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Volumn 28, Issue 2, 2003, Pages 123-138

Light Regulation of the Insulin Receptor in the Retina

Author keywords

Insulin receptor; Phosphatidylinositol 3,4,5 trisphosphate; Phosphatidylinositol 4,5 bisphosphate; Phosphoinositide 3 kinase; Phototransduction; Platelet derived growth factor; Rod outer segments; ROS

Indexed keywords

ANTIBODY; CALCIUM CHANNEL L TYPE; INSULIN; INSULIN RECEPTOR; INSULIN RECEPTOR BETA; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHOTYROSINE; PROTEIN P85; REACTIVE OXYGEN METABOLITE; RECEPTOR SUBUNIT; UNCLASSIFIED DRUG;

EID: 0742321912     PISSN: 08937648     EISSN: None     Source Type: Journal    
DOI: 10.1385/MN:28:2:123     Document Type: Conference Paper
Times cited : (15)

References (83)
  • 2
    • 0033605152 scopus 로고    scopus 로고
    • Structural features of the ligand-binding domain of the serotonin 5HT3 receptor
    • Yan D., Schulte M.K., Bloom K.E.et al (1999) Structural features of the ligand-binding domain of the serotonin 5HT3 receptor. J. Biol. Chem. 274, 5537-5541.
    • (1999) J. Biol. Chem. , vol.274 , pp. 5537-5541
    • Yan, D.1    Schulte, M.K.2    Bloom, K.E.3
  • 3
    • 0033028510 scopus 로고    scopus 로고
    • Signal perception and transduction: The role of protein kinases
    • Schenk P.W. and Snaar-Jagalska B.E. (1999) Signal perception and transduction: the role of protein kinases. Biochim. Biophys. Acta 1449, 1-24.
    • (1999) Biochim. Biophys. Acta , vol.1449 , pp. 1-24
    • Schenk, P.W.1    Snaar-Jagalska, B.E.2
  • 4
    • 0032541677 scopus 로고    scopus 로고
    • Tyrosine kinase receptor-activated signal transduction pathways which lead to oncogenesis
    • Porter A.C. and Vaillancourt R.R. (1998) Tyrosine kinase receptor-activated signal transduction pathways which lead to oncogenesis. Oncogene 17, 1343-1352.
    • (1998) Oncogene , vol.17 , pp. 1343-1352
    • Porter, A.C.1    Vaillancourt, R.R.2
  • 5
    • 0032430523 scopus 로고    scopus 로고
    • Signal transduction through cytokine receptors
    • Hibi M. and Hirano T. (1998) Signal transduction through cytokine receptors. Int. Rev. Immunol. 17, 75-102.
    • (1998) Int. Rev. Immunol. , vol.17 , pp. 75-102
    • Hibi, M.1    Hirano, T.2
  • 6
    • 0032077196 scopus 로고    scopus 로고
    • G protein-coupled receptor signalling in the kidney
    • Weiss R.H. (1998) G protein-coupled receptor signalling in the kidney. Cell Signalling 10, 313-320.
    • (1998) Cell Signalling , vol.10 , pp. 313-320
    • Weiss, R.H.1
  • 7
    • 0030812439 scopus 로고    scopus 로고
    • Signaling mechanisms in growth factor-stimulated cell motility
    • Anand-Apte B. and Zetter B. (1997) Signaling mechanisms in growth factor-stimulated cell motility. Stem Cells 15, 259-267.
    • (1997) Stem Cells , vol.15 , pp. 259-267
    • Anand-Apte, B.1    Zetter, B.2
  • 8
    • 0031846992 scopus 로고    scopus 로고
    • Insulin-dependent protein trafficking in skeletal muscle cells
    • Zhou M., Sevilla L., Vallega G., et al. (1998) Insulin-dependent protein trafficking in skeletal muscle cells. Am. J. Physiol 275, E187-E196.
    • (1998) Am. J. Physiol , vol.275
    • Zhou, M.1    Sevilla, L.2    Vallega, G.3
  • 9
    • 0030862919 scopus 로고    scopus 로고
    • Responsiveness of human neutrophils to interleukin-4: Induction of cytoskeletal rearrangements, de novo protein synthesis and delay of apoptosis
    • Girard D., Paquin R., and Beaulieu A.D. (1997) Responsiveness of human neutrophils to interleukin-4: induction of cytoskeletal rearrangements, de novo protein synthesis and delay of apoptosis. Biochem. J. 325(Pt 1), 147-153.
    • (1997) Biochem. J. , vol.325 , Issue.1 PART , pp. 147-153
    • Girard, D.1    Paquin, R.2    Beaulieu, A.D.3
  • 10
    • 1842367312 scopus 로고    scopus 로고
    • Kinetics and extent of T cell activation as measured with the calcium signal
    • Wulfing C., Rabinowitz J.D., Beeson C., et al. (1997) Kinetics and extent of T cell activation as measured with the calcium signal. J. Exp. Med. 185, 1815-1825.
