Changes in amylin and amylin-like peptide concentrations and beta-cell function in response to sulfonylurea or insulin therapy in NIDDM

What Was Tested

Researchers studied Amylin (Islet Amyloid Polypeptide) in this randomized controlled trial publication.

Amylin, a secretory peptide of beta-cells, is the constituent peptide of islet amyloid, which is characteristic of NIDDM, and changes in amylin secretion in response to therapies may influence the rate of production of islet amyloid.

The primary objective of this study was to determine whether therapy with sulfonylurea or basal insulin in NIDDM would alter amylin secretion in a way that might affect the formation of islet amyloid.

Who Took Part

PubMed indexes the participants as middle-aged adults and older adults, both men and women.

In a randomized crossover design, eight subjects with NIDDM underwent three 8-week periods of therapy with diet alone, sulfonylurea, or exogenous basal insulin, with evaluation of amylin, amylin-like peptide (ALP), and glucose and C-peptide concentrations, both during fasting and after a standard breakfast.

Changes in beta-cell function (% beta) were assessed, in the basal state by homeostasis model assessment (HOMA) and in the stimulated state by hyperglycemic clamps.

How the Study Was Run

The design is described as randomized and crossover.

Because people in this Amylin (Islet Amyloid Polypeptide) study were split into groups at random, differences between the groups are less likely to reflect who happened to join each one.

Each person switched between Amylin (Islet Amyloid Polypeptide) and the comparison at some point, usually with a gap in between.

Seven nondiabetic control subjects each underwent a meal profile and hyperglycemic clamp.

What Was Measured

The subject headings attached to it are Amyloid, Blood Glucose, C-Peptide, Diabetes Mellitus, Type 2, Fasting, Glucose and Glucose Clamp Technique.

What This Means in Plain Language

The paper is a randomized and crossover study of Amylin (Islet Amyloid Polypeptide).

Its findings take up roughly 5 sentences of the abstract and are left out here on purpose; the source paper is the place to read them.

The publication is from 1998 (Diabetes care), a journal based in United States.

More context: the Amylin (Islet Amyloid Polypeptide) compound page, all human trials.