메뉴 건너뛰기




Volumn 45, Issue 38, 2006, Pages 11605-11615

Involvement of insulin-like growth factor type 1 receptor and protein kinase Cδ in bis(maltolato)oxovanadium(IV)-induced phosphorylation of protein kinase B in HepG2 cells

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; CELLS; ENZYME KINETICS; GLUCOSE; INSULIN; MOLECULAR DYNAMICS;

EID: 33749039500     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi060403x     Document Type: Article
Times cited : (20)

References (71)
  • 1
    • 13244292329 scopus 로고    scopus 로고
    • Insulino-mimetic and anti-diabetic effects of vanadium compounds
    • Srivastava, A. K., and Mehdi, M. Z. (2005) Insulino-mimetic and anti-diabetic effects of vanadium compounds, Diabetes Med. 22, 2-13.
    • (2005) Diabetes Med. , vol.22 , pp. 2-13
    • Srivastava, A.K.1    Mehdi, M.Z.2
  • 2
    • 0032510713 scopus 로고    scopus 로고
    • Vanadyl sulfate-stimulated glycogen synthesis is associated with activation of phosphatidylinositol 3-kinase and is independent of insulin receptor tyrosine phosphorylation
    • Pandey, S. K., Anand-Srivastava, M. B., and Srivastava, A. K. (1998) Vanadyl sulfate-stimulated glycogen synthesis is associated with activation of phosphatidylinositol 3-kinase and is independent of insulin receptor tyrosine phosphorylation, Biochemistry 37, 7006-7014.
    • (1998) Biochemistry , vol.37 , pp. 7006-7014
    • Pandey, S.K.1    Anand-Srivastava, M.B.2    Srivastava, A.K.3
  • 3
    • 23744448553 scopus 로고    scopus 로고
    • Organo-vanadium compounds are potent activators of the protein kinase B signaling pathway and protein tyrosine phosphorylation: Mechanism of insulinomimesis
    • Mehdi, M. Z., and Srivastava, A. K. (2005) Organo-vanadium compounds are potent activators of the protein kinase B signaling pathway and protein tyrosine phosphorylation: Mechanism of insulinomimesis, Arch. Biochem. Biophys. 440, 158-164.
    • (2005) Arch. Biochem. Biophys. , vol.440 , pp. 158-164
    • Mehdi, M.Z.1    Srivastava, A.K.2
  • 4
    • 0040366479 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase requirement in activation of the ras/C-raf-1/MEK/ERK and p70(s6k) signaling cascade by the insulinomimetic agent vanadyl sulfate
    • Pandey, S. K., Theberge, J. F., Bernier, M., and Srivastava, A. K. (1999) Phosphatidylinositol 3-kinase requirement in activation of the ras/C-raf-1/MEK/ERK and p70(s6k) signaling cascade by the insulinomimetic agent vanadyl sulfate, Biochemistry 38, 14667-14675.
    • (1999) Biochemistry , vol.38 , pp. 14667-14675
    • Pandey, S.K.1    Theberge, J.F.2    Bernier, M.3    Srivastava, A.K.4
  • 6
    • 17144395975 scopus 로고    scopus 로고
    • The activation of Akt/PKB signaling pathway and cell survival
    • Song, G., Ouyang, G., and Bao, S. (2005) The activation of Akt/PKB signaling pathway and cell survival, J. Cell. Mol. Med. 9, 59-71.
    • (2005) J. Cell. Mol. Med. , vol.9 , pp. 59-71
    • Song, G.1    Ouyang, G.2    Bao, S.3
  • 7
    • 0027329076 scopus 로고
    • Improvement in cardiac dysfunction in streptozotocin-induced diabetic rats following chronic oral administration of bis(maltolato)oxovanadium(IV)
    • Yuen, V. G., Orvig, C., Thompson, K. H., and McNeill, J. H. (1993) Improvement in cardiac dysfunction in streptozotocin-induced diabetic rats following chronic oral administration of bis(maltolato)oxovanadium(IV), Can. J. Physiol. Pharmacol. 71, 270-276.
    • (1993) Can. J. Physiol. Pharmacol. , vol.71 , pp. 270-276
    • Yuen, V.G.1    Orvig, C.2    Thompson, K.H.3    McNeill, J.H.4
  • 8
    • 0033406265 scopus 로고    scopus 로고
    • Evidence for the improvement of noninsulin-dependent diabetes mellitus in KKAy mice with daily oral administration of bis(6-methylpicolinato) oxovanadium(IV) complex
    • Fujisawa, Y., and Sakurai, H. (1999) Evidence for the improvement of noninsulin-dependent diabetes mellitus in KKAy mice with daily oral administration of bis(6-methylpicolinato)oxovanadium(IV) complex, Chem. Pharm. Bull. 47, 1668-1670.
    • (1999) Chem. Pharm. Bull. , vol.47 , pp. 1668-1670
    • Fujisawa, Y.1    Sakurai, H.2
  • 9
    • 0032929963 scopus 로고    scopus 로고
    • Effects of vanadium complexes with organic ligands on glucose metabolism: A comparison study in diabetic rats
    • Reul, B. A., Amin, S. S., Buchet, J. P., Ongemba, L. N., Crans, D. C., and Brichard, S. M. (1999) Effects of vanadium complexes with organic ligands on glucose metabolism: A comparison study in diabetic rats, Br. J. Pharmacol. 126, 467-477.
