ArticleThe Biochemical journal1999
SNAP-25a and -25b isoforms are both expressed in insulin-secreting cells and can function in insulin secretion.
Article in The Biochemical journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 43 citations in OpenAlex.
- SNAP25 mutation disrupts metabolic homeostasis, steroid hormone production and central neurobehavior.Biochimica et biophysica acta. Molecular basis of disease · 2022Article
- A role for alternative splicing in circadian control of exocytosis and glucose homeostasis.Genes & development · 2020Article
- Developmental Time Course of SNAP-25 Isoforms Regulate Hippocampal Long-Term Synaptic Plasticity and Hippocampus-Dependent Learning.International journal of molecular sciences · 2020Article
- SNAP-25b-deficiency increases insulin secretion and changes spatiotemporal profile of CaScientific reports · 2017Article
- Synaptosomal Protein of 25 kDa (Snap25) Polymorphisms Associated with Glycemic Parameters in Type 2 Diabetes Patients.Journal of diabetes research · 2016Article
- Replacing SNAP-25b with SNAP-25a expression results in metabolic disease.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Synaptotagmin-7 is an asynchronous calcium sensor for synaptic transmission in neurons expressing SNAP-23.PloS one · 2014Article
- Role of the SNARE protein SNAP23 on cAMP-stimulated renin release in mouse juxtaglomerular cells.American journal of physiology. Renal physiology · 2013Article
- Localization of multidomain adaptor proteins, p140Cap and vinexin, in the pancreatic islet of a spontaneous diabetes mellitus model, Otsuka Long-Evans Tokushima Fatty rats.Medical molecular morphology · 2013Article
- Single secretory granules of live cells recruit syntaxin-1 and synaptosomal associated protein 25 (SNAP-25) in large copy numbers.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Insulin granule biogenesis, trafficking and exocytosis.Vitamins and hormones · 2009Review
- The role of the t-SNARE SNAP-25 in action potential-dependent calcium signaling and expression in GABAergic and glutamatergic neurons.BMC neuroscience · 2008Article
- The cytoplasmic domain of proEGF negatively regulates motility and elastinolytic activity in thyroid carcinoma cells.Neoplasia (New York, N.Y.) · 2008Article
- Phosphorylation of SNAP-25 at Ser187 mediates enhancement of exocytosis by a phorbol ester in INS-1 cells.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2008Article
- A dominant mutation in Snap25 causes impaired vesicle trafficking, sensorimotor gating, and ataxia in the blind-drunk mouse.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Developmentally regulated switch in alternatively spliced SNAP-25 isoforms alters facilitation of synaptic transmission.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2004Article
- Phosphorylation of SNAP-25 on serine-187 is induced by secretagogues in insulin-secreting cells, but is not correlated with insulin secretion.The Biochemical journal · 2002Article
- Lipid and cationic polymer based transduction of botulinum holotoxin, or toxin protease alone, extends the target cell range and improves the efficiency of intoxication.Toxicon : official journal of the International Society on ToxinologyArticle
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The tSNARE (the target-membrane soluble NSF-attachment protein receptor, where NSF is N-ethylmaleimide-sensitive fusion protein) synaptosomal-associated protein of 25 kDa (SNAP-25) is expressed in pancreatic B-cells and its cleavage by botulinum neurotoxin E (BoNT/E) abolishes stimulated secretion of insulin. In the nervous system, two SNAP-25 isoforms (a and b) have been described that are produced by alternative splicing. Here it is shown, using reverse transcriptase PCR, that messages for both SNAP-25 isoforms are expressed in primary pancreatic B and non-B cells as well as in insulin-secreting cell lines. After transfection, both isoforms can be detected at the plasma membrane as well as in an intracellular perinuclear region in the insulin-secreting cell line, HIT. To test for the functional role of the two isoforms in insulin secretion, mutant forms of SNAP-25a and b resistant against cleavage by BoNT/E were generated. Such mutant SNAP-25, when expressed in HIT cells, is not inactivated by BoNT/E and its ability to restore insulin secretion can thus be investigated. To obtain the toxin-resistant mutant isoforms, the sequence around the BoNT/E cleavage site (R176QIDRIM182) was changed to P176QIKRIT182. This is the sequence of the equivalent region of human SNAP-23 (P187-T194), which has been shown to be resistant to BoNT/E. The mutant SNAP-25 was resistant to BoNT/E in vitro and in vivo and both mutant isoforms were able to reconstitute insulin secretion from toxin-treated HIT cells.
Indexed as
Identifiers
10085240PMC1220140W2039987327What OpenQuestion holds
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.