • Brunetti, A.1    Brunetti, L.2    Foti, D.3    Accili, D.4    Goldfine, I.D.5
  • 11
    • 0028247360 scopus 로고
    • Insulin-sensitive association of GLUT-4 with endocytic clathrin-coated vesicles revealed with the use of brefeldin A
    • Chakrabarti R., Buxton J., Joly M., and Corvera S. (1994) Insulin-sensitive association of GLUT-4 with endocytic clathrin-coated vesicles revealed with the use of brefeldin A. J. Biol. Chem. 269, 7926-7933.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7926-7933
    • Chakrabarti, R.1    Buxton, J.2    Joly, M.3    Corvera, S.4
  • 12
    • 0028904053 scopus 로고
    • Insulin action and the insulin signaling network
    • Cheatham B. and Kahn C. R. (1995) Insulin action and the insulin signaling network. Endocr. Rev. 16, 117-142.
    • (1995) Endocr. Rev. , vol.16 , pp. 117-142
    • Cheatham, B.1    Kahn, C.R.2
  • 13
    • 0025248571 scopus 로고
    • Inhibition of forskolin-induced neurite outgrowth and protein phosphorylation by a newly synthesized selective inhibitor of cyclic AMP-dependent protein kinase, N[2-(p-bromocinnamylamino)ethyl]-5-isoquinolinesulfonamide (H-89), of PC12D pheochromocytoma cells
    • Chijiwa T., Mishima A., Hagiwara M., Sano M., Hayashi K., Inoue T., Naito K., Toshioka T., and Hidaka H. (1990) Inhibition of forskolin-induced neurite outgrowth and protein phosphorylation by a newly synthesized selective inhibitor of cyclic AMP-dependent protein kinase, N[2-(p-bromocinnamylamino)ethyl]-5-isoquinolinesulfonamide (H-89), of PC12D pheochromocytoma cells. J. Biol. Chem. 265, 5267-5272.
    • (1990) J. Biol. Chem. , vol.265 , pp. 5267-5272
    • Chijiwa, T.1    Mishima, A.2    Hagiwara, M.3    Sano, M.4    Hayashi, K.5    Inoue, T.6    Naito, K.7    Toshioka, T.8    Hidaka, H.9
  • 14
    • 0027418067 scopus 로고
    • Overexpression of protein kinase C isoenzymes α, β1, γ, and ε in cells overexpressing the insulin receptor. Effects on receptor phosphorylation and signaling
    • Chin J. E., Dickens M., Tavare J. M., and Roth R. A. (1993) Overexpression of protein kinase C isoenzymes α, β1, γ, and ε in cells overexpressing the insulin receptor. Effects on receptor phosphorylation and signaling. J. Biol. Chem. 268, 6338-6347.
    • (1993) J. Biol. Chem. , vol.268 , pp. 6338-6347
    • Chin, J.E.1    Dickens, M.2    Tavare, J.M.3    Roth, R.A.4
  • 15
    • 0029055746 scopus 로고
    • Protein kinase C is increased in the liver of humans and rats with non-insulin-dependent diabetes mellitus: An alteration not due to hyperglycemia
    • Considine R. V., Nyce M. R., Allen L. E., Morales L. M., Triester S., Serrano J., Colberg J., Lanza-Jacoby S., and Caro J. F. (1995) Protein kinase C is increased in the liver of humans and rats with non-insulin-dependent diabetes mellitus: an alteration not due to hyperglycemia. J. Clin. Invest. 95, 2938-2944.
    • (1995) J. Clin. Invest. , vol.95 , pp. 2938-2944
    • Considine, R.V.1    Nyce, M.R.2    Allen, L.E.3    Morales, L.M.4    Triester, S.5    Serrano, J.6    Colberg, J.7    Lanza-Jacoby, S.8    Caro, J.F.9
  • 16
    • 0028945928 scopus 로고
    • The transient nicotinic stimulation of tyrosine hydroxylase gene transcription in bovine adrenal chromaffin cells is independent of c-fos gene activation
    • Craviso G. L., Hemelt V. B., and Waymire J. C. (1995) The transient nicotinic stimulation of tyrosine hydroxylase gene transcription in bovine adrenal chromaffin cells is independent of c-fos gene activation. Mol. Brain Res. 29, 233-244.