    • (1999) Br. J. Pharmacol. , vol.126 , pp. 467-477
    • Reul, B.A.1    Amin, S.S.2    Buchet, J.P.3    Ongemba, L.N.4    Crans, D.C.5    Brichard, S.M.6
  • 10
    • 14344255690 scopus 로고    scopus 로고
    • A nonspecific phosphotyrosine phosphatase inhibitor, bis(maltolato) oxovanadium(IV), improves glucose tolerance and prevents diabetes in Zucker diabetic fatty rats
    • Winter, C. L., Lange, J. S., Davis, M. G., Gerwe, G. S., Downs, T. R., Peters, K. G., and Kasibhatla, B. (2005) A nonspecific phosphotyrosine phosphatase inhibitor, bis(maltolato)oxovanadium(IV), improves glucose tolerance and prevents diabetes in Zucker diabetic fatty rats, Exp. Biol. Med. (Maywood, NJ, U.S.) 230, 207-216.
    • (2005) Exp. Biol. Med. (Maywood, NJ, U.S.) , vol.230 , pp. 207-216
    • Winter, C.L.1    Lange, J.S.2    Davis, M.G.3    Gerwe, G.S.4    Downs, T.R.5    Peters, K.G.6    Kasibhatla, B.7
  • 11
    • 0036329131 scopus 로고    scopus 로고
    • Oral treatment with vanadium of Zucker fatty rats activates muscle glycogen synthesis and insulin-stimulated protein phosphatase-1 activity
    • Semiz, S., and McNeill, J. H. (2002) Oral treatment with vanadium of Zucker fatty rats activates muscle glycogen synthesis and insulin-stimulated protein phosphatase-1 activity, Mol. Cell. Biochem. 236, 123-131.
    • (2002) Mol. Cell. Biochem. , vol.236 , pp. 123-131
    • Semiz, S.1    McNeill, J.H.2
  • 12
    • 0036184822 scopus 로고    scopus 로고
    • Bis(maltolato)oxovanadium(IV) inhibits the activity of PTP1B in Zucker rat skeletal muscle in vivo
    • Mohammad, A., Wang, J., and McNeill, J. H. (2002) Bis(maltolato) oxovanadium(IV) inhibits the activity of PTP1B in Zucker rat skeletal muscle in vivo, Mol. Cell. Biochem. 229, 125-128.
    • (2002) Mol. Cell. Biochem. , vol.229 , pp. 125-128
    • Mohammad, A.1    Wang, J.2    McNeill, J.H.3
  • 13
    • 0036892912 scopus 로고    scopus 로고
    • Mechanisms by which bis(maltolato)oxovanadium(IV) normalizes phosphoenolpyruvate carboxykinase and glucose-6-phosphatase expression in streptozotocin-diabetic rats in vivo
    • Marzban, L., Rahimian, R., Brownsey, R. W., and McNeill, J. H. (2002) Mechanisms by which bis(maltolato)oxovanadium(IV) normalizes phosphoenolpyruvate carboxykinase and glucose-6-phosphatase expression in streptozotocin-diabetic rats in vivo, Endocrinology 143, 4636-4645.
    • (2002) Endocrinology , vol.143 , pp. 4636-4645
    • Marzban, L.1    Rahimian, R.2    Brownsey, R.W.3    McNeill, J.H.4
  • 14
    • 0027739879 scopus 로고
    • Does the insulin-mimetic action of vanadate involve insulin receptor kinase?
    • Pugazhenthi, S., and Khandelwal, R. L. (1993) Does the insulin-mimetic action of vanadate involve insulin receptor kinase? Mol. Cell. Biochem. 127-128, 211-218.
    • (1993) Mol. Cell. Biochem. , vol.127-128 , pp. 211-218
    • Pugazhenthi, S.1    Khandelwal, R.L.2
  • 15
    • 0025342047 scopus 로고
    • Effect of in vivo vanadate treatment on insulin receptor tyrosine kinase activity in partially pancreatectomized diabetic rats
    • Cordera, R., Andraghetti, G., DeFronzo, R. A., and Rossetti, L. (1990) Effect of in vivo vanadate treatment on insulin receptor tyrosine kinase activity in partially pancreatectomized diabetic rats, Endocrinology 126, 2177-2183.
    • (1990) Endocrinology , vol.126 , pp. 2177-2183
    • Cordera, R.1    Andraghetti, G.2    DeFronzo, R.A.3    Rossetti, L.4
  • 16
    • 0024416087 scopus 로고
    • Pervanadate [peroxide(s) of vanadate] mimics insulin action in rat adipocytes via activation of the insulin receptor tyrosine kinase
    • Fantus, I. G., Kadota, S., Deragon, G., Foster, B., and Posner, B. I. (1989) Pervanadate [peroxide(s) of vanadate] mimics insulin action in rat adipocytes via activation of the insulin receptor tyrosine kinase, Biochemistry 28, 8864-8871.
