메뉴 건너뛰기




Volumn 7, Issue 12, 2012, Pages

Agonism and Antagonism at the Insulin Receptor

Author keywords

[No Author keywords available]

Indexed keywords

INSULIN RECEPTOR; PROTEIN KINASE B; THYMIDINE;

EID: 84871658759     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0051972     Document Type: Article
Times cited : (44)

References (50)
  • 1
    • 0020065416 scopus 로고
    • Insulin stimulates the phosphorylation of the 95,000-dalton subunit of its own receptor
    • Kasuga M, Karlsson FA, Kahn CR (1982) Insulin stimulates the phosphorylation of the 95,000-dalton subunit of its own receptor. Science 215, 185-187.
    • (1982) Science , vol.215 , pp. 185-187
    • Kasuga, M.1    Karlsson, F.A.2    Kahn, C.R.3
  • 2
    • 0020417020 scopus 로고
    • Insulin activates a tyrosine-specific protein kinase in extracts of 3T3-L1 adipocytes and human placenta
    • Petruzzelli LM, Ganguly S, Smith CJ, Cobb MH, Rubin CS, et al. (1982) Insulin activates a tyrosine-specific protein kinase in extracts of 3T3-L1 adipocytes and human placenta. Proc. Natl. Acad. Sci. U. S. A. 79, 6792-6796.
    • (1982) Proc. Natl. Acad. Sci. U. S. A , vol.79 , pp. 6792-6796
    • Petruzzelli, L.M.1    Ganguly, S.2    Smith, C.J.3    Cobb, M.H.4    Rubin, C.S.5
  • 3
    • 0021924895 scopus 로고
    • The human insulin receptor cDNA: the structural basis for hormone-activated transmembrane signalling
    • Ebina Y, Ellis L, Jarnagin K, Edery M, Graf L, et al. (1985) The human insulin receptor cDNA: the structural basis for hormone-activated transmembrane signalling. Cell 40, 747-758.
    • (1985) Cell , vol.40 , pp. 747-758
    • Ebina, Y.1    Ellis, L.2    Jarnagin, K.3    Edery, M.4    Graf, L.5
  • 4
    • 0021985413 scopus 로고
    • Human insulin receptor and its relationship to the tyrosine kinase family of oncogenes
    • Ullrich A, Bell JR, Chen EY, Herrera R, Petruzzelli LM, et al. (1985) Human insulin receptor and its relationship to the tyrosine kinase family of oncogenes. Nature 313, 756-761.
    • (1985) Nature , vol.313 , pp. 756-761
    • Ullrich, A.1    Bell, J.R.2    Chen, E.Y.3    Herrera, R.4    Petruzzelli, L.M.5
  • 5
    • 0022800838 scopus 로고
    • Insulin-like growth factor I receptor primary structure: comparison with insulin receptor suggests structural determinants that define functional specificity
    • Ullrich A, Gray A, Tam AW, Yang-Feng T, Tsubokawa M, et al. (1986) Insulin-like growth factor I receptor primary structure: comparison with insulin receptor suggests structural determinants that define functional specificity. EMBO J. 5, 2503-2512.
    • (1986) EMBO J , vol.5 , pp. 2503-2512
    • Ullrich, A.1    Gray, A.2    Tam, A.W.3    Yang-Feng, T.4    Tsubokawa, M.5
  • 6
    • 0023193876 scopus 로고
    • High-level expression of human insulin receptor cDNA in mouse NIH 3T3 cells
    • Whittaker J, Okamoto AK, Thys R (1987) High-level expression of human insulin receptor cDNA in mouse NIH 3T3 cells. Proc. Natl. Acad. Sci. U. S. A. 84, 5237-5241.
    • (1987) Proc. Natl. Acad. Sci. U. S. A , vol.84 , pp. 5237-5241
    • Whittaker, J.1    Okamoto, A.K.2    Thys, R.3
  • 7
    • 0033786922 scopus 로고    scopus 로고
    • Protein tyrosine kinase structure and function
    • Hubbard SR, Till JH (2000) Protein tyrosine kinase structure and function. Annu. Rev. Biochem. 69, 373-398.