    • (1995) Mol. Brain Res. , vol.29 , pp. 233-244
    • Craviso, G.L.1    Hemelt, V.B.2    Waymire, J.C.3
  • 17
    • 0023881983 scopus 로고
    • Bovine chromaffin cells have insulin-like growth factor-I (IGF-I) receptors: IGF-I enhances catecholamine secretion
    • Dahmer M. K. and Perlman R. L. (1988) Bovine chromaffin cells have insulin-like growth factor-I (IGF-I) receptors: IGF-I enhances catecholamine secretion. J. Neurochem. 51, 321-323.
    • (1988) J. Neurochem. , vol.51 , pp. 321-323
    • Dahmer, M.K.1    Perlman, R.L.2
  • 18
    • 0025352515 scopus 로고
    • Chromaffin cells express two types of insulin-like growth factor receptors
    • Danielsen A., Larsen E., and Gammeltoft S. (1990) Chromaffin cells express two types of insulin-like growth factor receptors. Brain Res. 518, 95-100.
    • (1990) Brain Res. , vol.518 , pp. 95-100
    • Danielsen, A.1    Larsen, E.2    Gammeltoft, S.3
  • 19
    • 0029097626 scopus 로고
    • Activation of protein kinase C α inhibits signaling by members of the insulin receptor family
    • Danielsen A. G., Liu F., Hosomi Y., Shii K., and Roth R. A. (1995) Activation of protein kinase C α inhibits signaling by members of the insulin receptor family. J. Biol. Chem. 270, 21600-21605.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21600-21605
    • Danielsen, A.G.1    Liu, F.2    Hosomi, Y.3    Shii, K.4    Roth, R.A.5
  • 20
    • 0017334323 scopus 로고
    • Increased insulin binding by hepatic plasma membranes from diabetic rats
    • Davidson M. B. and Kaplan S. A. (1977) Increased insulin binding by hepatic plasma membranes from diabetic rats. J. Clin. Invest. 59, 22-30.
    • (1977) J. Clin. Invest. , vol.59 , pp. 22-30
    • Davidson, M.B.1    Kaplan, S.A.2
  • 21
    • 0027179841 scopus 로고
    • Receptor and protein kinase C-mediated regulation of ARF binding to the Golgi complex
    • De Matteis M. A., Santini G., Kahn R. A., Di Tullio G., and Luini A. (1993) Receptor and protein kinase C-mediated regulation of ARF binding to the Golgi complex. Nature 364, 818-821.
    • (1993) Nature , vol.364 , pp. 818-821
    • De Matteis, M.A.1    Santini, G.2    Kahn, R.A.3    Di Tullio, G.4    Luini, A.5
  • 22
    • 0028814675 scopus 로고
    • The developing CNS: A scenario for the action of proinsulin, insulin and insulin-like growth factors
    • de Pablo F. and de la Rosa E. J. (1995) The developing CNS: a scenario for the action of proinsulin, insulin and insulin-like growth factors. Trends Neurosci. 18, 143-150.
    • (1995) Trends Neurosci. , vol.18 , pp. 143-150
    • De Pablo, F.1    De La Rosa, E.J.2
  • 23
    • 0028485768 scopus 로고
    • PC12 cells overexpressing the insulin receptor undergo insulin-dependent neuronal differentiation
    • Dikic I., Schlessinger J., and Lax I. (1994) PC12 cells overexpressing the insulin receptor undergo insulin-dependent neuronal differentiation. Curr. Biol. 4, 702-708.
    • (1994) Curr. Biol. , vol.4 , pp. 702-708
    • Dikic, I.1    Schlessinger, J.2    Lax, I.3
  • 24
    • 0029969135 scopus 로고    scopus 로고
    • GLUT1-mediated glucose transport and its regulation by IGF-I in cultured bovine chromaffin cells
    • Fladeby C., Bjønness B., and Serck-Hanssen G. (1996) GLUT1-mediated glucose transport and its regulation by IGF-I in cultured bovine chromaffin cells. J. Cell. Physiol. 169, 242-247.