    • (1997) J. Exp. Med. , vol.185 , pp. 1815-1825
    • Wulfing, C.1    Rabinowitz, J.D.2    Beeson, C.3
  • 11
    • 0032437256 scopus 로고    scopus 로고
    • Signal transduction pathways that regulate cell survival and cell death
    • Dragovich T., Rudin C.M., and Thompson C.B. (1998) Signal transduction pathways that regulate cell survival and cell death. Oncogene 17, 3207-3213.
    • (1998) Oncogene , vol.17 , pp. 3207-3213
    • Dragovich, T.1    Rudin, C.M.2    Thompson, C.B.3
  • 12
    • 0028084335 scopus 로고
    • Receptor tyrosine kinases and their targets
    • Kazlauskas A. (1994) Receptor tyrosine kinases and their targets. Curr. Opin. Genet. Dev. 4, 5-14.
    • (1994) Curr. Opin. Genet. Dev. , vol.4 , pp. 5-14
    • Kazlauskas, A.1
  • 13
    • 0030749294 scopus 로고    scopus 로고
    • Serine/threonine kinase receptors and ligands
    • Josso N., di Clemente N. (1997) Serine/threonine kinase receptors and ligands. Curr. Opin. Genet. Dev. 7, 371-377.
    • (1997) Curr. Opin. Genet. Dev. , vol.7 , pp. 371-377
    • Josso, N.1    Di Clemente, N.2
  • 14
    • 0028085078 scopus 로고
    • The insulin signaling system
    • White M.F. and Kahn C.R. (1994) The insulin signaling system. J. Biol. Chem. 269, 1-4.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1-4
    • White, M.F.1    Kahn, C.R.2
  • 18
    • 0028012445 scopus 로고
    • Direct activation of the phosphatidylinositol 3′-kinase by the insulin receptor
    • Van Horn D.J., Myers M.G., Jr., and Backer J.M. (1994) Direct activation of the phosphatidylinositol 3′-kinase by the insulin receptor. J. Biol. Chem. 269, 29-32.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29-32
    • Van Horn, D.J.1    Myers Jr., M.G.2    Backer, J.M.3
  • 19
    • 0026660653 scopus 로고
    • Phosphatidylinositol 3′-kinase is activated by association with IRS-1 during insulin stimulation
    • Backer J.M., Myers M.G., Jr., Shoelson S.E., et al. (1992) Phosphatidylinositol 3′-kinase is activated by association with IRS-1 during insulin stimulation. EMBO J. 11, 3469-3479.
    • (1992) EMBO J. , vol.11 , pp. 3469-3479
    • Backer, J.M.1    Myers Jr., M.G.2    Shoelson, S.E.3
  • 20
    • 0027158159 scopus 로고
    • The insulin receptor substrate 1 associates with the SH2-containing phosphotyrosine phosphatase Syp
    • Kuhne M.R., Pawson T., Lienhard G.E., et al. (1993) The insulin receptor substrate 1 associates with the SH2-containing phosphotyrosine phosphatase Syp. J. Biol. Chem. 268, 11,479-11,481.
    • (1993) J. Biol. Chem. , vol.268 , pp. 11479-11481
    • Kuhne, M.R.1    Pawson, T.2    Lienhard, G.E.3
  • 21
    • 0027182367 scopus 로고
    • The function of GRB2 in linking the insulin receptor to Ras signaling pathways
    • Skolnik E.Y., Batzer A., Li N., et al. (1993) The function of GRB2 in linking the insulin receptor to Ras signaling pathways. Science 260, 1953-1955.
    • (1993) Science , vol.260 , pp. 1953-1955
    • Skolnik, E.Y.1    Batzer, A.2    Li, N.3
  • 22
    • 0027143218 scopus 로고
    • Nek associates with the SH2 domain-docking protein IRS-1 in insulin-stimulated cells
    • Lee C.H., Li W., Nishimura R., et al. (1993) Nek associates with the SH2 domain-docking protein IRS-1 in insulin-stimulated cells. Proc. Natl. Acad. Sci. USA 90, 11,713-11,717.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 11713-11717
    • Lee, C.H.1    Li, W.2    Nishimura, R.3
  • 23
    • 0025062397 scopus 로고
    • Human insulin-receptor gene
    • Seino S., Seino M., and Bell G.I. (1990) Human insulin-receptor gene. Diabetes 39, 129-133.
    • (1990) Diabetes , vol.39 , pp. 129-133
    • Seino, S.1    Seino, M.2    Bell, G.I.3
  • 24
    • 0023555715 scopus 로고
    • Retinal insulin receptors. 1. Structural heterogeneity and functional characterization
    • Waldbillig R.J., Fletcher R.T., Chader G.J. et al (1987) Retinal insulin receptors. 1. Structural heterogeneity and functional characterization. Exp. Eye Res. 45, 823-835.
