2
Views
5
CrossRef citations to date
0
Altmetric
Research Article

The Role of Insulin Receptor Sulphydryl Groups in Insulin Binding and Cellular Response in Rat Adipocytes

&
Pages 45-59 | Published online: 26 Sep 2008

References

  • Wilden P. A., Morrison B. D., Pessin J. E. Relationship between the insulin receptor subunit association and protein kinase activation: Insulin-dependent covalent and Mn/Mg ATP-dependent non-covalent associaton of αβ heterodimeric insulin receptors into an α2β2 heterotetrameric state. Biochemistry 1989; 28: 785–792
  • Klip A., Douen A. G. Role of kinases in insulin stimulation of glucose transport. J. Memb. Biol. 1989; 111: 1–23
  • Schweitzer J. B., Smith R. M., Jarett L. Differences in organizational structure of insulin receptor on rat adipocyte and liver plasma membranes: Role of disulfide bonds. Proc. Natl. Acad. Sci. USA 1980; 77: 4692–4696
  • Jarett L., Smith R. M. Partial disruption of naturally occuring groups of insulin receptors of adipocyte plasma membranes by dithiol and N-ethylmaleimide: The role of disulfide bonds. Proc. Natl. Acad. Sci. USA 1983; 80: 1023–1093
  • Czech M. P., Massague J., Pilch P. F. The insulin receptor structural features. Trends Biochem. Sci. 1981; 6: 223–225
  • Boni-Schnetzler M., Kaligian A., DelVecchio R., Pilch P. F. Ligand-dependent intersubunit association within the insulin receptor complex activates its intrinsic kinase activity. J. Biol. Chem. 1988; 263: 6822–6828
  • Boni-Schnetzler M., Rubin J. B., Pilch P. F. Structural requirements for the transmembrane activation of the insulin receptor kinase. J. Biol. Chem. 1986; 261: 15281–15287
  • Schenker E., Kohanski R. A. Conformational states of the insulin receptor. Biochem. Biophys. Res. Comm. 1988; 157: 140–145
  • Wilden P. A., Boyle T. R., Swanson M. L., Sweet L. J., Pessin J. E. Alteration of disulfides in insulin receptor/kinase by insulin and dithiothreitol: Insulin potentiates the apparent dithiothreitol-dependent subunit reduction of the insulin receptor. Biochem stry 1986; 25: 4381–4388
  • Kubar J., Van Obberghen E. Oligomeric states of the insulin receptor: Binding and autophosphorylation properties. Biochemistry 1989; 28: 1086–1093
  • Chen J-J., Kosower N. S., Petryshyn R., London I. M. The effects of N-ethylmaleimide on the phosphorylation and aggregation of insulin receptors in the isolated plasma membrane of 3T3-F422A adipocytes. J. Biol. Chem. 1986; 261: 902–908
  • Hannestad U., Sorbo B. Derivitization of dithiols and certain monothiols with phenylarsine oxide for gas chromatography. J. Chromatogr. 1980; 200: 171–177
  • Douen A. G., Jones M. N. Insulin processing and signal transduction in rat adipocytes. Biochim. Biophys. Acta 1989; 1010: 363–368
  • Douen A. G., Jones M. N. The action of phenylarsine oxide on the stereospecific uptake of D-glucose in basal and insulin stimulated rat adipocytes. Biochim. Biophys. Acta 1988; 968: 109–118
  • Walker-Smith D. J., Payne J. W. Characteristics of the protein carrier of the peptide transport system in the scutellum of germinating barley embryos. Planta 1984; 162: 166–173
  • Rodbell M. Metabolism of isolated fat cells: I. Effects of hormones on glucose metabolism and lipolysis. J. Biol. Chem. 1960; 239: 375–380
  • Krebs H. A., Henseleit K. Urea formation in the animal body. Hoppe-Seyler's Z. Physiol. Chem. 1932; 210: 33–36
  • Glieman J., Osterlind K., Vinten J., Gammeltoft S. A procedure for measurement of distribution spaces in isolated rat adipocytes. Biochim. Biophys. Acta 1972; 286: 1–9