    • (1996) J. Cell. Physiol. , vol.169 , pp. 242-247
    • Fladeby, C.1    Bjønness, B.2    Serck-Hanssen, G.3
  • 25
    • 0032557451 scopus 로고    scopus 로고
    • In NIH-3T3 fibroblasts, insulin receptor interaction with specific protein kinase C isoforms controls receptor intracellular routing
    • Formisano P., Oriente F., Miele C., Caruso M., Auricchio R., Vigliotta G., Condorelli G., and Beguinot F. (1998) In NIH-3T3 fibroblasts, insulin receptor interaction with specific protein kinase C isoforms controls receptor intracellular routing. J. Biol. Chem. 273, 13197-13202.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13197-13202
    • Formisano, P.1    Oriente, F.2    Miele, C.3    Caruso, M.4    Auricchio, R.5    Vigliotta, G.6    Condorelli, G.7    Beguinot, F.8
  • 27
    • 0028146956 scopus 로고
    • High glucose and insulin decrease fetal lung insulin receptor mRNA and tyrosine kinase activity in vitro
    • Gewolb I. H., O'Brien J., Palese T. A., and Phillip M. (1994) High glucose and insulin decrease fetal lung insulin receptor mRNA and tyrosine kinase activity in vitro. Biochem. Biophys. Res. Commun. 202, 694-700.
    • (1994) Biochem. Biophys. Res. Commun. , vol.202 , pp. 694-700
    • Gewolb, I.H.1    O'Brien, J.2    Palese, T.A.3    Phillip, M.4
  • 28
    • 0028907314 scopus 로고
    • Role of p70 s6 protein kinase in angiotensin II-induced protein synthesis in vascular smooth muscle cells
    • Giasson E. and Meloche S. (1995) Role of p70 S6 protein kinase in angiotensin II-induced protein synthesis in vascular smooth muscle cells. J. Biol. Chem. 270, 5225-5231.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5225-5231
    • Giasson, E.1    Meloche, S.2
  • 29
    • 0030599453 scopus 로고    scopus 로고
    • Atypical isoforms of PKC and insulin secretion from pancreatic β-cells: Evidence using G̈6976 and Ro 31-8220 as PKC inhibitors
    • Harris T. E., Persaud S. J., and Jones P. M. (1996) Atypical isoforms of PKC and insulin secretion from pancreatic β-cells: evidence using G̈6976 and Ro 31-8220 as PKC inhibitors. Biochem. Biophys. Res. Commun. 227, 672-676.
    • (1996) Biochem. Biophys. Res. Commun. , vol.227 , pp. 672-676
    • Harris, T.E.1    Persaud, S.J.2    Jones, P.M.3
  • 30
    • 0024545982 scopus 로고
    • Effects of growth and insulin treatment on the levels of insulin receptors and their mRNA in Hep G2 cells
    • Hatada E. N., McClain D. A., Potter E., Ullrich A., and Olefsky J. M. (1989) Effects of growth and insulin treatment on the levels of insulin receptors and their mRNA in Hep G2 cells. J. Biol. Chem. 264, 6741-6747.
    • (1989) J. Biol. Chem. , vol.264 , pp. 6741-6747
    • Hatada, E.N.1    McClain, D.A.2    Potter, E.3    Ullrich, A.4    Olefsky, J.M.5
  • 31
    • 0028812135 scopus 로고
    • Glucose-induced stimulation of human insulin-receptor mRNA and tyrosine kinase activity in cultured cells
    • Hauguel-de-Mouzon S., Mrejen C., Alengrin F., and Van Obberghen E. (1995) Glucose-induced stimulation of human insulin-receptor mRNA and tyrosine kinase activity in cultured cells. Biochem. J. 305, 119-124.
    • (1995) Biochem. J. , vol.305 , pp. 119-124
    • Hauguel-De-Mouzon, S.1    Mrejen, C.2    Alengrin, F.3    Van Obberghen, E.4
  • 34
    • 0024603065 scopus 로고
    • MgATP-independent and MgATP-dependent exocytosis. Evidence that MgATP primes adrenal chromaffin cells to undergo exocytosis
    • Holz R. W., Bittner M. A., Peppers S. C., Senter R. A., and Eberhard D. A. (1989) MgATP-independent and MgATP-dependent exocytosis. Evidence that MgATP primes adrenal chromaffin cells to undergo exocytosis. J. Biol. Chem. 264, 5412-5419.
