Insulin secretion in vitro and insulin binding to isolated hepatocytes in congenic mice with different H-2 complexes

Congenic male mice with differences in the H-2 complex have been used to investigate insulin secretion in vitro, insulin binding to isolated hepatocytes, plasma glucose, and serum insulin. Plasma glucose and serum insulin did not show consistent differences in the B10.BR, B10.D2, B10.A, B10.G, B10.M, B10.S, C57/10SCSN, and C3H.OH strains. Isolated islets of Langerhans responded to stimulation with 400 mg/dl glucose with a 3-5-fold increase in insulin secretion rates (2P less than 0.01): B10.BR greater than B10.M greater than C57BL/10SCSN greater than B10.G greater than C3H.OH, B10.D2, B10.A, B10.S. The biphasic pattern of insulin secretion was less distinct in B10.M, B10.G, and C3H.OH mice. The high-affinity constants of insulin binding to isolated hepatocytes at 37 degrees C varied between 4.5 X 10(7) L X mol-1 and 4.5 X 10(8) L X mol-1 (2P less than 0.01): B10.A greater than B10.BR greater than C57BL/10SCSN, B10.S, B10.D2 greater than B10.M, B10.G. The glucose-stimulated insulin secretion from isolated islets of Langerhans and the binding of insulin to isolated hepatocytes correlate to the H-2 complex independently.