    • (1987) Exp. Eye Res. , vol.45 , pp. 823-835
    • Waldbillig, R.J.1    Fletcher, R.T.2    Chader, G.J.3
  • 25
    • 0023580292 scopus 로고
    • Retinal insulin receptors. 2. Characterization and insulin-induced tyrosine kinase activity in bovine retinal rod outer segments
    • Waldbillig R.J., Fletcher R.T., Chader G.J., et al. (1987) Retinal insulin receptors. 2. Characterization and insulin-induced tyrosine kinase activity in bovine retinal rod outer segments. Exp. Eye Res. 45, 837-844.
    • (1987) Exp. Eye Res. , vol.45 , pp. 837-844
    • Waldbillig, R.J.1    Fletcher, R.T.2    Chader, G.J.3
  • 26
    • 0025163076 scopus 로고
    • Identification of retinal insulin receptors -using site-specific antibodies to a carboxyl-terminal peptide of the human insulin receptor alpha-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 alpha-subunit. Up-regulation of neuronal insulin receptors in diabetes. J. Biol. Chem. 265, 18,030-18,034.
    • (1990) J. Biol. Chem. , vol.265 , pp. 18030-18034
    • Rosenzweig, S.A.1    Zetterstrom, C.2    Benjamin, A.3
  • 27
    • 0025951277 scopus 로고
    • Characterization of a novel receptor in toad retina with dual specificity for insulin and insulin-like growth factor I
    • Zetterstrom C., Fang C., Benjamin A., et al. (1991) Characterization of a novel receptor in toad retina with dual specificity for insulin and insulin-like growth factor I. J. Neurochem. 57, 1332-1339.
    • (1991) J. Neurochem. , vol.57 , pp. 1332-1339
    • Zetterstrom, C.1    Fang, C.2    Benjamin, A.3
  • 28
    • 0028971216 scopus 로고
    • Autocrine/paracrine role of insulin-related growth factors in neurogenesis: Local expression and effects on cell proliferation and differentiation in retina
    • Hernandez-Sanchez C., Lopez-Carranza A., Alarcon C., et al. (1995) Autocrine/paracrine role of insulin-related growth factors in neurogenesis: local expression and effects on cell proliferation and differentiation in retina. Proc. Natl. Acad. Sci. USA 92, 9834-9838.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9834-9838
    • Hernandez-Sanchez, C.1    Lopez-Carranza, A.2    Alarcon, C.3
  • 29
    • 0028863148 scopus 로고
    • The role of the tyrosine kinase domain of the insulin-like growth factor-I receptor in intracellular signaling cellular proliferation, and tumorigenesis
    • Hernandez-Sanchez C., Blakesley V., Kalebic T., et al. (1995) The role of the tyrosine kinase domain of the insulin-like growth factor-I receptor in intracellular signaling cellular proliferation, and tumorigenesis. J. Biol. Chem. 270, 29,176-29,181.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29176-29181
    • Hernandez-Sanchez, C.1    Blakesley, V.2    Kalebic, T.3
  • 31
    • 0023871849 scopus 로고
    • Retinal insulin receptors: Localization using a polyclonal anti-insulin receptor antibody
    • Rodrigues M., Waldbillig R.J., Rajagopalan S., et al. (1988) Retinal insulin receptors: localization using a polyclonal anti-insulin receptor antibody. Brain Res. 443, 389-394.
    • (1988) Brain Res. , vol.443 , pp. 389-394
    • Rodrigues, M.1    Waldbillig, R.J.2    Rajagopalan, S.3
  • 32
    • 0035901754 scopus 로고    scopus 로고
    • Insulin inhibits voltage-dependent calcium influx into rod photoreceptors
    • Stella S.L., Jr., Bryson E.J., and Thoreson W.B. (2001) Insulin inhibits voltage-dependent calcium influx into rod photoreceptors. Neuroreport 12, 947-951.
    • (2001) Neuroreport , vol.12 , pp. 947-951
    • Stella Jr., S.L.1    Bryson, E.J.2    Thoreson, W.B.3
  • 33
    • 0032881941 scopus 로고    scopus 로고
    • Retinitis pigmentosa: Rod photoreceptor rescue by a calcium-channel blocker in the rd mouse
    • Frasson M., Sahel J.A., Fabre M., et al. (1999) Retinitis pigmentosa: rod photoreceptor rescue by a calcium-channel blocker in the rd mouse. Nat. Med. 5, 1183-1187.