    • (1989) Biochemistry , vol.28 , pp. 8864-8871
    • Fantus, I.G.1    Kadota, S.2    Deragon, G.3    Foster, B.4    Posner, B.I.5
  • 17
    • 0028261579 scopus 로고
    • Activation of mitogen activated protein (MAP) kinases by vanadate is independent of insulin receptor autophosphorylation
    • D'Onofrio, F., Le, M. Q., Chiasson, J. L., and Srivastava, A. K. (1994) Activation of mitogen activated protein (MAP) kinases by vanadate is independent of insulin receptor autophosphorylation, FEBS Lett. 340, 269-275.
    • (1994) FEBS Lett. , vol.340 , pp. 269-275
    • D'Onofrio, F.1    Le, M.Q.2    Chiasson, J.L.3    Srivastava, A.K.4
  • 18
    • 0025217688 scopus 로고
    • Impaired insulin action but normal insulin receptor activity in diabetic rat liver: Efect of vanadate
    • Blondel, O., Simon, J., Chevalier, B., and Portha, B. (1990) Impaired insulin action but normal insulin receptor activity in diabetic rat liver: Efect of vanadate, Am. J. Physiol. 258, E459-E467.
    • (1990) Am. J. Physiol. , vol.258
    • Blondel, O.1    Simon, J.2    Chevalier, B.3    Portha, B.4
  • 19
    • 0025847598 scopus 로고
    • Antidiabetic action of vanadyl in rats independent of in vivo insulin-receptor kinase activity
    • Venkatesan, N., Avidan, A., and Davidson, M. B. (1991) Antidiabetic action of vanadyl in rats independent of in vivo insulin-receptor kinase activity, Diabetes 40, 492-498.
    • (1991) Diabetes , vol.40 , pp. 492-498
    • Venkatesan, N.1    Avidan, A.2    Davidson, M.B.3
  • 20
    • 0032571476 scopus 로고    scopus 로고
    • Vanadate fully stimulates insulin receptor substrate-1 associated phosphatidyl inositol 3-kinase activity in adipocytes from young and old rats
    • Molero, J. C., Martinez, C., Andres, A., Satrustegui, J., and Carrascosa, J. M. (1998) Vanadate fully stimulates insulin receptor substrate-1 associated phosphatidyl inositol 3-kinase activity in adipocytes from young and old rats, FEBS Lett. 425, 298-304.
    • (1998) FEBS Lett. , vol.425 , pp. 298-304
    • Molero, J.C.1    Martinez, C.2    Andres, A.3    Satrustegui, J.4    Carrascosa, J.M.5
  • 21
    • 0038521255 scopus 로고    scopus 로고
    • The efficacy of small interfering RNAs targeted to the type 1 insulin-like growth factor receptor (IGF1R) is influenced by secondary structure in the IGF1R transcript
    • Bohula, E. A., Salisbury, A. J., Sohail, M., Playford, M. P., Riedemann, J., Southern, E. M., and Macaulay, V. M. (2003) The efficacy of small interfering RNAs targeted to the type 1 insulin-like growth factor receptor (IGF1R) is influenced by secondary structure in the IGF1R transcript, J. Biol. Chem. 278, 15991-15997.
    • (2003) J. Biol. Chem. , vol.278 , pp. 15991-15997
    • Bohula, E.A.1    Salisbury, A.J.2    Sohail, M.3    Playford, M.P.4    Riedemann, J.5    Southern, E.M.6    Macaulay, V.M.7
  • 22
    • 0036772687 scopus 로고    scopus 로고
    • Rottlerin inhibits insulin-stimulated glucose transport in 3T3-L1 adipocytes by uncoupling mitochondrial oxidative phosphorylation
    • Kayali, A. G., Austin, D. A., and Webster, N. J. (2002) Rottlerin inhibits insulin-stimulated glucose transport in 3T3-L1 adipocytes by uncoupling mitochondrial oxidative phosphorylation, Endocrinology 143, 3884-3896.
    • (2002) Endocrinology , vol.143 , pp. 3884-3896
    • Kayali, A.G.1    Austin, D.A.2    Webster, N.J.3
  • 24
    • 0023240345 scopus 로고
    • Human insulin receptors mutated at the ATP-binding site lack protein tyrosine kinase activity and fail to mediate postreceptor effects of insulin
    • Chou, C. K., Dull, T. J., Russell, D. S., Gherzi, R., Lebwohl, D., Ullrich, A., and Rosen, O. M. (1987) Human insulin receptors mutated at the ATP-binding site lack protein tyrosine kinase activity and fail to mediate postreceptor effects of insulin, J. Biol. Chem. 262, 1842-1847.
    • (1987) J. Biol. Chem. , vol.262 , pp. 1842-1847
    • Chou, C.K.1    Dull, T.J.2    Russell, D.S.3    Gherzi, R.4    Lebwohl, D.5    Ullrich, A.6    Rosen, O.M.7
  • 25
    • 0038485698 scopus 로고    scopus 로고
    • Activation of epidermal growth factor receptor is responsible for pervanadate-induced phospholipase D activation
    • Kim, Y. R., Cha, H. Y., Lim, K., Hwang, B. D., Hoe, K. L., Namgung, U., and Park, S. K. (2003) Activation of epidermal growth factor receptor is responsible for pervanadate-induced phospholipase D activation, Exp. Mol. Med. 35, 118-124.
