Effects of meal ingestion on plasma amylin concentration in NIDDM and nondiabetic humans - PubMed (original) (raw)

Effects of meal ingestion on plasma amylin concentration in NIDDM and nondiabetic humans

P C Butler et al. Diabetes. 1990 Jun.

Abstract

Recent interest has focused on the potential role of amylin in the pathogenesis of non-insulin-dependent diabetes mellitus (NIDDM). This 37-amino acid peptide is found in extracellular amyloid deposits in approximately 50% of pancreatic islets of patients with NIDDM and has been shown to inhibit skeletal muscle glycogen synthesis in vitro. Immunocytochemical studies have colocalized amylin and insulin within beta-cell secretory granules in nondiabetic humans, provoking the following questions. Is amylin cosecreted with insulin? Are circulating amylin concentrations higher in patients with NIDDM either before or after food ingestion? To answer these questions, we developed a sensitive and specific immunoassay to measure plasma concentrations of amylin in humans. Use of this assay indicated that, in lean nondiabetic subjects, glucose ingestion resulted in an increase (P less than 0.001) in the plasma concentration of amylin (from 2.03 +/- 0.22 to 3.78 +/- 0.39 pM) and insulin (from 48.3 +/- 3.1 to 265 +/- 44 pM). There was a significant correlation between the concentrations of insulin and amylin (r = 0.74, P less than 0.001) and the increase in insulin and amylin concentration (r = 0.65, P less than 0.005). Fasting concentrations of amylin did not differ in diabetic and weight-matched nondiabetic subjects and showed a similar pattern of change after ingestion of a mixed meal. We conclude that amylin is secreted in response to ingestion of either glucose or a mixed meal and circulates at concentrations that do not differ in patients with NIDDM and nondiabetic subjects. It remains to be determined whether amylin at physiological concentrations influences carbohydrate metabolism and if so whether its effects differ in diabetic and nondiabetic humans.

PubMed Disclaimer

Cited by

Degradation of islet amyloid polypeptide by neprilysin.
Guan H, Chow KM, Shah R, Rhodes CJ, Hersh LB. Guan H, et al. Diabetologia. 2012 Nov;55(11):2989-98. doi: 10.1007/s00125-012-2678-y. Epub 2012 Aug 17. Diabetologia. 2012. PMID: 22898766 Free PMC article.
Neurodevelopmental Programming of Adiposity: Contributions to Obesity Risk.
Skowronski AA, Leibel RL, LeDuc CA. Skowronski AA, et al. Endocr Rev. 2024 Mar 4;45(2):253-280. doi: 10.1210/endrev/bnad031. Endocr Rev. 2024. PMID: 37971140 Free PMC article. Review.
Ionic strength effects on amyloid formation by amylin are a complicated interplay among Debye screening, ion selectivity, and Hofmeister effects.
Marek PJ, Patsalo V, Green DF, Raleigh DP. Marek PJ, et al. Biochemistry. 2012 Oct 30;51(43):8478-90. doi: 10.1021/bi300574r. Epub 2012 Oct 16. Biochemistry. 2012. PMID: 23016872 Free PMC article.
Human-IAPP disrupts the autophagy/lysosomal pathway in pancreatic β-cells: protective role of p62-positive cytoplasmic inclusions.
Rivera JF, Gurlo T, Daval M, Huang CJ, Matveyenko AV, Butler PC, Costes S. Rivera JF, et al. Cell Death Differ. 2011 Mar;18(3):415-26. doi: 10.1038/cdd.2010.111. Epub 2010 Sep 3. Cell Death Differ. 2011. PMID: 20814419 Free PMC article.
Interactions of gastrointestinal peptides: ghrelin and its anorexigenic antagonists.
Wisser AS, Habbel P, Wiedenmann B, Klapp BF, Mönnikes H, Kobelt P. Wisser AS, et al. Int J Pept. 2010;2010:817457. doi: 10.1155/2010/817457. Epub 2010 Jan 6. Int J Pept. 2010. PMID: 20798884 Free PMC article.

Effects of meal ingestion on plasma amylin concentration in NIDDM and nondiabetic humans - PubMed (original) (raw)