A study of insulin binding sites in the chicken tissues.
Specific binding of chicken and porcine insulin was demonstrated in isolated chicken hepatocytes, chicken liver plasma membranes and chicken erythrocytes. In the liver, the binding reaction was characterized by a sensitivity and an apparent affinity which were similar to those observed in rat liver and, in contrast, by a decreased number of binding sites. In chicken liver, there were about 5 times fewer binding sites per mg of membrane protein or per unit of cell surface area than in rat liver. In chicken erythrocytes, the number of insulin binding sites per cell was even lower than in chicken hepatocytes. This decreased insulin binding was not accounted for by a faster insulin degradation in chicken tissues. Glucagon binding sites also appeared to be less numerous in chicken than in rat liver, at least at low glucagon concentration; however, the decrease in maximal binding capacity in chicken liver involved insulin and not glucagon binding. That chicken cells are equipped with insulin receptors which are less numerous than in mammalian cells may explain, partly at least, the physiological state of insulin resistance observed in the chicken.
D000262:Adenylyl Cyclases / Q000378:metabolism; D000818:Animals; D002462:Cell Membrane / Q000378:metabolism; D002645:Chickens; D004912:Erythrocytes / Q000378:metabolism*; D005934:Glucagon / Q000378:metabolism; D007328:Insulin / Q000378:metabolism*; D008099:Liver / Q000378:metabolism*; D051381:Rats; D011972:Receptor, Insulin / Q000378:metabolism*; D013552:Swine; D013696:Temperature
D007328:Insulin; D005934:Glucagon; D011972:Receptor, Insulin; D000262:Adenylyl Cyclases