    • (2003) Exp. Mol. Med. , vol.35 , pp. 118-124
    • Kim, Y.R.1    Cha, H.Y.2    Lim, K.3    Hwang, B.D.4    Hoe, K.L.5    Namgung, U.6    Park, S.K.7
  • 26
    • 0034111152 scopus 로고    scopus 로고
    • Mechanism of extracellular signal-regulated kinase (ERK)-1 and ERK-2 activation by vanadium pentoxide in rat pulmonary myofibroblasts
    • Wang, Y. Z., and Bonner, J. C. (2000) Mechanism of extracellular signal-regulated kinase (ERK)-1 and ERK-2 activation by vanadium pentoxide in rat pulmonary myofibroblasts, Am. J. Respir. Cell Mol. Biol. 22, 590-596.
    • (2000) Am. J. Respir. Cell Mol. Biol. , vol.22 , pp. 590-596
    • Wang, Y.Z.1    Bonner, J.C.2
  • 27
    • 13244290055 scopus 로고    scopus 로고
    • Vascular smooth muscle cell NAD(P)H oxidase activity during the development of hypertension: Effect of angiotensin II and role of insulinlike growth factor-1 receptor transactivation
    • Cruzado, M. C., Risler, N. R., Miatello, R. M., Yao, G., Schiffrin, E. L., and Touyz, R. M. (2005) Vascular smooth muscle cell NAD(P)H oxidase activity during the development of hypertension: Effect of angiotensin II and role of insulinlike growth factor-1 receptor transactivation, Am. J. Hypertens. 18, 81-87.
    • (2005) Am. J. Hypertens. , vol.18 , pp. 81-87
    • Cruzado, M.C.1    Risler, N.R.2    Miatello, R.M.3    Yao, G.4    Schiffrin, E.L.5    Touyz, R.M.6
  • 28
    • 2542464026 scopus 로고    scopus 로고
    • Transactivation of the insulin-like growth factor-I receptor by angiotensin II mediates downstream signaling from the angiotensin II type 1 receptor to phosphatidylinositol 3-kinase
    • Zahradka, P., Litchie, B., Storie, B., and Helwer, G. (2004) Transactivation of the insulin-like growth factor-I receptor by angiotensin II mediates downstream signaling from the angiotensin II type 1 receptor to phosphatidylinositol 3-kinase, Endocrinology 145, 2978-2987.
    • (2004) Endocrinology , vol.145 , pp. 2978-2987
    • Zahradka, P.1    Litchie, B.2    Storie, B.3    Helwer, G.4
  • 29
    • 0030909657 scopus 로고    scopus 로고
    • Specific inhibition of insulin-like growth factor-1 and insulin receptor tyrosine kinase activity and biological function by tyrphostins
    • Parrizas, M., Gazit, A., Levitzki, A., Wertheimer, E., and LeRoith, D. (1997) Specific inhibition of insulin-like growth factor-1 and insulin receptor tyrosine kinase activity and biological function by tyrphostins, Endocrinology 138, 1427-1433.
    • (1997) Endocrinology , vol.138 , pp. 1427-1433
    • Parrizas, M.1    Gazit, A.2    Levitzki, A.3    Wertheimer, E.4    LeRoith, D.5
  • 30
    • 0028968949 scopus 로고
    • Tyrosine kinase inhibition: An approach to drug development
    • Levitzki, A., and Gazit, A. (1995) Tyrosine kinase inhibition: An approach to drug development, Science 267, 1782-1788.
    • (1995) Science , vol.267 , pp. 1782-1788
    • Levitzki, A.1    Gazit, A.2
  • 33
    • 0035823635 scopus 로고    scopus 로고
    • Cooperative regulation of the invasive and metastatic phenotypes by different domains of the type I insulin-like growth factor receptor β subunit
    • Brodt, P., Fallavollita, L., Khatib, A. M., Samani, A. A., and Zhang, D. (2001) Cooperative regulation of the invasive and metastatic phenotypes by different domains of the type I insulin-like growth factor receptor β subunit, J. Biol. Chem. 276, 33608-33615.
    • (2001) J. Biol. Chem. , vol.276 , pp. 33608-33615
    • Brodt, P.1    Fallavollita, L.2    Khatib, A.M.3    Samani, A.A.4    Zhang, D.5
  • 34
    • 19644379805 scopus 로고    scopus 로고
    • PKC-δ-dependent pathways contribute to PDGF-stimulated ERK1/2 activation in vascular smooth muscle
    • Ginnan, R., and Singer, H. A. (2005) PKC-δ-dependent pathways contribute to PDGF-stimulated ERK1/2 activation in vascular smooth muscle, Am. J. Physiol. 288, C1193-C1201.
    • (2005) Am. J. Physiol. , vol.288
    • Ginnan, R.1    Singer, H.A.2
  • 35
    • 2442426180 scopus 로고    scopus 로고
    • Epidermal growth factor induces fibroblast contractility and motility via a protein kinase C δ-dependent pathway
    • Iwabu, A., Smith, K., Allen, F. D., Lauffenburger, D. A., and Wells, A. (2004) Epidermal growth factor induces fibroblast contractility and motility via a protein kinase C δ-dependent pathway, J. Biol. Chem. 279, 14551-14560.
