Peptidylglycine amidating monooxygenase
The overall effect is to slow the rate of appearance (Ra) of glucose in the blood after eating; this is accomplished via coordinate slowing down gastric emptying, inhibition of digestive secretion [gastric acid, pancreatic enzymes, and bile ejection], and a resulting reduction in food intake.
Appearance of new glucose in the blood is reduced by inhibiting secretion of the gluconeogenic hormone glucagon.
This is a condition wherein the body is unable to utilize insulin effectively, resulting in increased insulin production; since proinsulin and pro IAPP are cosecreted, this results in an increase in the production of pro IAPP as well.
Although little is known about IAPP regulation, its connection to insulin indicates that regulatory mechanisms that affect insulin also affect IAPP.
IAPP was identified independently by two groups as the major component of diabetes-associated islet amyloid deposits in 1987.
The difference in nomenclature is largely geographical; European researchers tend to prefer IAPP whereas American researchers tend to prefer amylin.
Thus blood glucose levels play an important role in regulation of pro IAPP synthesis.
Amylin functions as part of the endocrine pancreas and contributes to glycemic control.
Pro IAPP is secreted simultaneously, however, the enzymes that convert these precursor molecules into insulin and IAPP, respectively, are not able to keep up with the high levels of secretion, ultimately leading to the accumulation of pro IAPP.Some researchers discourage the use of "amylin" on the grounds that it may be confused with the pharmaceutical company.Islet amyloid formation, initiated by the aggregation of pro IAPP, may contribute to this progressive loss of islet β-cells.The unprocessed pro IAPP can then serve as the granule upon which IAPP can accumulate and form amyloid.Initially, the pro IAPP aggregates within secretory vesicles inside the cell.