ArticleThe Journal of cell biology1996
VAMP/synaptobrevin isoforms 1 and 2 are widely and differentially expressed in nonneuronal tissues.
Article in The Journal of cell biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 144 citations in OpenAlex.
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- Vesicular transport system in myotubes: ultrastructural study and signposting with vesicle-associated membrane proteins.Histochemistry and cell biology · 2014Article
- SNARE zippering and synaptic strength.PloS one · 2014Article
- Characterization of VAMP-2 in the lung: implication in lung surfactant secretion.Cell biology international · 2012Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
VAMP/synaptobrevin is part of the synaptic vesicle docking and fusion complex and plays a central role in neuroexocytosis. Two VAMP (vesicle-associated membrane protein) isoforms are expressed in the nervous system and are differently distributed among the specialized parts of the tissue. Here, VAMP-1 and -2 are shown to be present in all rat tissues tested, including kidney, adrenal gland, liver, pancreas, thyroid, heart, and smooth muscle. The two isoforms are differentially expressed in various tissues and their level may depend on differentiation. VAMP-1 is restricted to exocrine pancreas and to kidney tubular cells, whereas VAMP-2 is the predominant isoform present in Langerhans islets and in glomerular cells. Both isoforms show a patchy vesicular intracellular distribution in confocal microscopy. The present results provide evidence for the importance of neuronal VAMP proteins in the physiology of all cells.
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