ABSTRACT
The protein monomers that undergo abnormal self-aggregation to form the insoluble fibrils present in each form of amyloidosis are derived from one of several precursor proteins present in the blood or tissues. A number of forms of amyloidosis have an even more obvious and well-recognized association specifically with diseases of advanced age. Cerebral and cerebrovascular amyloidosis in Alzheimer's disease, islet amyloidosis in type II diabetes mellitus, and cardiac amyloidosis in Senile Systemic Amyloidosis are the most universally recognized examples of this more direct relationship between amyloidosis and aging. A more intensive and serious interest in the relationship between islet amyloid and type II diabetes mellitus was elicited with the discovery that islet amyloid represents a concentrated and aggregated form of a previously unknown islet-derived hormone. Like with many other amyloid fibril proteins, it has been shown that human islet amyloid polypeptide has a strong intrinsic tendency to form insoluble fibrils with properties typical of amyloid fibrils.