  • Simpson I. A., Yver D. R., Hissin P. J., Wardzala L. J., Karnieli E., Salans L. B., Cushman S. W. Insulin stimulated translocation of glucose transporters in the isolated rat adipose cells: Characterization of subcellular fractions. Biochim. Biophys. Acta 1983; 763: 292–407
  • Douen A. G., Kacem R., Jones M. N. Direct interaction of phenylarsine oxide with hexose transporters in isolated adipocytes. Biochim. Biophys. Acta 1988; 944: 444–450
  • Atkinson A., Gatenby A. D., Lowe A. G. The determination of inorganic orthophosphate in biological systems. Biochim. Biophys. Acta 1973; 320: 195–204
  • Bradford M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal. Biochem. 1976; 72: 248–254
  • Jones M. N., More J. E., Riley D. J. A thermodynamic approach to hormone-receptor interaction application to insulin binding to adipocytes, adipocyte plasma membranes and liposomes incorporating adipocyte insulin receptors. J. Receptor Res. 1986; 6: 361–380
  • Scatchard F. Attractions of proteins for small molecules and ions. Ann. N.Y. Acad. Sci. 1949; 57: 660–670
  • Olefsky J. M., Reaven G. M. Effects of age and obesity on insulin binding to isolated adipocytes. Endocrinology 1975; 96: 1486–1498
  • De Meyts P., Roth J., Neville D. M., Gavin J. R., Lesniak M. A. Insulin interaction with its receptors: Experimental evidence for negative cooperativity. Biochem. Biophys. Res. Comm. 1973; 55: 154–161
  • Etherton T. D., Walker O. A. Characterization of insulin binding to isolated swine adipocytes. Endocrinology 1982; 110: 1720–1724
  • Calderwood S. K., Hahn G. M. Thermal sensitivity and resistance of insulin-receptor binding. Biochim. Biophys. Acta 1983; 756: 1–8
  • Draznin B., Trowbridge M., Ferguson L. Quantitative studies of the rate of insulin internalization in isolated rat hepatocytes. Biochem. J. 1984; 218: 307–312
  • Knutson V. P., Ronnett G. V., Lane M. D. Rapid, reversible internalization of cell surface insulin receptors. J. Biol. Chem. 1983; 258: 12139–12142
  • Walker-Smith D. J., Payne J. W. Peptide uptake in germinating barley embryos involves a dithiol-dependent transport protein. FEBS Letters 1983; 160: 25–30
  • Yip C. C., Hsu H., Patel R. G., Hawley D. M., Maddux B. A., Goldfine I. D. Localization of insulin-binding to the cysteine region of the insulin receptor α-subunit. Biochem. Biophys. Res. Commun. 1988; 157: 321–329
  • Waugh S. M., DiBella E. E., Pilch P. F. Isolation of a proteolytically derived domain of the insulin receptor containing the major site of cross-linking/binding. Biochemistry 1989; 28: 3448–3455
  • Ullrich A., Bell J. R., Chen E. Y., Herrera R., Petruzzelli L. M., Dull T. J., Gray A., Coussens L., Liao Y-C., Tsobokawa M., Mason A., Seeburg P. H., Grunfeld C., Rosen O. M., Ramachandran J. Human insulin receptor and its relationship to the tyrosine kinase family of oncogenes. Nature 1985; 313: 756–761
  • Ebina Y., Ellis L., Jarnagin K., Edery M., Graf L., Clauser E., Ou J., Masairz F., Kan Y. W., Goldfine I. D., Rutter W. J. The human insulin receptor cDNA: The structural basis for hormone-activated transmembrane signalling. Cell 1985; 40: 747–758
  • Pike L. J., Eakes A. T., Krebs E. G. Characterization of affinity-purified receptor kinase. J. Biol. Chem. 1986; 261: 3782–3789
  • Pastan I. H., Willingham M. C. Receptor-mediated endocytosis of hormones in cultured cells. Ann. Rev. Physiol. 1981; 43: 239–250
  • Lerea K. M., Livingston J. N. A thiol-sensitive degradative process of liver uncouples autophosphorylation of the insulin receptor from insulin binding. Biochem. J. 1986; 236: 535–542
  • Kono T., Barham F. W. The relationship between the insulin-binding capacity of fat cells and the cellular response to insulin. J. Biol. Chem. 1971; 246: 6210–6216

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.