Co-localization of islet amyloid polypeptide and insulin in the B cell secretory granules of the human pancreatic islets
Open accessAbstract
Islet amyloid polypeptide is a novel 37 amino-acid-residues polypeptide which has been isolated from amyloid deposits in an insulinoma, and in human and cat islets of Langerhans. The molecule has 46% homology with the calcitonin gene-related peptide. Light microscopy examination of the pancreas shows that islet amyloid polypeptide immunoreactivity is restricted to the islet B cells. The present study utilized a rabbit antiserum against a synthetic peptide corresponding to positions 20-29 of islet amyloid polypeptide, a sequence without any amino-acid identity with calcitonin gene-related peptide. By applying the immunogold technique at the ultrastructural level, it was shown that both insulin and islet amyloid polypeptide immunoreactivity occurs in the central granular core of the human B cell secretory granules, while the A cells remain unlabelled. The demonstration that islet amyloid polypeptide is a granular protein of the B cells may indicate that it is released together with insulin. Further studies are necessary to evaluate the functional role of islet amyloid polypeptide.
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IAPP is co-localized within the same secretory granules as insulin and is typically co-released with insulin in vitro in response to glucose and non-glucose secretagogues.
“IAPP is co-localized within the same secretory granules as insulin [115] and is typically co-released with insulin in vitro in response to glucose and non-glucose secretagogues [116, 117].”
From The relative contributions of insulin resistance and beta-cell dysfunction to the pathophysiology of type 2 diabetes (2003) · cites this paper as [115]
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- Authors
- Lukinius, A., Wilander, E., Westermark, G. T., Engstr�m, U., & Westermark, P.
- Affiliations
- Uppsala University Hospital (SE)
- Linköping University Hospital (SE)
- Ludwig Cancer Research (SE)
- Venue
- Diabetologia
- Published
- 1989-04
- Volume
- 32
- Issue
- 4
- Pages
- 240-244
- ISSN
- 0012-186X (ISSN-L)
- 1432-0428
- OpenAlex
- W2004210837
- Cited by
- 371
- References
- 28
- Citations by year
- 2026: 5 · 2025: 3 · 2024: 8 · 2023: 1 · 2022: 5 · 2021: 7 · 2020: 4 · 2019: 9 · 2018: 9 · 2017: 5 · 2016: 6 · 2015: 11 · 2014: 7 · 2013: 9 · 2012: 8
- FWCI
- 42.77
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Diabetologia (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Medical Research Council
- Topics
- Health Sciences › Medicine › Surgery › Pancreatic function and diabetes
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuropeptides and Animal Physiology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Diabetes and associated disorders
- Keywords
- amylin, insulin, B cells, secretory granules, colocalization, pancreatic islets, calcitonin gene-related peptide, insulinoma, amyloid deposits, A cells
- MeSH terms
- Aged, Amyloid, Cytoplasmic Granules, Female, Humans, Immunohistochemistry, Islets of Langerhans, Male, Microscopy, Electron, Middle Aged, Pancreatic Neoplasms
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