    • (2004) J. Biol. Chem. , vol.279 , pp. 14551-14560
    • Iwabu, A.1    Smith, K.2    Allen, F.D.3    Lauffenburger, D.A.4    Wells, A.5
  • 36
    • 0036153719 scopus 로고    scopus 로고
    • Calcium-independent activation of extracellularly regulated kinases 1 and 2 by angiotensin II in hepatic C9 cells: Roles of protein kinase Cδ, Src/proline-rich tyrosine kinase 2, and epidermal growth receptor trans-activation
    • Shah, B. H., and Catt, K. J. (2002) Calcium-independent activation of extracellularly regulated kinases 1 and 2 by angiotensin II in hepatic C9 cells: Roles of protein kinase Cδ, Src/proline-rich tyrosine kinase 2, and epidermal growth receptor trans-activation, Mol. Pharmacol. 61, 343-351.
    • (2002) Mol. Pharmacol. , vol.61 , pp. 343-351
    • Shah, B.H.1    Catt, K.J.2
  • 37
    • 0036411819 scopus 로고    scopus 로고
    • Vascular endothelial growth factor induces protein kinase C (PKC)-dependent Akt/PKB activation and phosphatidylinositol 3′-kinase- mediates PKCδ phosphorylation: Role of PKC in angiogenesis
    • Gliki, G., Wheeler-Jones, C., and Zachary, I. (2002) Vascular endothelial growth factor induces protein kinase C (PKC)-dependent Akt/PKB activation and phosphatidylinositol 3′-kinase-mediates PKCδ phosphorylation: Role of PKC in angiogenesis, Cell Biol. Int. 26, 751-759.
    • (2002) Cell Biol. Int. , vol.26 , pp. 751-759
    • Gliki, G.1    Wheeler-Jones, C.2    Zachary, I.3
  • 38
    • 8444241833 scopus 로고    scopus 로고
    • Activation and translocation of PKCδ is necessary for VEGF-induced ERK activation through KDR in HEK293T cells
    • Kuriyama, M., Taniguchi, T., Shirai, Y., Sasaki, A., Yoshimura, A., and Saito, N. (2004) Activation and translocation of PKCδ is necessary for VEGF-induced ERK activation through KDR in HEK293T cells, Biochem. Biophys. Res. Commun. 325, 843-851.
    • (2004) Biochem. Biophys. Res. Commun. , vol.325 , pp. 843-851
    • Kuriyama, M.1    Taniguchi, T.2    Shirai, Y.3    Sasaki, A.4    Yoshimura, A.5    Saito, N.6
  • 40
    • 1542619260 scopus 로고    scopus 로고
    • 2-induced activation of ERK1/2, p38 MAPK, and protein kinase B signaling in vascular smooth muscle cells
    • 2-induced activation of ERK1/2, p38 MAPK, and protein kinase B signaling in vascular smooth muscle cells, Antioxid. Redox Signaling 6, 353-366.
    • (2004) Antioxid. Redox Signaling , vol.6 , pp. 353-366
    • Blanc, A.1    Pandey, N.R.2    Srivastava, A.K.3
  • 41
    • 10944238407 scopus 로고    scopus 로고
    • Distinctive activation mechanisms and functions for protein kinase Cδ
    • Steinberg, S. F. (2004) Distinctive activation mechanisms and functions for protein kinase Cδ, Biochem. J. 384, 449-459.
    • (2004) Biochem. J. , vol.384 , pp. 449-459
    • Steinberg, S.F.1
  • 42
    • 0035851112 scopus 로고    scopus 로고
    • Rottlerin is a mitochondrial uncoupler that decreases cellular ATP levels and indirectly blocks protein kinase Cδ tyrosine phosphorylation
    • Soltoff, S. P. (2001) Rottlerin is a mitochondrial uncoupler that decreases cellular ATP levels and indirectly blocks protein kinase Cδ tyrosine phosphorylation, J. Biol. Chem. 276, 37986-37992.
    • (2001) J. Biol. Chem. , vol.276 , pp. 37986-37992
    • Soltoff, S.P.1
  • 43
    • 0034989803 scopus 로고    scopus 로고
    • Modulation of PKCδ tyrosine phosphorylation and activity in salivary and PC-12 cells by Src kinases
    • Benes, C., and Soltoff, S. P. (2001) Modulation of PKCδ tyrosine phosphorylation and activity in salivary and PC-12 cells by Src kinases, Am. J. Physiol. 280, C1498-C1510.
    • (2001) Am. J. Physiol. , vol.280
    • Benes, C.1    Soltoff, S.P.2
  • 44
    • 2442498430 scopus 로고    scopus 로고
    • Stimulus-specific differences in protein kinase Cδ localization and activation mechanisms in cardiomyocytes
    • Rybin, V. O., Guo, J., Sabri, A., Elouardighi, H., Schaefer, E., and Steinberg, S. F. (2004) Stimulus-specific differences in protein kinase Cδ localization and activation mechanisms in cardiomyocytes, J. Biol. Chem. 279, 19350-19361.
