Immunohistochemical study of islet amyloid in diabetes mellitus.
Amyloid was isolated from islets of amyloidotic pancreata of monkey and human beings by solubilization of non-amyloid materials from the pancreas and digestion of contaminating collagen and elastin. The resulting pellet was estimated to be greater than 90% pure islet amyloid. Antibodies specific for monkey islet amyloid and for monkey and human liver amyloid A (AA) were raised in rabbits. Immunohistochemical reaction using the peroxidase antiperoxidase method demonstrated that amyloidotic pancreas reacted with both anti-AA and anti-islet amyloid antibodies. Although the antibodies are specific toward antigens, they cross-react with tissues from human and monkeys. The immunochemical results suggest the possibility that more than one kind of amyloid is associated with islet amyloidosis, but that a significant portion of the islet amyloid is related to AA. Preliminary chemical analysis indicated that islet amyloid is enriched with hexosamines while AA contains both hexosamines and hexoses. Establishment of the islet amyloid composition(s) can give insight into its source and its role in diabetes in Macaca nigra and human beings.
D000682:Amyloid / Q000032:analysis*; D000818:Animals; D003920:Diabetes Mellitus / Q000378:metabolism*; D003921:Diabetes Mellitus, Experimental / Q000378:metabolism*; D006801:Humans; D007124:Immunoenzyme Techniques; D007515:Islets of Langerhans / Q000032:analysis*; D008099:Liver / Q000032:analysis; D008251:Macaca; D000685:Serum Amyloid A Protein / Q000032:analysis
D000682:Amyloid; D000685:Serum Amyloid A Protein