    • (2000) Annu. Rev. Biochem , vol.69 , pp. 373-398
    • Hubbard, S.R.1    Till, J.H.2
  • 8
    • 0028146822 scopus 로고
    • The structural basis of insulin and insulin-like growth factor-I receptor binding and negative co-operativity, and its relevance to mitogenic versus metabolic signalling
    • De Meyts P (1994) The structural basis of insulin and insulin-like growth factor-I receptor binding and negative co-operativity, and its relevance to mitogenic versus metabolic signalling. Diabetologia 37 Suppl 2, S135-S148.
    • (1994) Diabetologia , vol.37 , Issue.SUPPL. 2
    • De Meyts, P.1
  • 10
    • 0028268592 scopus 로고
    • A model for insulin binding to the insulin receptor
    • Schäffer L (1994) A model for insulin binding to the insulin receptor. Eur. J. Biochem. 221, 1127-1132.
    • (1994) Eur. J. Biochem , vol.221 , pp. 1127-1132
    • Schäffer, L.1
  • 11
    • 33748639228 scopus 로고    scopus 로고
    • Structure of the insulin receptor ectodomain reveals a folded-over conformation
    • McKern NM, Lawrence MC, Streltsov VA, Lou MZ, Adams TE, et al. (2006) Structure of the insulin receptor ectodomain reveals a folded-over conformation. Nature 443, 218-221.
    • (2006) Nature , vol.443 , pp. 218-221
    • McKern, N.M.1    Lawrence, M.C.2    Streltsov, V.A.3    Lou, M.Z.4    Adams, T.E.5
  • 12
    • 60749092852 scopus 로고    scopus 로고
    • Harmonic oscillator model of the insulin and IGF1 receptors' allosteric binding and activation
    • Kiselyov VV, Versteyhe S, Gauguin L, De Meyts P (2009) Harmonic oscillator model of the insulin and IGF1 receptors' allosteric binding and activation. Mol. Sys. Biol 5, 243.
    • (2009) Mol. Sys. Biol , vol.5 , pp. 243
    • Kiselyov, V.V.1    Versteyhe, S.2    Gauguin, L.3    De Meyts, P.4
  • 13
    • 82455186745 scopus 로고    scopus 로고
    • Insight into the molecular basis for the kinetic differences between the two insulin receptor isoforms
    • Knudsen L, De Meyts, P, Kiselyov VV (2011) Insight into the molecular basis for the kinetic differences between the two insulin receptor isoforms. Biochem. J. 440(3), 397-403.
    • (2011) Biochem. J , vol.440 , Issue.3 , pp. 397-403
    • Knudsen, L.1    De Meyts, P.2    Kiselyov, V.V.3
  • 14
    • 0025055479 scopus 로고
    • Antagonistic effects of a covalently dimerized insulin derivative on insulin receptors in 3T3-L1 adipocytes
    • Weiland M, Brandenburg C, Brandenburg D, Joost HG (1990) Antagonistic effects of a covalently dimerized insulin derivative on insulin receptors in 3T3-L1 adipocytes. Proc. Natl. Acad. Sci. U. S. A. 87, 1154-1158.
    • (1990) Proc. Natl. Acad. Sci. U. S. A , vol.87 , pp. 1154-1158
    • Weiland, M.1    Brandenburg, C.2    Brandenburg, D.3    Joost, H.G.4
  • 15
    • 0037151087 scopus 로고    scopus 로고
    • Peptides identify the critical hotspots involved in the biological activation of the insulin receptor
    • Pillutla RC, Hsiao KC, Beasley JR, Brandt J, Ostergaard S, et al. (2002) Peptides identify the critical hotspots involved in the biological activation of the insulin receptor. J. Biol. Chem. 277, 22590-22594.
    • (2002) J. Biol. Chem , vol.277 , pp. 22590-22594
    • Pillutla, R.C.1    Hsiao, K.C.2    Beasley, J.R.3    Brandt, J.4    Ostergaard, S.5
  • 17
    • 36849015259 scopus 로고    scopus 로고
    • Activation of the insulin receptor by insulin and a synthetic peptide leads to divergent metabolic and mitogenic signaling and responses
    • Jensen M, Hansen B, De Meyts P, Schäffer L, Ursø B (2007) Activation of the insulin receptor by insulin and a synthetic peptide leads to divergent metabolic and mitogenic signaling and responses. J. Biol. Chem. 282, 35179-35186.