    • (1989) J. Biol. Chem. , vol.264 , pp. 5412-5419
    • Holz, R.W.1    Bittner, M.A.2    Peppers, S.C.3    Senter, R.A.4    Eberhard, D.A.5
  • 35
    • 0033529561 scopus 로고    scopus 로고
    • Effect of alternative glycosylation on insulin receptor processing
    • Hwang J. B. and Frost S. C. (1999) Effect of alternative glycosylation on insulin receptor processing. J. Biol. Chem. 274, 22813-22820.
    • (1999) J. Biol. Chem. , vol.274 , pp. 22813-22820
    • Hwang, J.B.1    Frost, S.C.2
  • 36
    • 0027977387 scopus 로고
    • Insulin's effect on protein kinase C and diacylglycerol induced by diabetes and glucose in vascular tissues
    • Inoguchi T., Xia P., Kunisaki M., Higashi S., Feener E. P., and King G. L. (1994) Insulin's effect on protein kinase C and diacylglycerol induced by diabetes and glucose in vascular tissues. Am. J. Physiol. 267, E369-E379.
    • (1994) Am. J. Physiol. , vol.267
    • Inoguchi, T.1    Xia, P.2    Kunisaki, M.3    Higashi, S.4    Feener, E.P.5    King, G.L.6
  • 37
    • 0030720512 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase is required for the formation of constitutive transport vesicles from the TGN
    • Jones S. M. 61nd Howell K. E. (1997) Phosphatidylinositol 3-kinase is required for the formation of constitutive transport vesicles from the TGN. J. Cell Biol. 139, 339-349.
    • (1997) J. Cell Biol. , vol.139 , pp. 339-349
    • Jones, S.M.1    Howell, K.E.2
  • 38
    • 0021745904 scopus 로고
    • Decreased autophosphorylation of the insulin receptor-kinase in streptozotocin-diabetic rats
    • Kadowaki T., Kasuga M., Akanuma Y., Ezaki O., and Takaku F. (1984) Decreased autophosphorylation of the insulin receptor-kinase in streptozotocin-diabetic rats. J. Biol. Chem. 259, 14208-14216.
    • (1984) J. Biol. Chem. , vol.259 , pp. 14208-14216
    • Kadowaki, T.1    Kasuga, M.2    Akanuma, Y.3    Ezaki, O.4    Takaku, F.5
  • 39
    • 0025761974 scopus 로고
    • Cellular trafficking and processing of the insulin receptor
    • Knutson V. P. (1991) Cellular trafficking and processing of the insulin receptor. FASEB J. 5, 2130-2138.
    • (1991) FASEB J. , vol.5 , pp. 2130-2138
    • Knutson, V.P.1
  • 40
    • 0018379923 scopus 로고
    • Effects of streptozotocin-induced diabetes on insulin binding, glucose transport, and intracellular glucose metabolism in isolated rat adipocytes
    • Kobayashi M. and Olefsky J. M. (1979) Effects of streptozotocin-induced diabetes on insulin binding, glucose transport, and intracellular glucose metabolism in isolated rat adipocytes. Diabetes 28, 87-95.
    • (1979) Diabetes , vol.28 , pp. 87-95
    • Kobayashi, M.1    Olefsky, J.M.2
  • 41
    • 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
  • 42
    • 0028903869 scopus 로고
    • The effect of 1,25-dihydroxyvitamin D3 on insulin binding, insulin receptor mRNA levels, and isotype RNA pattern in U-937 human promonocytic cells
    • Leal M. A., Aller P., Mas A., and Calle C. (1995) The effect of 1,25-dihydroxyvitamin D3 on insulin binding, insulin receptor mRNA levels, and isotype RNA pattern in U-937 human promonocytic cells. Exp. Cell Res. 217, 189-194.
    • (1995) Exp. Cell Res. , vol.217 , pp. 189-194
    • Leal, M.A.1    Aller, P.2    Mas, A.3    Calle, C.4
  • 43
    • 0026705304 scopus 로고
    • Identification of cis-and trans-acting factors regulating the expression of the human insulin receptor gene
    • Lee J. K., Tam J. W., Tsai M. J., and Tsai S. Y. (1992) Identification of cis-and trans-acting factors regulating the expression of the human insulin receptor gene. J. Biol. Chem. 267, 4638-4645.
