ArticleThe Biochemical journal1994
Levels of the conversion endoproteases PC1 (PC3) and PC2 distinguish between insulin-producing pancreatic islet beta cells and non-beta cells.
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 18 papers.
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Who cites it
18 citing papers in PubMed, 51 citations in OpenAlex.
- Inside the Insulin Secretory Granule.Metabolites · 2021Review
- Heterogeneous Expression of Proinsulin Processing Enzymes in Beta Cells of Non-diabetic and Type 2 Diabetic Humans.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2019Article
- Compensatory Islet Response to Insulin Resistance Revealed by Quantitative Proteomics.Journal of proteome research · 2015Article
- DsAAV8-mediated expression of glucagon-like peptide-1 in pancreatic beta-cells ameliorates streptozotocin-induced diabetes.Gene therapy · 2010Article
- Transcriptional analysis of intracytoplasmically stained, FACS-purified cells by high-throughput, quantitative nuclease protection.Nature biotechnology · 2009Article
- Immunocytochemical localization of prohormone convertase 1/3 and 2 in gastrointestinal carcinoids.Endocrine pathology · 2001Article
- Regulation of pancreatic PC1 and PC2 associated with increased glucagon-like peptide 1 in diabetic rats.The Journal of clinical investigation · 2000Article
- Immunocytochemical Localization of Prohormone Convertase 1/3 and 2 in Thyroid C-Cells and Medullary Thyroid Carcinomas.Endocrine pathology · 2000Article
- Insulin resistance in HIV protease inhibitor-associated diabetes.Journal of acquired immune deficiency syndromes (1999) · 1999Article
- Regulation of human prohormone convertase 2 promoter activity by the transcription factor EGR-1.The Biochemical journal · 1997Article
- Proinsulin processing in the rat insulinoma cell line INS after overexpression of the endoproteases PC2 or PC3 by recombinant adenovirus.The Biochemical journal · 1996Article
- Specific co-ordinated regulation of PC3 and PC2 gene expression with that of preproinsulin in insulin-producing beta TC3 cells.The Biochemical journal · 1996Article
- Heterologous processing of rat prosomatostatin to somatostatin-14 by PC2: requirement for secretory cell but not the secretion granule.The Biochemical journal · 1995Article
- Sequence requirements for proinsulin processing at the B-chain/C-peptide junction.The Biochemical journal · 1995Article
- Increased secretory demand rather than a defect in the proinsulin conversion mechanism causes hyperproinsulinemia in a glucose-infusion rat model of non-insulin-dependent diabetes mellitus.The Journal of clinical investigation · 1995Article
- pH-independent and -dependent cleavage of proinsulin in the same secretory vesicle.The Journal of cell biology · 1994Article
- Review
- Intra-islet glucagon-like peptide 1.Journal of diabetes and its complicationsReview
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
PC1 (PC3) and PC2, members of the mammalian family of proprotein convertases homologous to the yeast Kex2 gene product, are both expressed in pancreatic islets of Langerhans. Recent studies have suggested that PC1 and PC2 are responsible for the conversion of proinsulin to insulin and connecting peptide (C-peptide) in the islet beta cells. However, the insulin-secreting beta cells are not the only cells present in these complex micro-organs, prompting us to evaluate the expression of PC1 and PC2 in islet beta and non-beta cells. Rat islet cells were sorted by autofluorescence-activated flow cytometry to separate beta cells from non-beta cells, and conversion endoprotease levels were analysed by Western blotting. The immunolabel ratio of PC1/PC2 in beta cells was 2.6. Non-beta cells displayed much lower levels of PC1 than beta cells, but twice as much PC2 (PC1/PC2 = 0.05). Post-translational modification of the convertases themselves was found to differ between the cell types. In particular, a 75 kDa precursor form of PC2 (pro-PC2) was found to accumulate in beta cells, whereas only the fully processed 67 kDa form was detected in the non-beta cells. Finally, the quantification of PC1 and PC2 and their precursor forms in transformed cells (insulin-producing beta-TC and glucagon-producing alpha-TC) showed that transformation appeared to be accompanied by unusually high levels of the precursors.
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