    • (2007) J. Biol. Chem , vol.282 , pp. 35179-35186
    • Jensen, M.1    Hansen, B.2    De Meyts, P.3    Schäffer, L.4    Ursø, B.5
  • 19
    • 77956267447 scopus 로고    scopus 로고
    • Synchronization in G0/G1 enhances the mitogenic response of cells overexpressing the human insulin receptor A isoform to insulin
    • Bonnesen C, Nelander G-M, Hansen BF, Jensen P, Krabbe JS, et al. (2010) Synchronization in G0/G1 enhances the mitogenic response of cells overexpressing the human insulin receptor A isoform to insulin. Cell Biol. Toxicol. 26, 293-307.
    • (2010) Cell Biol. Toxicol , vol.26 , pp. 293-307
    • Bonnesen, C.1    Nelander, G.-M.2    Hansen, B.F.3    Jensen, P.4    Krabbe, J.S.5
  • 20
    • 68949144905 scopus 로고    scopus 로고
    • MCF-7 human mammary adenocarcinoma cells exhibit augmented responses to human insulin on a collagen IV surface
    • Listov-Saabye N, Jensen MB, Kiehr B, Hansen EW, Svendsen JE, et al. (2009) MCF-7 human mammary adenocarcinoma cells exhibit augmented responses to human insulin on a collagen IV surface. J. Appl. Toxicol. 29, 470-477.
    • (2009) J. Appl. Toxicol , vol.29 , pp. 470-477
    • Listov-Saabye, N.1    Jensen, M.B.2    Kiehr, B.3    Hansen, E.W.4    Svendsen, J.E.5
  • 21
    • 79957588372 scopus 로고    scopus 로고
    • Comparison of intracellular signalling by insulin and the hypermitogenic AspB10 analogue in MCF-7 breast adenocarcinoma cells
    • Oleksiewicz MB, Bonnesen C, Hegelund AC, Lundby A, Holm GM, et al. (2011) Comparison of intracellular signalling by insulin and the hypermitogenic AspB10 analogue in MCF-7 breast adenocarcinoma cells. J. Appl. Toxicol. 31, 329-341.
    • (2011) J. Appl. Toxicol , vol.31 , pp. 329-341
    • Oleksiewicz, M.B.1    Bonnesen, C.2    Hegelund, A.C.3    Lundby, A.4    Holm, G.M.5
  • 23
    • 0029862845 scopus 로고    scopus 로고
    • Sustained signalling from the insulin receptor after stimulation with insulin analogues exhibiting increased mitogenic potency
    • Hansen BF, Danielsen GM, Drejer K, Sørensen AR, Wiberg FC, et al. (1996) Sustained signalling from the insulin receptor after stimulation with insulin analogues exhibiting increased mitogenic potency. Biochem. J. 315, 271-279.
    • (1996) Biochem. J , vol.315 , pp. 271-279
    • Hansen, B.F.1    Danielsen, G.M.2    Drejer, K.3    Sørensen, A.R.4    Wiberg, F.C.5
  • 24
    • 0018388190 scopus 로고
    • Kinetic parameters of transport of 3-O-Methylglucose and glucose in adipocytes
    • Whitesell RR, Gliemann J (1979) Kinetic parameters of transport of 3-O-Methylglucose and glucose in adipocytes. J. Biol. Chem. 254, 5276-5283.
    • (1979) J. Biol. Chem , vol.254 , pp. 5276-5283
    • Whitesell, R.R.1    Gliemann, J.2
  • 25
    • 33244464562 scopus 로고    scopus 로고
    • Critical nodes in signalling pathways: insights into insulin action
    • Taniguchi CM, Emanuelli B, Kahn CR (2006) Critical nodes in signalling pathways: insights into insulin action. Nat. Rev. Mol. Cell Biol. 7, 85-96.