    • (1992) J. Biol. Chem. , vol.267 , pp. 4638-4645
    • Lee, J.K.1    Tam, J.W.2    Tsai, M.J.3    Tsai, S.Y.4
  • 44
    • 0026487343 scopus 로고
    • Regulation of insulin receptor gene expression. Cell cycle-mediated effects on insulin receptor mRNA stability
    • Levy J. R. and Hug V. (1992) Regulation of insulin receptor gene expression. Cell cycle-mediated effects on insulin receptor mRNA stability. J. Biol. Chem. 267, 25289-25295.
    • (1992) J. Biol. Chem. , vol.267 , pp. 25289-25295
    • Levy, J.R.1    Hug, V.2
  • 45
    • 0029997477 scopus 로고    scopus 로고
    • Evidence for a role of conventional protein kinase-C α in the control of homotypic contacts and cell scattering of HT-29 human intestinal cells
    • Llosas M. D., Batlle E., Coll O., Skoudy A., Fabre M., and Garcia de Herreros A. (1996) Evidence for a role of conventional protein kinase-C α in the control of homotypic contacts and cell scattering of HT-29 human intestinal cells. Biochem. J. 315, 1049-1054.
    • (1996) Biochem. J. , vol.315 , pp. 1049-1054
    • Llosas, M.D.1    Batlle, E.2    Coll, O.3    Skoudy, A.4    Fabre, M.5    Garcia De Herreros, A.6
  • 46
    • 0028872649 scopus 로고
    • Specificity of receptor tyrosine kinase signaling: Transient versus sustained extracellular signal-regulated kinase activation
    • Marshall C. J. (1995) Specificity of receptor tyrosine kinase signaling: transient versus sustained extracellular signal-regulated kinase activation. Cell 80, 179-185.
    • (1995) Cell , vol.80 , pp. 179-185
    • Marshall, C.J.1
  • 48
    • 0031029249 scopus 로고    scopus 로고
    • Nuclear translocation of PKC ζ during ischemia and its inhibition by wortmannin, an inhibitor of phosphatidylinositol 3-kinase
    • Mizukami Y., Hirata T., and Yoshida K. (1997) Nuclear translocation of PKC ζ during ischemia and its inhibition by wortmannin, an inhibitor of phosphatidylinositol 3-kinase. FEBS Lett. 401, 247-251.
    • (1997) FEBS Lett. , vol.401 , pp. 247-251
    • Mizukami, Y.1    Hirata, T.2    Yoshida, K.3
  • 49
    • 0031964645 scopus 로고    scopus 로고
    • Anchoring proteins for protein kinase C: A means for isozyme selectivity
    • Mochly-Rosen D. and Gordon A. S. (1998) Anchoring proteins for protein kinase C: a means for isozyme selectivity. FASEB J. 12, 35-42.
    • (1998) FASEB J. , vol.12 , pp. 35-42
    • Mochly-Rosen, D.1    Gordon, A.S.2
  • 50
    • 0030659646 scopus 로고    scopus 로고
    • Cloning and expression of a cDNA encoding a bovine brain brefeldin A-sensitive guanine nucleotide-exchange protein for ADP-ribosylation factor
    • Morinaga N., Moss J., and Vaughan M. (1997) Cloning and expression of a cDNA encoding a bovine brain brefeldin A-sensitive guanine nucleotide-exchange protein for ADP-ribosylation factor. Proc. Natl. Acad. Sci. USA 94, 12926-12931.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12926-12931
    • Morinaga, N.1    Moss, J.2    Vaughan, M.3
  • 51
    • 0029015710 scopus 로고
    • Structure and function of ARF proteins: Activators of cholera toxin and critical components of intracellular vesicular transport processes
    • Moss J. and Vaughan M. (1995) Structure and function of ARF proteins: activators of cholera toxin and critical components of intracellular vesicular transport processes. J. Biol. Chem. 270, 12327-12330.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12327-12330
    • Moss, J.1    Vaughan, M.2
  • 52
    • 0030987070 scopus 로고    scopus 로고
    • Regulation of protein kinase C
    • Newton A. C. (1997) Regulation of protein kinase C. Curr. Opin. Cell Biol. 9, 161-167.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 161-167
    • Newton, A.C.1
  • 53
    • 0029915031 scopus 로고    scopus 로고
    • P70 S6 kinase: An enigma with variations
    • Proud C. G. (1996) p70 S6 kinase: an enigma with variations. Trends Biochem. Sci. 21, 181-185.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 181-185
    • Proud, C.G.1
  • 54
    • 0025744290 scopus 로고
    • Insulin downregulates the steady-state level of its receptor's messenger ribonucleic acid
    • Rohilla A. M., Anderson C., Wood W. M., and Berhanu P. (1991) Insulin downregulates the steady-state level of its receptor's messenger ribonucleic acid. Biochem. Biophys. Res. Commun. 175, 520-526.
