Literature DB >> 7612869

Brefeldin A and a synthetic peptide to ADP-ribosylation factor (ARF) inhibit regulated exocytosis in melanotrophs.

M Rupnik1, G J Law, A J Northrop, W T Mason, R Zorec.   

Abstract

We investigated the role of ADP-ribosylation factor (ARF) in regulated exocytosis in patch-clamped rat melanotrophs. Addition of brefeldin A (BFA) to inhibit activation of endogenous ARF protein was found to attenuate regulated secretory activity monitored as changes in membrane capacitance (Cm). A synthetic peptide to amino acids 46-61 of ARF (P-14) was also found to inhibit Ca(2+)-induced secretory activity in these cells. This inhibition was not apparent with a scrambled amino acid sequence of ARF-P14 peptide. This paper provides the first patch-clamp study to suggest that the small GTP-binding protein ARF is required to trigger release of secretory granules from rat pituitary melanotrophs.

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Year:  1995        PMID: 7612869     DOI: 10.1097/00001756-199504190-00007

Source DB:  PubMed          Journal:  Neuroreport        ISSN: 0959-4965            Impact factor:   1.837


  1 in total

1.  Potentiation of Fcepsilon receptor I-activated Ca(2+) current (I(CRAC)) by cholera toxin: possible mediation by ADP ribosylation factor.

Authors:  M A McCloskey; L Zhang
Journal:  J Cell Biol       Date:  2000-01-10       Impact factor: 10.539

  1 in total

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