    • (1999) Nat. Med. , vol.5 , pp. 1183-1187
    • Frasson, M.1    Sahel, J.A.2    Fabre, M.3
  • 34
    • 0035980149 scopus 로고    scopus 로고
    • Insulin rescues retinal neurons from apoptosis by a phosphatidylinositol 3-kinase/Akt-mediated mechanism that reduces the activation of caspase-3
    • Barber A.J., Nakamura M., Wolpert E.B., et al. (2001) Insulin rescues retinal neurons from apoptosis by a phosphatidylinositol 3-kinase/Akt-mediated mechanism that reduces the activation of caspase-3. J. Biol. Chem. 276, 32,814-32,821.
    • (2001) J. Biol. Chem. , vol.276 , pp. 32814-32821
    • Barber, A.J.1    Nakamura, M.2    Wolpert, E.B.3
  • 35
    • 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
  • 36
    • 0026793456 scopus 로고
    • Growth factor signaling by receptor tyrosine kinases
    • Schlessinger J., Ullrich A. (1992) Growth factor signaling by receptor tyrosine kinases. Neuron 9, 383-391.
    • (1992) Neuron , vol.9 , pp. 383-391
    • Schlessinger, J.1    Ullrich, A.2
  • 37
    • 0031662594 scopus 로고    scopus 로고
    • Light stimulates tyrosine phosphorylation of rat rod outer segments in vivo
    • Ghalayini A.J., Guo X.X., Koutz C.A., et al. (1998) Light stimulates tyrosine phosphorylation of rat rod outer segments In vivo. Exp. Eye Res. 66, 817-821.
    • (1998) Exp. Eye Res. , vol.66 , pp. 817-821
    • Ghalayini, A.J.1    Guo, X.X.2    Koutz, C.A.3
  • 38
    • 0032733976 scopus 로고    scopus 로고
    • Association of the tyrosine phosphatase SHP-2 with transducin-alpha and a 97-kDa tyrosine-phosphorylated protein in photoreceptor rod outer segments
    • Bell M.W., Alvarez K., and Ghalayini A.J. (1999) Association of the tyrosine phosphatase SHP-2 with transducin-alpha and a 97-kDa tyrosine-phosphorylated protein in photoreceptor rod outer segments. J. Neurochem. 73, 2331-2340.
    • (1999) J. Neurochem. , vol.73 , pp. 2331-2340
    • Bell, M.W.1    Alvarez, K.2    Ghalayini, A.J.3
  • 39
    • 0033790127 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of the alpha subunit of transducin and its association with Src in photoreceptor rod outer segments
    • Bell M.W., Desai N., Guo X.X., et al. (2000) Tyrosine phosphorylation of the alpha subunit of transducin and its association with Src in photoreceptor rod outer segments. J. Neurochem. 75, 2006-2019.
    • (2000) J. Neurochem. , vol.75 , pp. 2006-2019
    • Bell, M.W.1    Desai, N.2    Guo, X.X.3
  • 40
    • 0035656204 scopus 로고    scopus 로고
    • Interaction of the insulin receptor beta-subunit with phosphatidylinositol 3-kinase in bovine ROS
    • Rajala R.V. and Anderson R.E. (2001) Interaction of the insulin receptor beta-subunit with phosphatidylinositol 3-kinase in bovine ROS. Investig. Ophthalmol. Vis. Sci. 42, 3110-3117.
    • (2001) Investig. Ophthalmol. Vis. Sci. , vol.42 , pp. 3110-3117
    • Rajala, R.V.1    Anderson, R.E.2
  • 41
    • 0037044798 scopus 로고    scopus 로고
    • In vivo regulation of phosphoinositide 3-kinase in retina through light-induced tyrosine phosphorylation of the insulin receptor beta-subunit
    • Rajala R.V., McClellan M.E., Ash J.D., et al. (2002) In vivo regulation of phosphoinositide 3-kinase in retina through light-induced tyrosine phosphorylation of the insulin receptor beta-subunit. J. Biol. Chem. 277, 43,319-13,326.
    • (2002) J. Biol. Chem. , vol.277 , pp. 43319-113326
    • Rajala, R.V.1    McClellan, M.E.2    Ash, J.D.3
  • 42
    • 0025201426 scopus 로고
    • Purification and characterization of phosphoinositide 3-kinase from rat liver
    • Carpenter C.L., Duckworth B.C., Auger K.R., et al. (1990) Purification and characterization of phosphoinositide 3-kinase from rat liver. J. Biol. Chem. 265, 19,704-19,711.
    • (1990) J. Biol. Chem. , vol.265 , pp. 19704-19711
    • Carpenter, C.L.1    Duckworth, B.C.2    Auger, K.R.3
  • 43
    • 0027953284 scopus 로고
    • PI 3-kinase is a dual specificity enzyme: Autoregulation by an intrinsic protein-serine kinase activity
    • Dhand R., Hiles I., Panayotou G., et al. (1994) PI 3-kinase is a dual specificity enzyme: autoregulation by an intrinsic protein-serine kinase activity. EMBO J. 13, 522-533.
