Islet amyloid in Type 2 (non-insulin-dependent) diabetes is related to insulin.
Amyloid deposition is the most typical islet alteration in Type 2 (non-insulin-dependent) diabetes. In the present study we show by immunohistochemistry that the amyloid reacts with an antiserum against insulin B chain. Islet amyloid was also purified, dissolved in guanidine-HCl and gel filtered on a Sepharose 6B column. Immunization of a guinea pig with a high molecular weight fraction from this gel filtration resulted in an antiserum with insulin-binding capacity. This binding was partially blocked with pure insulin B chain. The results indicate that islet amyloid contains insulin B chain and that the amyloid is a product of the islet B cells. Thus the study support previous morphological studies.
D000368:Aged; D000682:Amyloid / Q000032:analysis; D000686:Amyloidosis / Q000150:complications / Q000378:metabolism*; D000818:Animals; D002850:Chromatography, Gel; D048909:Diabetes Complications; D003920:Diabetes Mellitus / Q000378:metabolism*; D005260:Female; D006168:Guinea Pigs / Q000276:immunology; D006801:Humans; D007124:Immunoenzyme Techniques; D007328:Insulin / Q000378:metabolism*; D007330:Insulin Antibodies; D007515:Islets of Langerhans / Q000378:metabolism*; D008297:Male
D000682:Amyloid; D007328:Insulin; D007330:Insulin Antibodies