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Research Article

The Human Insulin Receptor Cdna: A New Tool to study the Function of this Receptor

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Pages 377-404 | Published online: 26 Sep 2008

References

  • Ronnett G. V., Knutson V. P., Kohanski R. A., Simpson T. L., Lane M. D. Role of glycosylation in the processing of newly translated insulin proreceptor in 3T3-L1 adipocytes. J. Biol. Chem. 1984; 259: 4566–4575
  • Pilch P. F., Czech M. P. Interaction of cross-linking agents with the insulin effector system of isolated fat cells. J. Biol. Chem. 1979; 254: 3375–3381
  • Kasuga M., Zick Y., Blith D. L., Karlssom F. A., Karing H. U., Kahn C. R. Insulin stimulation of phosphorylation of the ß-subunit of the insulin receptor. Formation of both phosphoserine and phosphotyrosine. J. Biol. Chem. 1982; 257: 9891–9894
  • Roth R. A., Cassell D. J. Insulin receptor: evidence that it is a protein kinase. Science 1983; 219: 299–301
  • Hunter T. The proteins of oncogenes Sci. Am. 1984; 251: 70–79
  • Cohen S., Carpenter G., King L. E., Jr. Epidermal growth factor-receptor-protein kinase interactions Co-purification of receptor and epidermal growth factor enhanced phosphorylation activity. J. Biol. Chem. 1980; 255: 4834–4842
  • Heldin C. H., Ek B., Ronnstrand L. Characterization of the receptor for platelet-derived growth factor on human fibroblasts. J. Biol. Chem. 1983; 258: 10054–10061
  • Jacobs S., Kull F. C., Jr, Earp H. S., Svoboda M. E., Van Wyk J. J., Cuatrecasas P. Somatomedin C stimulates the phosphorylation of the beta-subunit of its own receptor. J. Biol. Chem. 1983; 258: 9581–9584
  • Ebina Y., Ellis L., Jarnagin K., Edery M., Graf L., Clauser E., Ou J., Masiarz F., Kan Y. W., Goldfine I. D., Roth R. A., Rutter W. J. The human insulin receptor cDNA: The structural basis for hormone-activated transmembrane signalling. Cell 1985; 40: 747–758
  • Ullrich A., Bell J. R., Chen E. Y., Herrera R., Petruzelli L. M., Dull T. J., Gray A., Coussens L., Liao Y. C., Tsubokawa M., Mason A., Seeburg P. H., Grunfeld C., Rosen O. M., Ramachandran J. Human insulin receptor and its relationships to the tyrosine kinase family of oncogenes. Nature 1985; 313: 756–761
  • Roth R. A., Mesirow M. L., Cassell D. J. Preferential degradation of the beta-subunit of purified insulin receptor. Effect on insulin binding and protein kinase activities of the receptor. J. Biol. Chem. 1983; 258: 14456
  • Bohlen O., Stein S., Stone J., Undenfriend S. Automatic monitoring of primary amines in preparative column effluents with fluorescamine. Anal. Biochem. 1975; 67: 438
  • Hunkapiller M. W., Hewich R. M., Dreyer W. J., Hood L. E. High sensitivity sequencing with a gas-phase sequenator. Meth. Enzymol. 1983; 92: 399
  • Maniatis T., Fritsch E F., Sambrook J. Molecular cloning Cold Spring Harbor. Cold Spring Harbor Laboratory, New York 1982
  • Huynh T. V., Young R. A., Davis R. W. DNA Cloning, M. Glover. IRL Press, Oxford, Washington, DC, vol.1: 49–78
  • Wallace R. B., Schold M., Johnson M. J., Dembek P., Itakura K. Oligonucleotide directed mutagenesis of the human beta-globin gene: a general method for producing specific point mutations in cloned DNA. Nucl. Acids Res. 1981; 9: 3647–3656
  • Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain terminating inhibitors. Proc. Natl. Acad. Sci. USA 1977; 74: 5463–5467
  • Rice C. M., Franke C. A., Strauss J. H., Hruby D. E. Expression of Sindbis virus structural proteins via recombinant vaccinia virus: synthesis, processing and incorporation into mature Sindbis virions. J. Virol. 1985; 56: b227–239
  • Zoller M., Smith M. Oligonucleotide-directed mutagenesis: a simple method using two oligonucleotide primers and a single stranded DNA template. DNA 1984; 3: 479–488