    • (2006) Nat. Rev. Mol. Cell Biol , vol.7 , pp. 85-96
    • Taniguchi, C.M.1    Emanuelli, B.2    Kahn, C.R.3
  • 26
    • 34447625738 scopus 로고    scopus 로고
    • Multiple GPCR conformations and signalling pathways: implications for antagonist affinity estimates
    • Baker JG, Hill SJ (2007) Multiple GPCR conformations and signalling pathways: implications for antagonist affinity estimates. Trends Pharmacol. Sci. 28, 374-381.
    • (2007) Trends Pharmacol. Sci , vol.28 , pp. 374-381
    • Baker, J.G.1    Hill, S.J.2
  • 27
    • 0026764441 scopus 로고
    • Rational design of potent antagonists to the human growth hormone receptor
    • Fuh G, Cunningham BC, Fukunaga R, Nagata S, Goeddel DV, et al. (1992) Rational design of potent antagonists to the human growth hormone receptor. Science 256, 1677-1680.
    • (1992) Science , vol.256 , pp. 1677-1680
    • Fuh, G.1    Cunningham, B.C.2    Fukunaga, R.3    Nagata, S.4    Goeddel, D.V.5
  • 28
    • 84995826606 scopus 로고
    • Receptor dimerization determines the effects of growth hormone in primary rat adipocytes and cultured human IM-9 lymphocytes
    • Ilondo MM, Damholt AB, Cunningham BA, Wells JA, De Meyts P, et al. (1994) Receptor dimerization determines the effects of growth hormone in primary rat adipocytes and cultured human IM-9 lymphocytes. Endocrinology 134, 2397-2403.
    • (1994) Endocrinology , vol.134 , pp. 2397-2403
    • Ilondo, M.M.1    Damholt, A.B.2    Cunningham, B.A.3    Wells, J.A.4    De Meyts, P.5
  • 29
    • 0036782071 scopus 로고    scopus 로고
    • Structural biology of insulin and IGF1 receptors: Implications for drug design
    • De Meyts P, Whittaker J (2002) Structural biology of insulin and IGF1 receptors: Implications for drug design. Nat. Rev. Drug Discov. 1, 769-783.
    • (2002) Nat. Rev. Drug Discov , vol.1 , pp. 769-783
    • De Meyts, P.1    Whittaker, J.2
  • 30
    • 33746347333 scopus 로고    scopus 로고
    • Tyrphostins and other tyrosine kinase inhibitors
    • Levitzki A, Mishani E (2006) Tyrphostins and other tyrosine kinase inhibitors. Annu. Rev. Biochem. 75, 93-109.
    • (2006) Annu. Rev. Biochem , vol.75 , pp. 93-109
    • Levitzki, A.1    Mishani, E.2
  • 31
    • 41249097332 scopus 로고    scopus 로고
    • A molecular view of anti-ErbB monoclonal antibody therapy
    • Leahy DJ (2008) A molecular view of anti-ErbB monoclonal antibody therapy. Cancer Cell 13, 291-293.
    • (2008) Cancer Cell , vol.13 , pp. 291-293
    • Leahy, D.J.1
  • 34
    • 0020334260 scopus 로고
    • Characterization of [LeuB-24]- and [LeuB-25]-insulin analogues. Receptor binding and biological activity
    • Kobayashi M, Ohgaku S, Iwasaki M, Maegawa H, Shigeta Y, et al. (1982) Characterization of [LeuB-24]- and [LeuB-25]-insulin analogues. Receptor binding and biological activity. Biochem. J. 206, 597-603.
    • (1982) Biochem. J , vol.206 , pp. 597-603
    • Kobayashi, M.1    Ohgaku, S.2    Iwasaki, M.3    Maegawa, H.4    Shigeta, Y.5
  • 36
    • 0019869810 scopus 로고
    • Impaired negative cooperativity of the semisynthetic analogues human [LeuB24]- and [LeuB25]-insulins
    • Keefer LM, Piron MA, De Meyts P, Gattner HG, Diaconescu C, et al. (1981) Impaired negative cooperativity of the semisynthetic analogues human [LeuB24]- and [LeuB25]-insulins. Biochem. Biophys. Res. Commun. 100, 1229-1236.
