ArticleThe Biochemical journal1994
The post-translational processing of chromogranin A in the pancreatic islet: involvement of the eukaryote subtilisin PC2.
Article in The Biochemical journal, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 68 citations in OpenAlex.
- Immunohistochemical evaluation of the post-translational processing of chromogranin A in human pituitary adenomas.Pituitary · 2000Trial
- Chromogranin A-derived peptides pancreastatin and catestatin: emerging therapeutic target for diabetes.Amino acids · 2023Review
- Review
- Chromogranin A regulates vesicle storage and mitochondrial dynamics to influence insulin secretion.Cell and tissue research · 2017Article
- Detection of vasostatin-1-specific CD8(+) T cells in non-obese diabetic mice that contribute to diabetes pathogenesis.Clinical and experimental immunology · 2016Article
- Specificity and detection of insulin-reactive CD4+ T cells in type 1 diabetes in the nonobese diabetic (NOD) mouse.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- The chromogranins: their roles in secretion from neuroendocrine cells and as markers for neuroendocrine neoplasia.Endocrine pathology · 2003Review
- Novel autocrine feedback control of catecholamine release. A discrete chromogranin a fragment is a noncompetitive nicotinic cholinergic antagonist.The Journal of clinical investigation · 1997Article
- pH-dependent processing of secretogranin II by the endopeptidase PC2 in isolated immature secretory granules.The Biochemical journal · 1997Article
- Chromogranin A processing and secretion: specific role of endogenous and exogenous prohormone convertases in the regulated secretory pathway.The Journal of clinical investigation · 1996Article
- Processing of chromogranins in chromaffin cell culture: effects of reserpine and alpha-methyl-p-tyrosine.The Biochemical journal · 1996Article
- Large variations in the proteolytic formation of a chromogranin A-derived peptide (GE-25) in neuroendocrine tissues.The Biochemical journal · 1995Article
- Differences between the catalytic properties of recombinant human PC2 and endogenous rat PC2.The Biochemical 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
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The post-translational processing of chromogranin A (CGA) and the nature of the enzyme(s) involved were investigated in rat pancreatic islet and insulinoma tissue. Pulse-chase radiolabelling experiments using sequence-specific antisera showed that the 98 kDa (determined by SDS/PAGE) precursor was processed to an N-terminal 21 kDa peptide, a C-terminal 14 kDa peptide and a 45 kDa centrally located peptide with a rapid time course (t1/2 approx. 30 min) after an initial delay of 30-60 min. The 45 kDa peptide was, in turn, converted partially into a 5 kDa peptide with pancreastatin immunoreactivity and a 3 kDa peptide with WE-14 immunoreactivity over a longer time period. Incubation of bovine CGA with rat insulinoma secretory-granule lysate produced peptides of 18, 16 and 40 kDa via intermediates of 65 and 55 kDa. N-terminal sequence analysis indicated that cleavage occurred at the conserved paired basic sites Lys114-Arg115 and Lys330-Arg331, suggesting that cleavage of the equivalent sites (Lys129-Arg130 and Lys357-Arg358) in the rat molecule produced the initial post-translational products observed in intact pancreatic beta-cells. The enzyme activity responsible for the cleavage of bovine CGA co-chromatographed on DEAE-cellulose with the type-2 proinsulin endopeptidase and with PC2 immunoreactivity. The type-1 enzyme (PC1/3) appeared inactive towards CGA. The requirement for Ca2+ ions and an acidic pH for conversion was consistent with the involvement of a member of the eukaryote subtilisin family, and the composition of the released peptides in pulse-chase and secretion studies suggested that conversion occurred in the secretory-granule compartment. The overall catalytic rate as well as the relative susceptibilities of the Lys114-Arg115 and Lys330-Arg331 sites to cleavage were affected by pH, suggesting that the ionic environment of the processing compartment may play a role in the differential processing of CGA which is evident in various neuroendocrine cells.
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