    • (1994) EMBO J. , vol.13 , pp. 522-533
    • Dhand, R.1    Hiles, I.2    Panayotou, G.3
  • 44
    • 0025921611 scopus 로고
    • Cloning of PI3 kinase-associated p85 utilizing a novel method for expression/cloning of target proteins for receptor tyrosine kinases
    • Skolnik E.Y., Margolis B., Mohammadi M., et al. (1991) Cloning of PI3 kinase-associated p85 utilizing a novel method for expression/cloning of target proteins for receptor tyrosine kinases. Cell 65, 83-90.
    • (1991) Cell , vol.65 , pp. 83-90
    • Skolnik, E.Y.1    Margolis, B.2    Mohammadi, M.3
  • 46
    • 0035804251 scopus 로고    scopus 로고
    • The lipid phosphatase SHIP2 controls insulin sensitivity
    • Clement S., Krause U., Desmedt F., et al. (2001) The lipid phosphatase SHIP2 controls insulin sensitivity. Nature 409, 92-97.
    • (2001) Nature , vol.409 , pp. 92-97
    • Clement, S.1    Krause, U.2    Desmedt, F.3
  • 47
    • 0032904432 scopus 로고    scopus 로고
    • PTEN: A tumour suppressor that functions as a phospholipid phosphatase
    • Maehama T., Dixon J.E. (1999) PTEN: a tumour suppressor that functions as a phospholipid phosphatase. Trends Cell Biol. 9, 125-128.
    • (1999) Trends Cell Biol. , vol.9 , pp. 125-128
    • Maehama, T.1    Dixon, J.E.2
  • 48
    • 0037205048 scopus 로고    scopus 로고
    • The phosphoinositide 3-kinase pathway
    • Cantley L.C. (2002) The phosphoinositide 3-kinase pathway. Science 296, 1655-1657.
    • (2002) Science , vol.296 , pp. 1655-1657
    • Cantley, L.C.1
  • 49
    • 0023665111 scopus 로고
    • Common elements in growth factor stimulation and oncogenic transformation: 85 kd phosphoprotein and phosphatidylinositol kinase activity
    • Kaplan D.R., Whitman M., Schaffhausen B., et al. (1987) Common elements in growth factor stimulation and oncogenic transformation: 85 kd phosphoprotein and phosphatidylinositol kinase activity. Cell 50, 1021-1029.
    • (1987) Cell , vol.50 , pp. 1021-1029
    • Kaplan, D.R.1    Whitman, M.2    Schaffhausen, B.3
  • 50
    • 0029849774 scopus 로고    scopus 로고
    • Association between phosphatidylinositol-3 kinase, Cb1 and other tyrosine phosphorylated proteins in colony-stimulating factor-1-stimulated macrophages
    • Kanagasundaram V., Jaworowski A., and Hamilton J.A. (1996) Association between phosphatidylinositol-3 kinase, Cb1 and other tyrosine phosphorylated proteins in colony-stimulating factor-1-stimulated macrophages. Biochem. J. 320(Pt 1), 69-77.
    • (1996) Biochem. J. , vol.320 , Issue.1 PART , pp. 69-77
    • Kanagasundaram, V.1    Jaworowski, A.2    Hamilton, J.A.3
  • 51
    • 0028198388 scopus 로고
    • Activation of phosphatidylinositol-3′ kinase by Src-family kinase SH3 binding to the p85 subunit
    • Pleiman C.M., Hertz W.M., and Cambier J.C. (1994) Activation of phosphatidylinositol-3′ kinase by Src-family kinase SH3 binding to the p85 subunit. Science 263, 1609-1612.
    • (1994) Science , vol.263 , pp. 1609-1612
    • Pleiman, C.M.1    Hertz, W.M.2    Cambier, J.C.3
  • 52
    • 0026802515 scopus 로고
    • Nerve growth factor promotes the activation of phosphatidylinositol 3-kinase and its association with the trk tyrosine kinase
    • Soltoff S.P., Rabin S.L., Cantley L.C., et al. (1992) Nerve growth factor promotes the activation of phosphatidylinositol 3-kinase and its association with the trk tyrosine kinase. J. Biol. Chem. 267, 17,472-17,477.
    • (1992) J. Biol. Chem. , vol.267 , pp. 17472-17477
    • Soltoff, S.P.1    Rabin, S.L.2    Cantley, L.C.3
  • 53
    • 0031962265 scopus 로고    scopus 로고
    • SH2- and SH3-mediated interactions between focal adhesion kinase and Src
    • Thomas J.W., Ellis B., Boerner R.J., et al. (1998) SH2- and SH3-mediated interactions between focal adhesion kinase and Src. J. Biol. Chem. 273, 577-583.