    • (1981) Biochem. Biophys. Res. Commun , vol.100 , pp. 1229-1236
    • Keefer, L.M.1    Piron, M.A.2    De Meyts, P.3    Gattner, H.G.4    Diaconescu, C.5
  • 38
    • 0018102801 scopus 로고
    • Mapping of the residues responsible for the negative cooperativity of the receptor-binding region of insulin
    • De Meyts P, Van Obberghen E, Roth J, Brandenburg D, Wollmer A (1978) Mapping of the residues responsible for the negative cooperativity of the receptor-binding region of insulin. Nature 273, 504-509.
    • (1978) Nature , vol.273 , pp. 504-509
    • De Meyts, P.1    Van Obberghen, E.2    Roth, J.3    Brandenburg, D.4    Wollmer, A.5
  • 39
    • 0022474285 scopus 로고
    • Monoclonal antibodies reacting with multiple epitopes on the human insulin receptor
    • Soos MA, Siddle K, Baron MD, Heward JM, Luzio JP, et al. (1986) Monoclonal antibodies reacting with multiple epitopes on the human insulin receptor. Biochem. J. 235, 199-208.
    • (1986) Biochem. J , vol.235 , pp. 199-208
    • Soos, M.A.1    Siddle, K.2    Baron, M.D.3    Heward, J.M.4    Luzio, J.P.5
  • 40
    • 0026632363 scopus 로고
    • A panel of monoclonal antibodies for the type I insulin-like growth factor receptor. Epitope mapping, effects on ligand binding, and biological activity
    • Soos MA, Field CE, Lammers R, Ullrich A, Zhang B, et al. (1992) A panel of monoclonal antibodies for the type I insulin-like growth factor receptor. Epitope mapping, effects on ligand binding, and biological activity. J. Biol. Chem. 267, 12955-12963.
    • (1992) J. Biol. Chem , vol.267 , pp. 12955-12963
    • Soos, M.A.1    Field, C.E.2    Lammers, R.3    Ullrich, A.4    Zhang, B.5
  • 41
    • 0023853790 scopus 로고
    • Reversal of insulin-induced negative cooperativity by monoclonal antibodies that stabilize the slowly dissociating ("Ksuper") state of the insulin receptor
    • Gu JL, Goldfine ID, Forsayeth JR, De Meyts P (1988) Reversal of insulin-induced negative cooperativity by monoclonal antibodies that stabilize the slowly dissociating ("Ksuper") state of the insulin receptor. Biochem. Biophys. Res. Commun. 150, 694-701.
    • (1988) Biochem. Biophys. Res. Commun , vol.150 , pp. 694-701
    • Gu, J.L.1    Goldfine, I.D.2    Forsayeth, J.R.3    De Meyts, P.4
  • 42
    • 0023721910 scopus 로고
    • Insulin and insulin-like growth factor I regulate the same biological functions in HEP-G2 cells via their own specific receptors
    • Verspohl EJ, Maddux BA, Goldfine ID (1988) Insulin and insulin-like growth factor I regulate the same biological functions in HEP-G2 cells via their own specific receptors. J. Clin. Endocrinol. Metab. 67, 169-174.
    • (1988) J. Clin. Endocrinol. Metab , vol.67 , pp. 169-174
    • Verspohl, E.J.1    Maddux, B.A.2    Goldfine, I.D.3
  • 43
    • 34247872895 scopus 로고    scopus 로고
    • Characterization of insulin/IGF hybrid receptors: Contributions of the insulin receptor L2 and Fn1 domains and the alternatively spliced exon 11 sequence to ligand binding and receptor activation
    • Benyoucef S, Surinya KH, Hadaschik D, Siddle K (2007) Characterization of insulin/IGF hybrid receptors: Contributions of the insulin receptor L2 and Fn1 domains and the alternatively spliced exon 11 sequence to ligand binding and receptor activation. Biochem. J., 403, 603-613.
