Inhibitors of the insulin receptor tyrosine kinase.
Insulin is a polypeptide hormone consisting of 51 amino acids. Insulin promotes a variety of anabolic enzymatic pathways and inhibits many catabolic enzymatic pathways involved in energy storage, as well as in synthesis of structural tissue proteins. In addition, insulin serves as a growth factor, modulating mitogenesis, growth and differentiation. Insulin mediates all of its effects by initially binding and activating its specific cell-surface receptor. Conformational changes induced by insulin binding lead to activation of intrinsic receptor tyrosine kinase. Thus, the study of tyrosine kinase inhibitors, whether synthetically produced or purified from microorganisms or humans, has led to elucidation of molecular details of physiological insulin signaling.
Department of Internal Medicine, Wayne State University, Detroit, MI 48201.
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Srinivas
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Grunberger
D000818:Animals; D006801:Humans; D007328:Insulin / Q000502:physiology*; D017027:Protein Tyrosine Phosphatases / Q000502:physiology; D011505:Protein-Tyrosine Kinases / Q000037:antagonists & inhibitors* / Q000502:physiology; D011972:Receptor, Insulin / Q000037:antagonists & inhibitors* / Q000502:physiology; D015398:Signal Transduction / Q000502:physiology; D013329:Structure-Activity Relationship
D007328:Insulin; D011505:Protein-Tyrosine Kinases; D011972:Receptor, Insulin; D017027:Protein Tyrosine Phosphatases