    • (1998) J. Biol. Chem. , vol.273 , pp. 577-583
    • Thomas, J.W.1    Ellis, B.2    Boerner, R.J.3
  • 54
    • 0026742317 scopus 로고
    • Modification of the 85-kilodalton subunit of phosphatidylinositol-3 kinase in platelet-derived growth factor-stimulated cells
    • Kavanaugh W.M., Klippel A., Escobedo J.A., et al. (1992) Modification of the 85-kilodalton subunit of phosphatidylinositol-3 kinase in platelet-derived growth factor-stimulated cells. Mol. Cell Biol. 12, 3415-3424.
    • (1992) Mol. Cell Biol. , vol.12 , pp. 3415-3424
    • Kavanaugh, W.M.1    Klippel, A.2    Escobedo, J.A.3
  • 55
    • 0026344857 scopus 로고
    • Phosphorylation in vitro of the 85 kDa subunit of phosphatidylinositol 3-kinase and its possible activation by insulin receptor tyrosine kinase
    • Hayashi H., Miyake N., Kanai F., et al. (1991) Phosphorylation in vitro of the 85 kDa subunit of phosphatidylinositol 3-kinase and its possible activation by insulin receptor tyrosine kinase. Biochem. J. 280(Pt 3), 769-775.
    • (1991) Biochem. J. , vol.280 , Issue.3 PART , pp. 769-775
    • Hayashi, H.1    Miyake, N.2    Kanai, F.3
  • 56
    • 0028095620 scopus 로고
    • Structure, regulation and function of phosphoinositide 3-kinases
    • Fry M.J. (1994) Structure, regulation and function of phosphoinositide 3-kinases. Biochim. Biophys. Acta 1226, 237-268.
    • (1994) Biochim. Biophys. Acta , vol.1226 , pp. 237-268
    • Fry, M.J.1
  • 57
    • 0032512824 scopus 로고    scopus 로고
    • Interleukin-2 stimulation induces tyrosine phosphorylation of p120-Cb1 and CrkL and formation of multimolecular signaling complexes in T lymphocytes and natural killer cells
    • Gesbert F., Garbay C., and Bertoglio J. (1998) Interleukin-2 stimulation induces tyrosine phosphorylation of p120-Cb1 and CrkL and formation of multimolecular signaling complexes in T lymphocytes and natural killer cells. J. Biol. Chem. 273, 3986-3993.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3986-3993
    • Gesbert, F.1    Garbay, C.2    Bertoglio, J.3
  • 58
    • 0026720350 scopus 로고
    • Phosphatidylinositol 3-kinase: Structure and expression of the 110 kd catalytic subunit
    • Hiles I.D., Otsu M., Volinia S., et al. (1992) Phosphatidylinositol 3-kinase: structure and expression of the 110 kd catalytic subunit. Cell 70, 419-429.
    • (1992) Cell , vol.70 , pp. 419-429
    • Hiles, I.D.1    Otsu, M.2    Volinia, S.3
  • 59
    • 0034605626 scopus 로고    scopus 로고
    • Tyrosine phosphorylation is involved in phosphatidylinositol 3-kinase activation in bovine rod outer segments
    • Guo X.X., Huang Z., Bell M.W., et al. (2000) Tyrosine phosphorylation is involved in phosphatidylinositol 3-kinase activation in bovine rod outer segments. Mol. Vis. 6, 216-221.
    • (2000) Mol. Vis. , vol.6 , pp. 216-221
    • Guo, X.X.1    Huang, Z.2    Bell, M.W.3
  • 60
    • 0023752767 scopus 로고
    • IGF-I receptors in the bovine neural retina: Structure, kinase activity and comparison with retinal insulin receptors
    • Waldbillig R.J., Fletcher R.T., Somers R.L., et al. (1988) IGF-I receptors in the bovine neural retina: structure, kinase activity and comparison with retinal insulin receptors. Exp. Eye Res. 47, 587-607.
    • (1988) Exp. Eye Res. , vol.47 , pp. 587-607
    • Waldbillig, R.J.1    Fletcher, R.T.2    Somers, R.L.3
  • 61
    • 0023664702 scopus 로고
    • Insulin-like growth factor I receptors in retinal rod outer segments
    • Zick Y., Spiegel A.M., and Sagi-Eisenberg R. (1987) Insulin-like growth factor I receptors in retinal rod outer segments. J. Biol. Chem. 262, 10,259-10,264.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10259-10264
    • Zick, Y.1    Spiegel, A.M.2    Sagi-Eisenberg, R.3
  • 62
    • 0025119824 scopus 로고
    • Src homology region 2 domains direct protein-protein interactions in signal transduction
    • Moran M.F., Koch C.A., Anderson D., et al. (1990) Src homology region 2 domains direct protein-protein interactions in signal transduction. Proc. Natl. Acad. Sci. USA 87, 8622-8626.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 8622-8626
    • Moran, M.F.1    Koch, C.A.2    Anderson, D.3
  • 63
    • 0027409064 scopus 로고
    • Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: Crystal structures of the complexed and peptide-free forms
    • Waksman G., Shoelson S.E., Pant N., et al. (1993) Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: crystal structures of the complexed and peptide-free forms. Cell 72, 779-790.