    • (2007) Biochem. J , vol.403 , pp. 603-613
    • Benyoucef, S.1    Surinya, K.H.2    Hadaschik, D.3    Siddle, K.4
  • 44
    • 79951511000 scopus 로고    scopus 로고
    • Relative influence of testosterone and insulin in the regulation of prostatic cell proliferation and growth
    • Vikram A, Kushwaha S, Jena GB (2011) Relative influence of testosterone and insulin in the regulation of prostatic cell proliferation and growth. Steroids 76, 416-423.
    • (2011) Steroids , vol.76 , pp. 416-423
    • Vikram, A.1    Kushwaha, S.2    Jena, G.B.3
  • 45
    • 77955058188 scopus 로고    scopus 로고
    • S961, an insulin receptor antagonist causes hyperinsulinemia, insulin-resistance and depletion of energy stores in rats
    • Vikram A, Jena G (2010) S961, an insulin receptor antagonist causes hyperinsulinemia, insulin-resistance and depletion of energy stores in rats. Biochem. Biophys. Res. Commun. 398, 260-265.
    • (2010) Biochem. Biophys. Res. Commun , vol.398 , pp. 260-265
    • Vikram, A.1    Jena, G.2
  • 46
    • 65449168837 scopus 로고    scopus 로고
    • Ligand-induced activation of the insulin receptor: a multi-step process involving structural changes in both the ligand and the receptor
    • Ward CW, Lawrence MC (2009) Ligand-induced activation of the insulin receptor: a multi-step process involving structural changes in both the ligand and the receptor. BioEssays 31, 422-434.
    • (2009) BioEssays , vol.31 , pp. 422-434
    • Ward, C.W.1    Lawrence, M.C.2
  • 47
    • 84863884698 scopus 로고    scopus 로고
    • α-Helical element at the hormone-binding surface of the insulin receptor functions as a signalling element to activate its tyrosine kinase
    • Whittaker J, Whittaker LJ, Roberts CT Jr, Phillips NB, Ismail-Beigi F, et al. (2012) α-Helical element at the hormone-binding surface of the insulin receptor functions as a signalling element to activate its tyrosine kinase. Proc. Natl. Acad. Sci. U.S.A. 109, 11166-11171.
    • (2012) Proc. Natl. Acad. Sci. U.S.A , vol.109 , pp. 11166-11171
    • Whittaker, J.1    Whittaker, L.J.2    Roberts Jr., C.T.3    Phillips, N.B.4    Ismail-Beigi, F.5
  • 48
    • 67049158418 scopus 로고    scopus 로고
    • A thermodynamic study of ligand binding to the first three domains of the human insulin receptor: Relationship between the receptor α-chain c-terminal peptide and the site 1 insulin mimetic peptides
    • Menting JG, Ward CW, Margetts MB, Lawrence MC (2009) A thermodynamic study of ligand binding to the first three domains of the human insulin receptor: Relationship between the receptor α-chain c-terminal peptide and the site 1 insulin mimetic peptides. Biochemistry 48, 5492-5500.
    • (2009) Biochemistry , vol.48 , pp. 5492-5500
    • Menting, J.G.1    Ward, C.W.2    Margetts, M.B.3    Lawrence, M.C.4
  • 49
    • 77951058594 scopus 로고    scopus 로고
    • Structural resolution of a tandem hormone-binding element in the insulin receptor and its implications for design of peptide agonists
    • Smith BJ, Huang K, Kong G, Chan SJ, Nakagawa S, et al. (2010) Structural resolution of a tandem hormone-binding element in the insulin receptor and its implications for design of peptide agonists. Proc. Natl. Acad. Sci. U.S.A. 107, 6771-6776.
    • (2010) Proc. Natl. Acad. Sci. U.S.A , vol.107 , pp. 6771-6776
    • Smith, B.J.1    Huang, K.2    Kong, G.3    Chan, S.J.4    Nakagawa, S.5
  • 50
    • 84862616645 scopus 로고    scopus 로고
    • Similar but different: ligand-induced activation of the insulin and epidermal growth factor receptor families
    • Ward CW, Lawrence MC (2012) Similar but different: ligand-induced activation of the insulin and epidermal growth factor receptor families. Curr. Opin. Struct. Biol. 22, 360-366.
    • (2012) Curr. Opin. Struct. Biol , vol.22 , pp. 360-366
    • Ward, C.W.1    Lawrence, M.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.