ArticleThe Biochemical journal1996
Proinsulin processing in the rat insulinoma cell line INS after overexpression of the endoproteases PC2 or PC3 by recombinant adenovirus.
Article in The Biochemical journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
11 citing papers in PubMed, 44 citations in OpenAlex.
- Inside the Insulin Secretory Granule.Metabolites · 2021Review
- Defective transport of the obesity mutant PC1/3 N222D contributes to loss of function.Endocrinology · 2014Article
- A novel dual-color reporter for identifying insulin-producing beta-cells and classifying heterogeneity of insulinoma cell lines.PloS one · 2012Article
- Proinsulin maturation, misfolding, and proteotoxicity.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Improving function and survival of pancreatic islets by endogenous production of glucagon-like peptide 1 (GLP-1).Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Suppression of Pdx-1 perturbs proinsulin processing, insulin secretion and GLP-1 signalling in INS-1 cells.Diabetologia · 2005Article
- Constitutive and regulated expression of processed insulin following in vivo hepatic gene transfer.Gene therapy · 2002Article
- Insulin resistance in HIV protease inhibitor-associated diabetes.Journal of acquired immune deficiency syndromes (1999) · 1999Article
- Regulation of bone morphogenetic protein activity by pro domains and proprotein convertases.The Journal of cell biology · 1999Article
- Review
- Defective prohormone processing and altered pancreatic islet morphology in mice lacking active SPC2.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proinsulin is converted to insulin by the two endoproteases PC2 and PC3. For complete conversion to insulin, cleavage must occur at both the B-chain/C-peptide and C-peptide/A-chain junctions of proinsulin. Studies in vitro have shown the specificity of PC3 for the B-chain/C-peptide junction and that of PC2 for the C-peptide/A-chain junction. In contrast, studies in vivo have suggested that the proinsulin cleavage substrate specificity of these two endoproteases might be more complex. We have now used recombinant adenovirus to overexpress PC2 or PC3 in the rat insulinoma cell line INS. These cells convert proinsulin more slowly than primary pancreatic beta-cells, possibly reflecting their lower levels of PC3. Infection of INS cells with the corresponding recombinant adenovirus led to 5-10-fold and 20-40-fold increases in PC2 and PC3 expression respectively. Recombinant adenovirus is thus an effective tool for expressing proteins at high levels in slow-growing INS cells. Overexpression of either PC2 or PC3 in INS cells led to a striking acceleration of conversion of proinsulin to insulin and to a decreased accumulation of the conversion intermediate des-64.65-split proinsulin (cleaved only at the A-chain/C-peptide junction). There was no detectable accumulation of des-31.32-split proinsulin (cleaved only at the B-chain /C-peptide junction) after overexpression of either enzyme. Taken together, the data indicate that when expressed at high levels, both PC2 and PC3 seem to be able to cleave proinsulin at both its junctions in vivo.
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Registered trials
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