    • (2004) J. Biol. Chem. , vol.279 , pp. 19350-19361
    • Rybin, V.O.1    Guo, J.2    Sabri, A.3    Elouardighi, H.4    Schaefer, E.5    Steinberg, S.F.6
  • 45
    • 0031684848 scopus 로고    scopus 로고
    • Protein kinase C-δ is an important signaling molecule in insulin-like growth factor I receptor-mediated cell transformation
    • Li, W., Jiang, Y. X., Zhang, J., Soon, L., Flechner, L., Kapoor, V., Pierce, J. H., and Wang, L. H. (1998) Protein kinase C-δ is an important signaling molecule in insulin-like growth factor I receptor-mediated cell transformation, Mol. Cell. Biol. 18, 5888-5898.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 5888-5898
    • Li, W.1    Jiang, Y.X.2    Zhang, J.3    Soon, L.4    Flechner, L.5    Kapoor, V.6    Pierce, J.H.7    Wang, L.H.8
  • 47
    • 0036305564 scopus 로고    scopus 로고
    • Vanadium increases GLUT4 in diabetic rat skeletal muscle
    • Mohammad, A., Sharma, V., and McNeill, J. H. (2002) Vanadium increases GLUT4 in diabetic rat skeletal muscle, Mol. Cell. Biochem. 233, 139-143.
    • (2002) Mol. Cell. Biochem. , vol.233 , pp. 139-143
    • Mohammad, A.1    Sharma, V.2    McNeill, J.H.3
  • 48
    • 0037306526 scopus 로고    scopus 로고
    • Redox-dependent MAP kinase signaling by Ang II in vascular smooth muscle cells: Role of receptor tyrosine kinase transactivation
    • Touyz, R. M., Cruzado, M., Tabet, F., Yao, G., Salomon, S., and Schiffrin, E. L. (2003) Redox-dependent MAP kinase signaling by Ang II in vascular smooth muscle cells: Role of receptor tyrosine kinase transactivation, Can. J. Physiol. Pharmacol. 81, 159-167.
    • (2003) Can. J. Physiol. Pharmacol. , vol.81 , pp. 159-167
    • Touyz, R.M.1    Cruzado, M.2    Tabet, F.3    Yao, G.4    Salomon, S.5    Schiffrin, E.L.6
  • 49
    • 29244467700 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase activation by hydrogen peroxide is mediated through tyrosine kinase-dependent, protein kinase C-independent pathways in vascular smooth muscle cells: Upregulation in spontaneously hypertensive rats
    • Tabet, F., Schiffrin, E. L., and Touyz, R. M. (2005) Mitogen-activated protein kinase activation by hydrogen peroxide is mediated through tyrosine kinase-dependent, protein kinase C-independent pathways in vascular smooth muscle cells: Upregulation in spontaneously hypertensive rats, J. Hypertens. 23, 2005-2012.
    • (2005) J. Hypertens. , vol.23 , pp. 2005-2012
    • Tabet, F.1    Schiffrin, E.L.2    Touyz, R.M.3
  • 50
    • 33646344489 scopus 로고    scopus 로고
    • P2Y(12) receptor signalling towards PKB proceeds through IGF-I receptor cross-talk and requires activation of Src, Pyk2 and Rap1
    • Van Kolen, K., Gilany, K., Moens, L., Esmans, E. L., and Slegers, H. (2005) P2Y(12) receptor signalling towards PKB proceeds through IGF-I receptor cross-talk and requires activation of Src, Pyk2 and Rap1, Cell Signaling 18, 1169-1181.
    • (2005) Cell Signaling , vol.18 , pp. 1169-1181
    • Van Kolen, K.1    Gilany, K.2    Moens, L.3    Esmans, E.L.4    Slegers, H.5
  • 51
    • 0037409235 scopus 로고    scopus 로고
    • Angiotensin II signaling pathways mediated by tyrosine kinases
    • Yin, G., Yan, C., and Berk, B. C. (2003) Angiotensin II signaling pathways mediated by tyrosine kinases, Int. J. Biochem. Cell Biol. 35, 780-783.
    • (2003) Int. J. Biochem. Cell Biol. , vol.35 , pp. 780-783
    • Yin, G.1    Yan, C.2    Berk, B.C.3
  • 52
    • 0030207118 scopus 로고    scopus 로고
    • Signaling via the insulin-like growth factor-I receptor: Does it differ from insulin receptor signaling?
    • Blakesley, V. A., Scrimgeour, A., Esposito, D., and Le Roith, D. (1996) Signaling via the insulin-like growth factor-I receptor: Does it differ from insulin receptor signaling? Cytokine Growth Factor Rev. 7, 153-159.
    • (1996) Cytokine Growth Factor Rev. , vol.7 , pp. 153-159
    • Blakesley, V.A.1    Scrimgeour, A.2    Esposito, D.3    Le Roith, D.4
  • 53
    • 30744470893 scopus 로고    scopus 로고
    • Insulin Signal Mimicry as a Mechanism for the Insulin-Like Effects of Vanadium
    • Mehdi, M. Z., Pandey, S. K., Theberge, J. F., and Srivastava, A. K. (2006) Insulin Signal Mimicry as a Mechanism for the Insulin-Like Effects of Vanadium, Cell Biochem. Biophys. 44, 73-81.
    • (2006) Cell Biochem. Biophys. , vol.44 , pp. 73-81
    • Mehdi, M.Z.1    Pandey, S.K.2    Theberge, J.F.3    Srivastava, A.K.4
  • 54
    • 0029586674 scopus 로고
    • In vivo effects of vanadate on hepatic glycogen metabolizing and lipogenic enzymes in insulin-dependent and insulin-resistant diabetic animals
    • Khandelwal, R. L., and Pugazhenthi, S. (1995) In vivo effects of vanadate on hepatic glycogen metabolizing and lipogenic enzymes in insulin-dependent and insulin-resistant diabetic animals, Mol. Cell. Biochem. 153, 87-94.
