ArticleProceedings of the National Academy of Sciences of the United States of America1993
Chromostatin, a chromogranin A-derived bioactive peptide, is present in human pancreatic insulin (beta) cells.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 52 citations in OpenAlex.
- Role and function of granin proteins in diabetes mellitus.World journal of diabetes · 2021Review
- The Emerging Roles of Chromogranins and Derived Polypeptides in Atherosclerosis, Diabetes, and Coronary Heart Disease.International journal of molecular sciences · 2021Review
- Chromogranin A - unspecific neuroendocrine marker. Clinical utility and potential diagnostic pitfalls.Archives of medical science : AMS · 2016Article
- Mapping Mammalian Cell-type-specific Transcriptional Regulatory Networks Using KD-CAGE and ChIP-seq Data in the TC-YIK Cell Line.Frontiers in genetics · 2015Article
- Guanylin and functional coupling proteins in the hepatobiliary system of rat and guinea pig.Histochemistry and cell biology · 2012Article
- Pancreatic beta cells synthesize neuropeptide Y and can rapidly release peptide co-transmitters.PloS one · 2011Article
- The normal cellular prion protein (PrPc) is strongly expressed in bovine endocrine pancreas.Histochemistry and cell biology · 2006Article
- Guanylin and functional coupling proteins in the human salivary glands and gland tumors : expression, cellular localization, and target membrane domains.The American journal of pathology · 2002Article
- Tertiary hypothyroidism and hyperglycemia in mice with targeted disruption of the thyrotropin-releasing hormone gene.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
- Loss of GLUT2 glucose transporter expression in pancreatic beta cells from diabetic Chinese hamsters.Virchows Archiv : an international journal of pathology · 1996Article
- Pancreastatin secretion by pituitary adenomas and regulation of chromogranin B mRNA expression.The American journal of pathology · 1996Article
- Immunohistochemical detection of secretoneurin, a novel neuropeptide endoproteolytically processed from secretogranin II, in normal human endocrine and neuronal tissues.The Histochemical journal · 1995Article
- Analysis of the chromogranin A post-translational cleavage product pancreastatin and the prohormone convertases PC2 and PC3 in normal and neoplastic human pituitaries.The American journal of pathology · 1995Article
- Immunohistochemical Localization of Chromostatin and Pancreastatin, Chromogranin A-Derived Bioactive Peptides, in Normal and Neoplastic Neuroendocrine Tissues.Endocrine pathology · 1995Article
- Enterochromaffin cells of the digestive system: cellular source of guanylin, a guanylate cyclase-activating peptide.Proceedings of the National Academy of Sciences of the United States of America · 1994Article
- The granin protein family: markers for neuroendocrine cells and tools for the diagnosis of neuroendocrine tumors.Journal of endocrinological investigation · 1994Review
- Expression of chromogranin A and B and secretoneurin immunoreactivity in neoplastic and nonneoplastic pancreatic alpha cells.Virchows Archiv : an international journal of pathology · 1994Article
- Immunocytochemical and ultrastructural heterogeneities of normal and glibenclamide stimulated pancreatic beta cells in the rat.Virchows Archiv : an international journal of pathology · 1994Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Chromogranin A (CGA) is a secretory protein present in the adrenal medulla and in a variety of endocrine organs. This protein may serve as precursor for pancreastatin (PST) and for other biologically active peptides. Recently, chromostatin (CST), a CGA derivative, has been identified that possesses high biological activity. The cellular distribution of CST in various endocrine organs is completely unknown. Using immunohistochemistry on plastic sections, we investigated the occurrence and cellular distribution of CST, PST, and CGA in human endocrine pancreas of healthy and diseased states and in the adrenal medulla. In the normal and diabetic pancreas, CST immunoreactivity was localized exclusively in beta cells, which were mostly unreactive for PST and CGA. Both latter peptides were confined mainly to glucagon (alpha) cells. Insulinoma cells displayed strong insulin, PST, and CGA immunoreactivities, but they were faintly immunoreactive for CST or unreactive. Adrenal chromaffin cells exhibited strong immunoreactivity for CGA but lacked CST and PST immunoreactivities. Based on the peculiar distributive pattern of CST, PST, and CGA, we suggest that CGA is differentially processed in chromaffin and islet tissues and in insulinoma cells. The unique cellular localization of CST in the endocrine pancreas of normal and pathological conditions may indicate that CST is involved in beta-cell function.
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