    • (1991) Biochem. Biophys. Res. Commun. , vol.175 , pp. 520-526
    • Rohilla, A.M.1    Anderson, C.2    Wood, W.M.3    Berhanu, P.4
  • 55
    • 0025163076 scopus 로고
    • Identification of retinal insulin receptors using site-specific antibodies to a carboxyl-terminal peptide of the human insulin receptor α-subunit. Up-regulation of neuronal insulin receptors in diabetes
    • Rosenzweig S. A., Zetterstrom C., and Benjamin A. (1990) Identification of retinal insulin receptors using site-specific antibodies to a carboxyl-terminal peptide of the human insulin receptor α-subunit. Up-regulation of neuronal insulin receptors in diabetes. J. Biol. Chem. 265, 18030-18034.
    • (1990) J. Biol. Chem. , vol.265 , pp. 18030-18034
    • Rosenzweig, S.A.1    Zetterstrom, C.2    Benjamin, A.3
  • 56
    • 0029165020 scopus 로고
    • MRNA stability in mammalian cells
    • Ross J. (1995) mRNA stability in mammalian cells. Microbiol. Rev. 59, 423-450.
    • (1995) Microbiol. Rev. , vol.59 , pp. 423-450
    • Ross, J.1
  • 58
    • 0028232859 scopus 로고
    • Regulation of insulin receptor, insulin receptor substrate-1 and phosphatidylinositol 3-kinase in 3T3-F442A adipocytes. Effects of differentiation, insulin, and dexamethasone
    • Saad M. J., Folli F., Araki E., Hashimoto N., Csermely P., and Kahn C. R. (1994) Regulation of insulin receptor, insulin receptor substrate-1 and phosphatidylinositol 3-kinase in 3T3-F442A adipocytes. Effects of differentiation, insulin, and dexamethasone. Mol. Endocrinol. 8, 545-557.
    • (1994) Mol. Endocrinol. , vol.8 , pp. 545-557
    • Saad, M.J.1    Folli, F.2    Araki, E.3    Hashimoto, N.4    Csermely, P.5    Kahn, C.R.6
  • 59
    • 0029791502 scopus 로고    scopus 로고
    • Transport of protein kinase C α into the nucleus requires intact cytoskeleton while the transport of a protein containing a canonical nuclear localization signal does not
    • Schmalz D., Kalkbrenner F., Hucho F., and Buchner K. (1996) Transport of protein kinase C α into the nucleus requires intact cytoskeleton while the transport of a protein containing a canonical nuclear localization signal does not. J. Cell Sci. 109, 2401-2406.
    • (1996) J. Cell Sci. , vol.109 , pp. 2401-2406
    • Schmalz, D.1    Kalkbrenner, F.2    Hucho, F.3    Buchner, K.4
  • 60
    • 0031826010 scopus 로고    scopus 로고
    • Nuclear import of protein kinase C occurs by a mechanism distinct from the mechanism used by protein with a classical nuclear localization signal
    • Schmalz D., Hucho F., and Buchner K. (1998) Nuclear import of protein kinase C occurs by a mechanism distinct from the mechanism used by protein with a classical nuclear localization signal. J. Cell Sci. 111, 1823-1830.
    • (1998) J. Cell Sci. , vol.111 , pp. 1823-1830
    • Schmalz, D.1    Hucho, F.2    Buchner, K.3
  • 61
    • 0027991035 scopus 로고
    • Brefeldin A down-regulates the transferrin receptors in K562 cells
    • Schonhorn J. E. and Wessling-Resnick M. (1994) Brefeldin A down-regulates the transferrin receptors in K562 cells. Mol. Cell. Biochem. 135, 159-169.
