Abstract
Despite detailed understanding of the structure, biosynthesis, and metabolic effects of insulin, it is not known how the interaction of insulin with its receptor generates a biological signal (Cobb and Rosen, 1984). Evidence for mediation of insulin action by a small peptide second messenger has been presented (Larner et al., 1978; Seals and Jarrett, 1980; Seals and Czech, 1980). Recently, however, the discovery that the insulin receptor is associated with an insulin-dependent protein kinase activity (Kasuga et al., 1982a,b,c; Petruzzelli et al., 1982; Van Obberghen and Kowalski, 1982; Haring et al., 1982; Zick et al., 1983a,b; Avruch et al., 1982; Shia and Pilch, 1983; Van Obberghen et al., 1983; Kasuga et al., 1983; Rosen et al., 1983) has suggested additional or alternative models for transduction of the insulin signal (for review, see Cobb and Rosen, 1984). In this chapter we present (1) our evidence that the insulin receptor is itself an insulin-dependent tyrosine protein kinase; (2) the properties of the enzyme derived from an insulin-sensitive cell line, 3T3-L1, and from human placenta; and (3) possible roles of the insulin-dependent protein kinase in bioregulation.
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© 1985 Plenum Press, New York
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Petruzzelli, L.M. et al. (1985). The Insulin Receptor as a Tyrosine- Specific Protein Kinase. In: Poste, G., Crooke, S.T. (eds) Mechanisms of Receptor Regulation. New Horizons in Therapeutics. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-2131-6_4
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DOI: https://doi.org/10.1007/978-1-4613-2131-6_4
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