0363-6119/94 $3.00 Copyright membrane. The receptor in all vertebrate species studied so far, including a primitive Agnathan hagfish, is a heterotetramer containing two extracellular a-subunits and two transmembrane p-subunits (9). When binds to the a-subunits, a conformational change takes place, which activates tyrosine kinase activity of the cytoplasmatic domain of the P-subunits, initiating a phosphorylation cascade that leads eventually to signal transduction (19). The process can be modulated by changes in receptor capacity and affinity as well and in tyrosine kinase activity. Decline of one or more of these parameters has been found in -resistant (obese) mammals (7, 25) and in humans with non--dependent diabetes mellitus (NIDDM) (7, 11). In contrast, either fasting or high-carbohydrate diet caused in mammals an upregulation of both binding capacity and tyrosine kinase activity of (3,lO). -receptor binding in liver, and heart , brain, red blood cells, and gonads has been studied in variety of fish species (13, 16, 17, 22, 27, 28, 30). Autophosphorylation of the receptor of the stingray Dasyatis americana liver and lamprey Lampetra fZuviatilis liver have been reported (32, 24), and the phosphorylation of exogenous substrates by receptor of carp ovaries was demonstrated (16). Although Leibush (22) has compared
AJP - Regulatory, Integrative and Comparative Physiology – The American Physiological Society
Published: Jun 1, 1994
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