    • (1994) Mol. Cell. Biochem. , vol.135 , pp. 159-169
    • Schonhorn, J.E.1    Wessling-Resnick, M.2
  • 62
    • 0029896749 scopus 로고    scopus 로고
    • Interactions of protein kinase C with insulin signaling. Influence on GAP and Sos activities
    • Schubert C., Carel K., DePaolo D., Leitner W., and Draznin B. (1996) Interactions of protein kinase C with insulin signaling. Influence on GAP and Sos activities. J. Biol. Chem. 271, 15311-15314.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15311-15314
    • Schubert, C.1    Carel, K.2    DePaolo, D.3    Leitner, W.4    Draznin, B.5
  • 63
    • 0030222298 scopus 로고    scopus 로고
    • Receptor signalling and the regulation of endocytic membrane transport
    • Seaman M. N., Burd C. G., and Emr S. D. (1996) Receptor signalling and the regulation of endocytic membrane transport. Curr. Opin. Cell Biol. 8, 549-556.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 549-556
    • Seaman, M.N.1    Burd, C.G.2    Emr, S.D.3
  • 64
    • 0029068521 scopus 로고
    • Rapid and long-term effects on protein kinase C on receptor tyrosine kinase phosphorylation and degradation
    • Seedorf K., Shearman M., and Ullrich A. (1995) Rapid and long-term effects on protein kinase C on receptor tyrosine kinase phosphorylation and degradation. J. Biol. Chem. 270, 18953-18960.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18953-18960
    • Seedorf, K.1    Shearman, M.2    Ullrich, A.3
  • 65
    • 0030020443 scopus 로고    scopus 로고
    • Differential regulation of histamine-and bradykinin-stimulated phospholipase C in adrenal chromaffin cells: Evidence for involvement of different protein kinase C isoforms
    • Sena C. M., Rosário L. M., Parker P. J., Patel V., and Boarder M. R. (1996) Differential regulation of histamine-and bradykinin-stimulated phospholipase C in adrenal chromaffin cells: evidence for involvement of different protein kinase C isoforms. J. Neurochem. 66, 1086-1094.
    • (1996) J. Neurochem. , vol.66 , pp. 1086-1094
    • Sena, C.M.1    Rosário, L.M.2    Parker, P.J.3    Patel, V.4    Boarder, M.R.5
  • 66
    • 0028310844 scopus 로고
    • Stimulation of protein phosphatase-1 activity by phorbol esters. Evaluation of the regulatory role of protein kinase C in insulin action
    • Srinivasan M. and Begum N. (1994) Stimulation of protein phosphatase-1 activity by phorbol esters. Evaluation of the regulatory role of protein kinase C in insulin action. J. Biol. Chem. 269, 16662-16667.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16662-16667
    • Srinivasan, M.1    Begum, N.2
  • 68
    • 0029948401 scopus 로고    scopus 로고
    • Differential modulation of protein kinase C isozymes in rat parotid acinar cells
    • Terzian A. R., Zhang X., and Rubin R. P. (1996) Differential modulation of protein kinase C isozymes in rat parotid acinar cells. Biochem. Pharmacol. 52, 569-577.
    • (1996) Biochem. Pharmacol. , vol.52 , pp. 569-577
    • Terzian, A.R.1    Zhang, X.2    Rubin, R.P.3
  • 69
    • 0024442077 scopus 로고
    • Characterization of the promoter regions and 3′ end of the human insulin receptor gene
    • Tewari D. S., Cook D. M., and Taub R. (1989) Characterization of the promoter regions and 3′ end of the human insulin receptor gene. J. Biol. Chem. 264, 16238-16245.
    • (1989) J. Biol. Chem. , vol.264 , pp. 16238-16245
    • Tewari, D.S.1    Cook, D.M.2    Taub, R.3
  • 70
    • 0028947293 scopus 로고
    • A single pulse of nerve growth factor triggers long-term neuronal excitability through sodium channel gene induction
    • Toledo-Aral J. J., Brehm P., Halegoua S., and Mandel G. (1995) A single pulse of nerve growth factor triggers long-term neuronal excitability through sodium channel gene induction. Neuron 14, 607-611.
    • (1995) Neuron , vol.14 , pp. 607-611
    • Toledo-Aral, J.J.1    Brehm, P.2    Halegoua, S.3    Mandel, G.4
  • 71
    • 0026061706 scopus 로고
    • Long-term activation of protein kinase C by angiotensin II in cultured bovine adrenal medullary cells
    • Tuominen R. K., Hudson P. M., McMillian M. K., Ye H., Stachowiak M. K., and Hong J.-S. (1991) Long-term activation of protein kinase C by angiotensin II in cultured bovine adrenal medullary cells. J. Neurochem. 56, 1292-1298.