    • (1993) Cell , vol.72 , pp. 779-790
    • Waksman, G.1    Shoelson, S.E.2    Pant, N.3
  • 65
    • 0027403027 scopus 로고
    • SH2 domains recognize specific phosphopeptide sequences
    • Songyang Z., Shoelson S.E., Chaudhuri M., et al. (1993) SH2 domains recognize specific phosphopeptide sequences. Cell 72, 767-778.
    • (1993) Cell , vol.72 , pp. 767-778
    • Songyang, Z.1    Shoelson, S.E.2    Chaudhuri, M.3
  • 66
    • 0028032895 scopus 로고
    • Alternative pathway of insulin signalling in mice with targeted disruption of the IRS-1 gene
    • Araki E., Lipes M.A., Patti M.E., et al. (1994) Alternative pathway of insulin signalling in mice with targeted disruption of the IRS-1 gene. Nature 372, 186-190.
    • (1994) Nature , vol.372 , pp. 186-190
    • Araki, E.1    Lipes, M.A.2    Patti, M.E.3
  • 67
    • 0028032894 scopus 로고
    • Insulin resistance and growth retardation in mice lacking insulin receptor substrate-1
    • Tamemoto H., Kadowaki T., Tobe K., et al. (1994) Insulin resistance and growth retardation in mice lacking insulin receptor substrate-1. Nature 372, 182-186.
    • (1994) Nature , vol.372 , pp. 182-186
    • Tamemoto, H.1    Kadowaki, T.2    Tobe, K.3
  • 68
    • 0036470613 scopus 로고    scopus 로고
    • Cytoskeleton participation in subcellular trafficking of signal transduction proteins in rod photoreceptor cells
    • McGinnis J.F., Matsumoto B., Whelan J.P., et al. (2002) Cytoskeleton participation in subcellular trafficking of signal transduction proteins in rod photoreceptor cells. J. Neurosci. Res. 67, 290-297.
    • (2002) J. Neurosci. Res. , vol.67 , pp. 290-297
    • McGinnis, J.F.1    Matsumoto, B.2    Whelan, J.P.3
  • 69
    • 0023697234 scopus 로고
    • Light-dependent subcellular movement of photoreceptor proteins
    • Whelan J.P., McGinnis J.F. (1988) Light-dependent subcellular movement of photoreceptor proteins. J. Neurosci. Res. 20, 263-270.
    • (1988) J. Neurosci. Res. , vol.20 , pp. 263-270
    • Whelan, J.P.1    McGinnis, J.F.2
  • 70
    • 0033894567 scopus 로고    scopus 로고
    • COX-2 inhibition prevents insulin-dependent diabetes in low-dose streptozotocin-treated mice
    • Tabatabaie T., Waldon A.M., Jacob J.M., et al. (2000) COX-2 inhibition prevents insulin-dependent diabetes in low-dose streptozotocin-treated mice. Biochem. Biophys. Res. Commun. 273, 699-704.
    • (2000) Biochem. Biophys. Res. Commun. , vol.273 , pp. 699-704
    • Tabatabaie, T.1    Waldon, A.M.2    Jacob, J.M.3
  • 71
    • 0032568457 scopus 로고    scopus 로고
    • Vitamin B2-based blue-light photoreceptors in the retinohypothalamic tract as the photoactive pigments for setting the circadian clock in mammals
    • Miyamoto Y., Sancar A. (1998) Vitamin B2-based blue-light photoreceptors in the retinohypothalamic tract as the photoactive pigments for setting the circadian clock in mammals. Proc. Natl. Acad. Sci. USA 95, 6097-6102.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6097-6102
    • Miyamoto, Y.1    Sancar, A.2
  • 72
    • 0033525721 scopus 로고    scopus 로고
    • The endogenous chromophore of retinal G protein-coupled receptor opsin from the pigment epithelium
    • Hao W. and Fong H.K. (1999) The endogenous chromophore of retinal G protein-coupled receptor opsin from the pigment epithelium. J. Biol. Chem. 274, 6085-6090.
    • (1999) J. Biol. Chem. , vol.274 , pp. 6085-6090
    • Hao, W.1    Fong, H.K.2
  • 73
    • 0021823168 scopus 로고
    • Src kinase catalyzes the phosphorylation and activation of the insulin receptor kinase
    • Yu K.T., Werth D.K., Pastan I.H., et al. (1985) src kinase catalyzes the phosphorylation and activation of the insulin receptor kinase. J. Biol. Chem. 260, 5838-5846.
