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SNAP-23 is not cleaved by botulinum neurotoxin E and can replace SNAP-25 in the process of insulin secretion

Berger, A.
Niemann, H.
Weller, U.
Roche, P. A.
Klip, A.
Trimble, W. S.
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Published in Journal of Biological Chemistry. 1997, vol. 272, no. 52, p. 33023-33027
Abstract The synaptosomal-associated protein of 25 kDa (SNAP-25) is expressed in neurons and endocrine cells. It has been shown to play an important role in the release mechanism of neurotransmitters and peptide hormones, including insulin. Thus, when insulin-secreting cells are permeabilized and treated with botulinum neurotoxin E (BoNT/E), SNAP-25 is hydrolyzed, and insulin secretion is inhibited. Recently SNAP-23, a more generally expressed isoform of SNAP-25, has been described. The functional role of SNAP-23 has not been investigated to date. It is now shown that SNAP-23 is resistant to cleavage by BoNT/E. It was therefore possible to test whether transfection of HIT (transformed pancreatic B-) cells with SNAP-23 reconstitutes insulin release from BoNT/E treated cells, in which SNAP-25 is inactivated by the toxin. The results show that SNAP-23 is able to replace SNAP-25 when it is overexpressed. While these results demonstrate that SNAP-23 is a functional homologue of SNAP-25, able to function in regulated exocytosis, they indicate that SNAP-23 may be inefficient in this process. This suggests that both isoforms may have their own specific binding partners and discrete, albeit mechanistically similar, functional roles within the cell.
Keywords AnimalsBotulinum Toxins/ metabolismCarrier Proteins/genetics/ metabolismCricetinaeFluorescent Antibody Technique, IndirectInsulin/ secretionMembrane ProteinsNerve Tissue Proteins/genetics/ metabolismQb-SNARE ProteinsQc-SNARE ProteinsSynaptosomal-Associated Protein 25TransfectionTumor Cells, Cultured
PMID: 9407084
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Other version: http://www.jbc.org/content/272/52/33023.full.pdf
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SADOUL, Karin et al. SNAP-23 is not cleaved by botulinum neurotoxin E and can replace SNAP-25 in the process of insulin secretion. In: Journal of Biological Chemistry, 1997, vol. 272, n° 52, p. 33023-33027. https://archive-ouverte.unige.ch/unige:9008

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Deposited on : 2010-07-12

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