    • (1991) J. Neurochem. , vol.56 , pp. 1292-1298
    • Tuominen, R.K.1    Hudson, P.M.2    McMillian, M.K.3    Ye, H.4    Stachowiak, M.K.5    Hong, J.-S.6
  • 72
  • 74
    • 0029854499 scopus 로고    scopus 로고
    • Protein kinase C bound to the Golgi apparatus supports the formation of constitutive transport vesicles
    • Westermann P., Knoblich M., Maier O., Lindschau C., and Haller H. (1996) Protein kinase C bound to the Golgi apparatus supports the formation of constitutive transport vesicles. Biochem. J. 320, 651-658.
    • (1996) Biochem. J. , vol.320 , pp. 651-658
    • Westermann, P.1    Knoblich, M.2    Maier, O.3    Lindschau, C.4    Haller, H.5
  • 75
    • 0022195442 scopus 로고
    • Relationship between the regulation of enkephalin-containing peptide and dopamine-β-hydroxylase levels in cultured adrenal chromaffin cells
    • Wilson S. P., Viveros O. H., and Kirshner N. (1985) Relationship between the regulation of enkephalin-containing peptide and dopamine-β-hydroxylase levels in cultured adrenal chromaffin cells. J. Neurochem. 45, 1363-1370.
    • (1985) J. Neurochem. , vol.45 , pp. 1363-1370
    • Wilson, S.P.1    Viveros, O.H.2    Kirshner, N.3
  • 76
    • 0029813804 scopus 로고    scopus 로고
    • Up-regulation of functional voltage-dependent sodium channels by insulin in cultured bovine adrenal chromaffin cells
    • Yamamoto R., Yanagita T., Kobayashi H., Yuhi T., Yokoo H., and Wada A. (1996) Up-regulation of functional voltage-dependent sodium channels by insulin in cultured bovine adrenal chromaffin cells. J. Neurochem. 67, 1401-1408.
    • (1996) J. Neurochem. , vol.67 , pp. 1401-1408
    • Yamamoto, R.1    Yanagita, T.2    Kobayashi, H.3    Yuhi, T.4    Yokoo, H.5    Wada, A.6
  • 77
    • 0030022581 scopus 로고    scopus 로고
    • Protein kinase C-mediated down-regulation of voltage-dependent sodium channels in adrenal chromaffin cells
    • Yanagita T., Wada A., Yamamoto R., Kobayashi H., Yuhi T., Urabe M., and Niina H. (1996) Protein kinase C-mediated down-regulation of voltage-dependent sodium channels in adrenal chromaffin cells. J. Neurochem. 66, 1249-1253.
    • (1996) J. Neurochem. , vol.66 , pp. 1249-1253
    • Yanagita, T.1    Wada, A.2    Yamamoto, R.3    Kobayashi, H.4    Yuhi, T.5    Urabe, M.6    Niina, H.7
  • 79
    • 0034023605 scopus 로고    scopus 로고
    • Protein kinase C-α and -ε down-regulate cell surface sodium channels via differential mechanisms in adrenal chromaffin cells
    • Yanagita T., Kobayashi H., Yamamoto R., Kataoka H., Yokoo H., Shiraishi S., Minami S., Koono M., and Wada A. (2000) Protein kinase C-α and -ε down-regulate cell surface sodium channels via differential mechanisms in adrenal chromaffin cells. J. Neurochem. 74, 1674-1684.
    • (2000) J. Neurochem. , vol.74 , pp. 1674-1684
    • Yanagita, T.1    Kobayashi, H.2    Yamamoto, R.3    Kataoka, H.4    Yokoo, H.5    Shiraishi, S.6    Minami, S.7    Koono, M.8    Wada, A.9
  • 80
    • 0026704151 scopus 로고
    • Differential expression of retinal insulin receptors in STZ-induced diabetic rats
    • Zetterström C., Benjamin A., and Rosenzweig S. A. (1992) Differential expression of retinal insulin receptors in STZ-induced diabetic rats. Diabetes 41, 818-825.
    • (1992) Diabetes , vol.41 , pp. 818-825
    • Zetterström, C.1    Benjamin, A.2    Rosenzweig, S.A.3


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