By H.P.T. Ammon, H.U. Häring, M. Kellerer, H. Laube, L. Mosthaf, E.J. Verspohl and M.A. Wahl (Eds.)
Quantity 27, the 1st thematic quantity within the sequence, presents an outline of current wisdom with reference to the pharmacological and scientific features of antidiabetic medications. It goals to stimulate extra attention of attainable ideas within the improvement of latest antidiabetic medicines.
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Extra info for Antidiabetic Agents: Recent Advances in their Molecular and Clinical Pharmacology
1989) and specificity for ligand binding. , 1989). The 12 amino acids at the C-terminus of the a-subunit also appear to play MECHANISMS OF INSULIN ACTION 31 a role in insulin binding, since the presence of these amino acids (insulin receptor isoform B) results in a decrease in insulin affinity. The coupling of the a-subunit to the extracellular part of the/3-subunit occurs through disulphide bonds. There is some evidence from tryptic cleavage experiments (Frias and Waugh, 1989) that the amino acids involved in the disulphide coupling are located in positions 435,468 or 524 in the a-chain.
Finland has a leading position with 28 cases/100 000 per year. 8/100 000). This again suggests a predominant effect of environmental factors in the genesis of Type-I diabetes. The incidence rate of Type-I diabetes may also vary considerably over a narrow geographic range. 2/100000, pointing to an effect of different genetic background. 2 CLINICAL SYMPTOMS The onset of the autoimmune disease Type-I diabetes has a protracted prodromal period. Overt symptoms such as hyperglycaemia occur only months and years after initial metabolic and immunological abnormalities such as impaired glucose tolerance, ICA and IAA are noted.
1989). These naturally occurring hybrid receptors could give new insights into the specific forms of insulin resistance. This is suggested by studies with hybrid receptors that consist of mutated kinase-inactive a,/3-insulin receptor dimers or IGF-I receptor dimers. , 1992). Furthermore, studies with chimeric insulin receptors in which residues 191-290 of the IGF-I receptor replaced the corresponding domain of the insulin receptor gave interesting results, conferring on insulin and IGF-Iligand specificity and affinity.