  • Southern P. J., Berg P. Transformation of mammalian cells to antibiotic resistance with a bacterial gene under control of SV40 early region promoter. J. Mol. Appl. Genet. 1982; 1: 327–341
  • Ebina Y., Edery M., Ellis L., Standring D. N., Beaudoin J., Roth R. A., Rutter W. J. Expression of a functional human insulin receptor from a cloned cDNA in Chinese hamster ovary cells. Proc. Natl. Acad. Sci. USA 1985; 82: 8014–8018
  • Ellis L., Clauser E., Morgan D., Edery M., Roth R. A., Rutter W. J. Replacement of insulin receptor tyrosine residues 1162 and 1163 compromises insulin-stimulated kinase activity and uptake of 2-deoxyglucose. Cell 1986; 45: 721–732
  • Ellis L., Morgan D., Clauser E., Roth R. A., Rutter W. J. A membrane-anchored cytoplasmic domain of the human insulin receptor mediates a constitutively elevated insulin-independent uptake of 2-deoxyglucose. Mol. Endocribol.
  • Cuatrecasas P. Properties of the insulin receptor isolated from liver and fat cell membranes. J. Biol. Chem. 1972; 247: 1980–1991
  • Ullrich A., Coussens L., Hayflick J. S., Dull T. J., Gray A., Tam A. W., Lee J., Yarden Y., Libermann T. A., Schlessinger J., Downward J., Mayes E. L.V., Whittle N., Waterfield M. D., Seeburg P. H. Human epidermal growth factor receptor cDNA sequence and aberrant expression of the amplified gene in A431 epidermoid carcinoma cells. Nature 1984; 309: 418–425
  • Yamamoto T., Davis C. G., Brown M. S., Schneider W. J., Casey M. L., Goldstein J. L., Russel D. W. The human LDL receptor: a cystein-rich protein with multiple Alu sequences in its RNA. Cell 1984; 39: 27–38
  • Grunfeld C., Kwan Shigenaga J., Ramachandran J. Urea treatment allows dithiothreitol to release the binding subunit of the insulin receptor from the cell membrane: Implications for the structural organization of the insulin receptor. Biochem. Biophys. Res. Com. 1985; 133: 389–396
  • Petruzelli L., Herrera R., Rosen O. M. The insulin receptor is an insulin-dependent tyrosine phosphokinase: Copurification of insulin-binding activity and protein kinase activity to homogeneity from human placenta. Proc. Natl. Acad. Sci. USA 1984; 81: 3327–3331
  • White M. F., Takayama S., Kahn C. R. Differences in the sites of phosphorylation of the insulin receptor in vivo and in vitro. J. Biol. Chem. 1985; 260: 9470–9478
  • Yu K. T., Czech M. P. Tyrosine phosphorylation of the insulin receptor beta subunit activates receptor associated tyrosine kinase activity. J. Biol. Chem. 1984; 259: 5277–5286
  • Nickameyer W. S., Wang L. H. Nucleotide sequence of avian sarcoma virus UR2 and comparison of its transforming gene with other members of the tyrosine kinase oncogene family. J. Virol. 1985; 53: 879–884
  • Jarett L., Seals J. R. Pyruvate dehydrogenase activation in adipocyte mitochondria by an insulin-generated mediator from muscle. Science 1979; 206: 1407–1408
  • Larner J., Galasko G., Cheng K., Depaoli-Roach A. A., Huang L., Daggy P., Kellog J. Generation by insulin of a chemical mediator that controls protein phosphorylation and dephosphorylation. Science 1979; 206: 1408–1410
  • Morgan D. O., Ho L., Korn L. J., Roth R. A. Insulin action is blocked by a monoclonal antibody that inhibits the insulin receptor kinase. Proc. Natl. Acad. Sci. USA 1986; 83: 328–332
  • Stadtmaner L., Rosen O. M. Increasing the cAMP content of IM-9-cells alters the phosphorylation state and protein kinase activity of the insulin receptor. J. Biol. Chem. 1986; 261: 3402–3407
  • Herrera R., Petruzzelli L., Thomas N., Bramson H. N., Kaiser E. T., Rosen O. M. An antipeptide antibody that specifically inhibits insulin receptor autophosphorylation and protein kinase activity. Proc. Natl. Acad. Sci. USA 1985; 82: 7899–7903
  • Shaw D. J., Bell G. I. RsaI polymorphism at the insulin receptor locus (INSR) on chromosome 19. Nucl. Acids Res. 1985; 13: 8661

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