    • (1985) J. Biol. Chem. , vol.260 , pp. 5838-5846
    • Yu, K.T.1    Werth, D.K.2    Pastan, I.H.3
  • 74
    • 0029955955 scopus 로고    scopus 로고
    • Src phosphorylates the insulin-like growth factor type I receptor on the autophosphorylation sites. Requirement for transformation by src
    • Peterson J.E., Kulik G., Jelinek T., et al. (1996) Src phosphorylates the insulin-like growth factor type I receptor on the autophosphorylation sites. Requirement for transformation by src. J. Biol. Chem. 271, 31,562-31,571.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31562-31571
    • Peterson, J.E.1    Kulik, G.2    Jelinek, T.3
  • 75
    • 0037059804 scopus 로고    scopus 로고
    • Light-dependent association of Src with photoreceptor rod outer segment membrane proteins in vivo
    • Ghalayini A.J., Desai N., Smith K.R., et al. (2002) Light-dependent association of Src with photoreceptor rod outer segment membrane proteins in vivo. J. Biol. Chem. 277, 1469-1476.
    • (2002) J. Biol. Chem. , vol.277 , pp. 1469-1476
    • Ghalayini, A.J.1    Desai, N.2    Smith, K.R.3
  • 76
    • 0036470213 scopus 로고    scopus 로고
    • Insulin signaling pathways in time and space
    • Saltiel A.R., Pessin J.E. (2002) Insulin signaling pathways in time and space. Trends Cell Biol. 12, 65-71.
    • (2002) Trends Cell Biol. , vol.12 , pp. 65-71
    • Saltiel, A.R.1    Pessin, J.E.2
  • 77
  • 78
    • 0018427565 scopus 로고
    • Photoreceptor outer segment development: Light and dark regulate the rate of membrane addition and loss
    • Hollyfield J.G., Rayborn M.E. (1979) Photoreceptor outer segment development: light and dark regulate the rate of membrane addition and loss. Investig. Ophthalmol. Vis. Sci. 18, 117-132.
    • (1979) Investig. Ophthalmol. Vis. Sci. , vol.18 , pp. 117-132
    • Hollyfield, J.G.1    Rayborn, M.E.2
  • 79
    • 0017297774 scopus 로고
    • Photoreceptor shedding is initiated by light in the frog retina
    • Basinger S., Huffman R., and Matthes M. (1976) Photoreceptor shedding is initiated by light in the frog retina. Science 194, 1074-1076.
    • (1976) Science , vol.194 , pp. 1074-1076
    • Basinger, S.1    Huffman, R.2    Matthes, M.3
  • 80
    • 0031054670 scopus 로고    scopus 로고
    • Insulin-like growth factor and potassium depolarization maintain neuronal survival by distinct pathways: Possible involvement of PI 3-kinase in IGF-1 signaling
    • D'Mello S.R., Borodezt K., and Soltoff S.P. (1997) Insulin-like growth factor and potassium depolarization maintain neuronal survival by distinct pathways: possible involvement of PI 3-kinase in IGF-1 signaling. J. Neurosci. 17, 1548-1560.
    • (1997) J. Neurosci. , vol.17 , pp. 1548-1560
    • D'Mello, S.R.1    Borodezt, K.2    Soltoff, S.P.3
  • 81
    • 1842370285 scopus 로고    scopus 로고
    • Nerve growth factor protects PC12 cells against peroxynitrite-induced apoptosis via a mechanism dependent on phosphatidylinositol 3-kinase
    • Spear N., Estevez A.G., Barbeito L., et al. (1997) Nerve growth factor protects PC12 cells against peroxynitrite-induced apoptosis via a mechanism dependent on phosphatidylinositol 3-kinase. J. Neurochem. 69, 53-59.
    • (1997) J. Neurochem. , vol.69 , pp. 53-59
    • Spear, N.1    Estevez, A.G.2    Barbeito, L.3
  • 82
    • 0015207786 scopus 로고
    • Irreversible effects on visible light on the retina: Role of vitamin A
    • Noell W.K., Albrecht R. (1971) Irreversible effects on visible light on the retina: role of vitamin A. Science 172, 76-79.
    • (1971) Science , vol.172 , pp. 76-79
    • Noell, W.K.1    Albrecht, R.2
  • 83
    • 0019190592 scopus 로고
    • Possible mechanisms of photoreceptor damage by light in mammalian eyes
    • Noell W.K. (1980) Possible mechanisms of photoreceptor damage by light in mammalian eyes. Vision Res. 20, 1163-1171.
    • (1980) Vision Res. , vol.20 , pp. 1163-1171
    • Noell, W.K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.