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 c atabolic enzymatic pathways involved in energy storage, as well as in synthesis of structural tissue proteins. In addition, insulin serves a s a growth factor, modulating mitogenesis, growth and differentiation. Insulin mediates all of its effects by initially binding and activati ng its specific cell-surface receptor. Conformational changes induced by insulin binding lead to activation of intrinsic receptor tyrosine k inase. Thus, the study of tyrosine kinase inhibitors, whether syntheti cally produced or purified from microorganisms of humans, has led to e lucidation of molecular details of physiological insulin signaling.