ArticleCellular and molecular neurobiology1998
Protein kinase C controls the priming step of regulated exocytosis in adrenal chromaffin cells.
Article in Cellular and molecular neurobiology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed, 19 citations in OpenAlex.
- The Role of Calmodulin vs. Synaptotagmin in Exocytosis.Frontiers in molecular neuroscience · 2021Review
- Modulation of neurotransmitter release by the second messenger-activated protein kinases: implications for presynaptic plasticity.Pharmacology & therapeutics · 2005Review
- Protein kinase C-dependent phosphorylation of synaptosome-associated protein of 25 kDa at Ser187 potentiates vesicle recruitment.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2002Article
- Involvement of protein kinase C in the presynaptic nicotinic modulation of [(3)H]-dopamine release from rat striatal synaptosomes..British journal of pharmacology · 2001Article
- Mitochondria regulate the Ca(2+)-exocytosis relationship of bovine adrenal chromaffin cells.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1999Article
Corrections and comments
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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
1. To investigate the mechanism whereby protein kinase C enhances secretory function in adrenal chromaffin cells, we examined the effects of 12-O-tetradecanoylphorbor-13-acetate (TPA) on Ca(2+)-induced catecholamine release from digitonin-permeabilized cells, resolving the release into a MgATP-dependent priming step and a MgATP-independent Ca(2+)-triggered step. Treatment with TPA selectively potentiated the priming activity of MgATP, with little increase in the MgATP-independent release. The potentiation by TPA of the MgATP-dependent priming was blocked by [Ser25]protein kinase C(19-31), a specific substrate of protein kinase C. Gö 6976, an inhibitor selective for protein kinase C alpha and beta isoforms, also blocked the potentiation by TPA. These results suggest that activation of protein kinase C, probably the alpha isoform, potentiates the MgATP-dependent priming step. 2. The antibody raised against GAP-43, a known substrate of protein kinase C, also potentiated the MgATP-dependent priming. The effect of TPA and that of the anti-GAP-43 antibody were not additive. Calmodulin, which binds to GAP-43 and inhibits its phosphorylation by protein kinase C, abolished the effect of TPA. Thus, the present results suggest that protein kinase C potentiates MgATP-dependent priming, at least in part, through phosphorylation of GAP-43.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.