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IGF I Receptor Phosphorylation

  • Cary Moxham
  • Vincent Duronio
  • Steven Jacobs

Abstract

Physiologically, cells are simultaneously exposed to a plethora of hormones. The way in which a cell responds to stimulation by a specific hormone depends not only upon the concentration of that hormone, but upon the presence of other hormones as well. Receptors for both insulin and IGF I are phosphorylated when cells are exposed to phorbol esters, presumably through activation of protein kinase-C (1–4). Since protein kinase C is physiologically activated by a number of hormones whose receptors are coexpressed with insulin and IGF I receptors, it seems possible that these hormones could regulate responsiveness of insulin and IGF I receptors by activating protein kinase C.

Keywords

Insulin Receptor Phorbol Ester Beta Subunit Receptor Internalization Antiphosphotyrosine Antibody 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1989

Authors and Affiliations

  • Cary Moxham
    • 1
  • Vincent Duronio
    • 1
  • Steven Jacobs
    • 1
  1. 1.Research Triangle ParkBurroughs Wellcome Co.USA

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