ArticleThe Biochemical journal1989
Effects of protein kinase C activation on the regulation of the stimulus-secretion coupling in pancreatic beta-cells.
Article in The Biochemical journal, 1989. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 82 citations in OpenAlex.
- Diacylglycerol-evoked activation of PKC and PKD isoforms in regulation of glucose and lipid metabolism: a review.Lipids in health and disease · 2020Review
- Regulation of insulin exocytosis by calcium-dependent protein kinase C in beta cells.Cell calcium · 2017Review
- Autocrine Signaling Underlies Fast Repetitive Plasma Membrane Translocation of Conventional and Novel Protein Kinase C Isoforms in β Cells.The Journal of biological chemistry · 2016Article
- Protein kinase C function in muscle, liver, and beta-cells and its therapeutic implications for type 2 diabetes.Diabetes · 2008Review
- Ca2+-secretion coupling is impaired in diabetic Goto Kakizaki rats.The Journal of general physiology · 2007Article
- Phorbol ester impairs electrical excitation of rat pancreatic beta-cells through PKC-independent activation of KATP channels.BMC pharmacology · 2001Article
- CaM kinase II-dependent mobilization of secretory granules underlies acetylcholine-induced stimulation of exocytosis in mouse pancreatic B-cells.The Journal of physiology · 1999Article
- Insulin-like growth factor II signaling through the insulin-like growth factor II/mannose-6-phosphate receptor promotes exocytosis in insulin-secreting cells.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
- The harmony of the spheres: inducible nitric oxide synthase and related genes in pancreatic beta cells.Diabetologia · 1996Review
- Dissociation between changes in cytoplasmic free Ca2+ concentration and insulin secretion as evidenced from measurements in mouse single pancreatic islets.Proceedings of the National Academy of Sciences of the United States of America · 1995Article
- Muscarinic stimulation exerts both stimulatory and inhibitory effects on the concentration of cytoplasmic Ca2+ in the electrically excitable pancreatic B-cell.The Biochemical journal · 1995Article
- Insulin-like growth factor-II gene expression in a rat insulin-producing beta-cell line (INS-1) is regulated by glucose.Diabetologia · 1995Article
- Inhibition of glucose-stimulated insulin secretion by Ro 31-8220, a protein kinase C inhibitor.Endocrine · 1995Article
- Protein phosphorylation and beta-cell function.Diabetologia · 1994Review
- Activation of protein kinases and inhibition of protein phosphatases play a central role in the regulation of exocytosis in mouse pancreatic beta cells.Proceedings of the National Academy of Sciences of the United States of America · 1994Article
- Influence of staurosporine on glucose-mediated and glucose-conditioned insulin secretion.The Biochemical journal · 1991Article
- Effects of the phorbol ester phorbol 12-myristate 13-acetate (PMA) on islet-cell responsiveness.The Biochemical journal · 1991Article
- Potentiation of stimulus-induced insulin secretion in protein kinase C-deficient RINm5F cells.The Biochemical journal · 1990Article
- Glucose-induced translocation of protein kinase C in rat pancreatic islets.Proceedings of the National Academy of Sciences of the United States of America · 1990Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Effects of protein kinase C (PKC) activation on the insulin-secretory process were investigated, by using beta-cell-rich suspensions obtained from pancreatic islets of obese-hyperglycaemic mice. The phorbol ester 12-O-tetradecanoylphorbol 13-acetate (TPA), which is known to activate PKC directly, the muscarinic-receptor agonist carbamoylcholine and high glucose concentration enhanced the phosphorylation of a specific 80 kDa PKC substrate in the beta-cells. At a non-stimulatory glucose concentration, 10 nM-TPA increased insulin release, although there were no changes in either the cytoplasmic free Ca2+ concentration ([Ca2+]i) or membrane potential, as measured with the fluorescent indicators quin-2 and bisoxonol respectively. At a stimulatory glucose concentration TPA caused a lowering in [Ca2+]i, whereas membrane potential was unaffected. Despite the decrease in [Ca2+]i, there was a large stimulation of insulin release. Addition of TPA lowered [Ca2+]i also in beta-cells stimulated by tolbutamide or high K+, although to a lesser extent than in those stimulated by glucose. There was no effect of TPA on either Ca2+ buffering or the ability of Ins(1,4,5)P3 to release Ca2+ in permeabilized beta-cells. However, the phorbol ester inhibited the rise in [Ca2+]i in response to carbamoylcholine, which stimulates the formation of InsP3, in intact beta-cells. Down-regulation of PKC influenced neither glucose-induced insulin release nor the increase in [Ca2+]i. Hence, although PKC activation is of no major importance in glucose-stimulated insulin release, this enzyme can serve as a modulator of the glucose-induced insulin-secretory response. Such a modulation involves mechanisms promoting both amplification of the secretory response and lowering of [Ca2+]i.
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