    • (1995) Mol. Cell. Biochem. , vol.153 , pp. 87-94
    • Khandelwal, R.L.1    Pugazhenthi, S.2
  • 56
    • 6344282286 scopus 로고    scopus 로고
    • Role of protein kinase Cδ in endothelin-induced type I collagen expression in cardiac myofibroblasts isolated from the site of myocardial infarction
    • Chintalgattu, V., and Katwa, L. C. (2004) Role of protein kinase Cδ in endothelin-induced type I collagen expression in cardiac myofibroblasts isolated from the site of myocardial infarction, J. Pharmacol. Exp. Ther. 311, 691-699.
    • (2004) J. Pharmacol. Exp. Ther. , vol.311 , pp. 691-699
    • Chintalgattu, V.1    Katwa, L.C.2
  • 58
    • 0033305091 scopus 로고    scopus 로고
    • Dependence of insulin-stimulated glucose transporter 4 translocation on 3-phosphoinositide-dependent protein kinase-1 and its target threonine-410 in the activation loop of protein kinase C-ζ
    • Bandyopadhyay, G., Standaert, M. L., Sajan, M. P., Karnitz, L. M., Cong, L., Quon, M. J., and Farese, R. V. (1999) Dependence of insulin-stimulated glucose transporter 4 translocation on 3-phosphoinositide-dependent protein kinase-1 and its target threonine-410 in the activation loop of protein kinase C-ζ, Mol. Endocrinol. 13, 1766-1772.
    • (1999) Mol. Endocrinol. , vol.13 , pp. 1766-1772
    • Bandyopadhyay, G.1    Standaert, M.L.2    Sajan, M.P.3    Karnitz, L.M.4    Cong, L.5    Quon, M.J.6    Farese, R.V.7
  • 59
    • 0033233463 scopus 로고    scopus 로고
    • Protein kinase Cδ mediates insulin-induced glucose transport in primary cultures of rat skeletal muscle
    • Braiman, L., Alt, A., Kuroki, T., Ohba, M., Bak, A., Tennenbaum, T., and Sampson, S. R. (1999) Protein kinase Cδ mediates insulin-induced glucose transport in primary cultures of rat skeletal muscle, Mol. Endocrinol. 13, 2002-2012.
    • (1999) Mol. Endocrinol. , vol.13 , pp. 2002-2012
    • Braiman, L.1    Alt, A.2    Kuroki, T.3    Ohba, M.4    Bak, A.5    Tennenbaum, T.6    Sampson, S.R.7
  • 60
    • 85047681823 scopus 로고    scopus 로고
    • Protein kinase Cθ expression is increased upon differentiation of human skeletal muscle cells: Dysregulation in type 2 diabetic patients and a possible role for protein kinase Cθ in insulin-stimulated glycogen synthase activity
    • Chalfant, C. E., Ciaraldi, T. P., Watson, J. E., Nikoulina, S., Henry, R. R., and Cooper, D. R. (2000) Protein kinase Cθ expression is increased upon differentiation of human skeletal muscle cells: Dysregulation in type 2 diabetic patients and a possible role for protein kinase Cθ in insulin-stimulated glycogen synthase activity, Endocrinology 141, 2773-2778.
    • (2000) Endocrinology , vol.141 , pp. 2773-2778
    • Chalfant, C.E.1    Ciaraldi, T.P.2    Watson, J.E.3    Nikoulina, S.4    Henry, R.R.5    Cooper, D.R.6
  • 61
    • 0034746437 scopus 로고    scopus 로고
    • PKCδ activation: A divergence point in the signaling of insulin and IGF-1-induced proliferation of skin keratinocytes
    • Shen, S., Alt, A., Wertheimer, E., Gartsbein, M., Kuroki, T., Ohba, M., Braiman, L., Sampson, S. R., and Tennenbaum, T. (2001) PKCδ activation: A divergence point in the signaling of insulin and IGF-1-induced proliferation of skin keratinocytes, Diabetes 50, 255-264.
    • (2001) Diabetes , vol.50 , pp. 255-264
    • Shen, S.1    Alt, A.2    Wertheimer, E.3    Gartsbein, M.4    Kuroki, T.5    Ohba, M.6    Braiman, L.7    Sampson, S.R.8    Tennenbaum, T.9
  • 62
    • 0033215244 scopus 로고    scopus 로고
    • In L6 skeletal muscle cells, glucose induces cytosolic translocation of protein kinase C-α and trans-activates the insulin receptor kinase
    • Caruso, M., Miele, C., Oriente, F., Maitan, A., Bifulco, G., Andreozzi, F., Condorelli, G., Formisano, P., and Beguinot, F. (1999) In L6 skeletal muscle cells, glucose induces cytosolic translocation of protein kinase C-α and trans-activates the insulin receptor kinase, J. Biol. Chem. 274, 28637-28644.
