Basal and stimulated plasma levels of pancreatic amylin indicate its co-secretion with insulin in humans
Open accessAbstract
Amylin is a 37-amino acid pancreatic polypeptide, probably involved in the pathophysiology of Type 2 (non-insulin-dependent) diabetes mellitus. We have determined amylin in human plasma by extraction-based radioimmunoassay (Sep-Pak C18). Of 23 healthy control subjects plasma amylin was determined as 11.9 +/- 3.5 ng/l. Of 27 patients with Type 2 diabetes receiving insulin the amylin levels were lower, and in 16 patients with Type 2 diabetes on oral medication they were higher than in the control subjects; 8.2 +/- 4.4 ng/l (p less than 0.01) vs 18.8 +/- 9.9 ng/l (p less than 0.05). In 14 Type 1 (insulin-dependent) diabetic patients we found extremely low mean amounts of amylin: 2.9 +/- 1.9 ng/l (p less than 0.002). Thus, basal amylin appears to be associated with the capacity to release insulin. An oral glucose load stimulated the release of amylin, this was more pronounced in patients with Type 2 diabetes than in healthy subjects. An excellent correlation of mean amylin with mean insulin concentrations was obtained (r = 0.949). In patients with Type 2 diabetes amylin was reduced congruent to decreases in C-peptide during a hyperinsulinaemic, euglycaemic glucose clamp experiment (r = 0.971 for linear correlation between C-peptide levels and amylin). We conclude, that amylin and insulin are co-secreted in humans, and that the amylin release is under feedback-control by insulin.
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Circulating amylin levels are higher in humans and animal models of obesity and type 2 diabetes.
“Higher levels of circulating amylin were found in humans and animal models of obesity and type 2 diabetes (24, 88, 151, 184).”
From The Activity of Peptides of the Calcitonin Family in Bone (2019) · cites this paper as [88]
The section on plasma amylin concentrations reports higher levels in humans with type 2 diabetes taking oral medication than in healthy controls, but lower levels in those receiving insulin (page unavailable). The paper does not report circulating amylin levels in obesity or animal models, so it supports only part of the cited statement. (LLM, conf=0.90)
Experimental — accuracy not yet measuredAmylin suppresses postprandial glucagon and delays gastric emptying.
“It suppresses postprandial glucagon and delays gastric emptying (46).”
From New Frontiers in Obesity Treatment: GLP-1 and Nascent Nutrient-Stimulated Hormone-Based Therapeutics (2023) · cites this paper as [46]
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- Authors
- Hartter, E., Svoboda, T., Ludvik, B., Schuller, M., Lell, B., Kuenburg, E., Brunnbauer, M., Woloszczuk, W., & Prager, R.
- Affiliations
- University of Vienna (AT)
- Venue
- Diabetologia
- Published
- 1991-01
- Volume
- 34
- Issue
- 1
- Pages
- 52-54
- ISSN
- 0012-186X (ISSN-L)
- 1432-0428
- OpenAlex
- W2028720966
- Semantic Scholar
- 7bcce23d22ccce45511afbba3d1f5ba261c8e68f
- Cited by
- 191
- References
- 11
- Citations by year
- 2026: 2 · 2025: 5 · 2024: 4 · 2023: 6 · 2022: 5 · 2021: 10 · 2020: 6 · 2019: 1 · 2018: 12 · 2017: 5 · 2016: 5 · 2015: 3 · 2014: 1 · 2013: 5 · 2012: 2
- FWCI
- 17.77
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Diabetologia (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Strong
- Topics
- Health Sciences › Medicine › Surgery › Pancreatic function and diabetes
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Diabetes Treatment and Management
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuropeptides and Animal Physiology
- Keywords
- amylin, insulin, co-secretion, type 2 diabetes, type 1 diabetes, oral glucose tolerance, hyperinsulinemic-euglycemic clamp, C-peptide, pancreatic polypeptide
- MeSH terms
- Insulin Secretion, Adult, Amyloid, C-Peptide, Diabetes Mellitus, Type 1, Diabetes Mellitus, Type 2, Glucose, Humans, Insulin, Islets of Langerhans, Kinetics, Middle Aged, Reference Values, Time Factors, Islet Amyloid Polypeptide
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