    • (1999) J. Biol. Chem. , vol.274 , pp. 28637-28644
    • Caruso, M.1    Miele, C.2    Oriente, F.3    Maitan, A.4    Bifulco, G.5    Andreozzi, F.6    Condorelli, G.7    Formisano, P.8    Beguinot, F.9
  • 63
    • 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
  • 64
    • 0034306450 scopus 로고    scopus 로고
    • Specificity and mechanism of action of some commonly used protein kinase inhibitors
    • Davies, S. P., Reddy, H., Caivano, M., and Cohen, P. (2000) Specificity and mechanism of action of some commonly used protein kinase inhibitors, Biochem. J. 351, 95-105.
    • (2000) Biochem. J. , vol.351 , pp. 95-105
    • Davies, S.P.1    Reddy, H.2    Caivano, M.3    Cohen, P.4
  • 65
    • 0032474741 scopus 로고    scopus 로고
    • Tyrosine phosphorylation-dependent and -independent associations of protein kinase C-δ with Src family kinases in the RBL-2H3 mast cell line: Regulation of Src family kinase activity by protein kinase C-δ
    • Song, J. S., Swann, P. G., Szallasi, Z., Blank, U., Blumberg, P. M., and Rivera, J. (1998) Tyrosine phosphorylation-dependent and -independent associations of protein kinase C-δ with Src family kinases in the RBL-2H3 mast cell line: Regulation of Src family kinase activity by protein kinase C-δ, Oncogene 16, 3357-3368.
    • (1998) Oncogene , vol.16 , pp. 3357-3368
    • Song, J.S.1    Swann, P.G.2    Szallasi, Z.3    Blank, U.4    Blumberg, P.M.5    Rivera, J.6
  • 66
    • 0033547434 scopus 로고    scopus 로고
    • Protein kinase C-α overexpression stimulates Akt activity and suppresses apoptosis induced by interleukin 3 withdrawal
    • Li, W., Zhang, J., Flechner, L., Hyun, T., Yam, A., Franke, T. F., and Pierce, J. H. (1999) Protein kinase C-α overexpression stimulates Akt activity and suppresses apoptosis induced by interleukin 3 withdrawal, Oncogene 18, 6564-6572.
    • (1999) Oncogene , vol.18 , pp. 6564-6572
    • Li, W.1    Zhang, J.2    Flechner, L.3    Hyun, T.4    Yam, A.5    Franke, T.F.6    Pierce, J.H.7
  • 67
    • 0034533061 scopus 로고    scopus 로고
    • Inhibition of growth-factor-induced phosphorylation and activation of protein kinase B/Akt by atypical protein kinase C in breast cancer cells
    • Mao, M., Fang, X., Lu, Y., LaPushin, R., Bast, R. C., Jr., and Mills, G. B. (2000) Inhibition of growth-factor-induced phosphorylation and activation of protein kinase B/Akt by atypical protein kinase C in breast cancer cells, Biochem. J. 352 (Part 2), 475-482.
    • (2000) Biochem. J. , vol.352 , Issue.PART 2 , pp. 475-482
    • Mao, M.1    Fang, X.2    Lu, Y.3    Lapushin, R.4    Bast Jr., R.C.5    Mills, G.B.6
  • 68
    • 0037209633 scopus 로고    scopus 로고
    • Negative regulation of phosphatidylinositol 3-kinase and Akt signalling pathway by PKC
    • Wen, H. C., Huang, W. C., Ali, A., Woodgett, J. R., and Lin, W. W. (2003) Negative regulation of phosphatidylinositol 3-kinase and Akt signalling pathway by PKC, Cell. Signalling 15, 37-45.
    • (2003) Cell. Signalling , vol.15 , pp. 37-45
    • Wen, H.C.1    Huang, W.C.2    Ali, A.3    Woodgett, J.R.4    Lin, W.W.5
  • 69
    • 0028082161 scopus 로고
    • Protein kinase C: A question of specificity
    • Dekker, L. V., and Parker, P. J. (1994) Protein kinase C: A question of specificity, Trends Biochem. Sci. 19, 73-77.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 73-77
    • Dekker, L.V.1    Parker, P.J.2
  • 70
    • 0032924312 scopus 로고    scopus 로고
    • Protein kinases C-γ and -δ are involved in insulin-like growth factor I-induced migration of colonic epithelial cells
    • Andre, F., Rigot, V., Remacle-Bonnet, M., Luis, J., Pommier, G., and Marvaldi, J. (1999) Protein kinases C-γ and -δ are involved in insulin-like growth factor I-induced migration of colonic epithelial cells, Gastroenterologe 116, 64-77.
    • (1999) Gastroenterologe , vol.116 , pp. 64-77
    • Andre, F.1    Rigot, V.2    Remacle-Bonnet, M.3    Luis, J.4    Pommier, G.5    Marvaldi, J.6
  • 71
    • 0033304873 scopus 로고    scopus 로고
    • Down-regulation of protein kinase C inhibits insulin-like growth factor I-induced vascular smooth muscle cell proliferation, migration, and gene expression
    • Yano, K., Bauchat, J. R., Liimatta, M. B., Clemmons, D. R., and Duan, C. (1999) Down-regulation of protein kinase C inhibits insulin-like growth factor I-induced vascular smooth muscle cell proliferation, migration, and gene expression, Endocrinology 140, 4622-4632.
    • (1999) Endocrinology , vol.140 , pp. 4622-4632
    • Yano, K.1    Bauchat, J.R.2    Liimatta, M.B.3    Clemmons, D.R.4    Duan, C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.