ArticleThe Biochemical journal1996
Inhibition of insulin release by synthetic peptides shows that the H3 region at the C-terminal domain of syntaxin-1 is crucial for Ca(2+)- but not for guanosine 5'-[gamma-thio]triphosphate-induced secretion.
Article in The Biochemical journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 38 citations in OpenAlex.
- SNARE Modulators and SNARE Mimetic Peptides.Biomolecules · 2022Review
- Pancreatic islet cells: a model for calcium-dependent peptide release.HFSP journal · 2010Article
- Identification of SNARE complex modulators that inhibit exocytosis from an alpha-helix-constrained combinatorial library.The Biochemical journal · 2003Article
- Insulin granule dynamics in pancreatic beta cells.Diabetologia · 2003Review
- Effects of calcium buffering on glucose-induced insulin release in mouse pancreatic islets: an approximation to the calcium sensor.The Journal of physiology · 1999Article
- Syntaxin 1 interacts with the L(D) subtype of voltage-gated Ca(2+) channels in pancreatic beta cells.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
- The stimulatory action of tolbutamide on Ca2+-dependent exocytosis in pancreatic beta cells is mediated by a 65-kDa mdr-like P-glycoprotein.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
- SNAP-25a and -25b isoforms are both expressed in insulin-secreting cells and can function in insulin secretion.The Biochemical journal · 1999Article
- Cysteine string protein (CSP) is an insulin secretory granule-associated protein regulating beta-cell exocytosis.The EMBO journal · 1998Article
- The first C2 domain of synaptotagmin is required for exocytosis of insulin from pancreatic beta-cells: action of synaptotagmin at low micromolar calcium.The EMBO journal · 1997Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Recently, we have described the presence and possible role of syntaxin in pancreatic beta-cells by using monoclonal antibodies [F. Martin, F. Moya, L. M. Gutierrez, J.A. Reig, B. Soria (1995) Diabetologia 38, 860-863]. In order to characterize further the importance of specific domains of this protein, the functional role of a particular region of the syntaxin-1 molecule has now been investigated by using two synthetic peptides, SynA and SynB, corresponding to two portions of the H3 region at the C-terminal domain of the protein, residues 229-251 and 197-219 respectively. Functional experiments carried out in permeabilized pancreatic beta-cells demonstrate that these peptides inhibit Ca(2+)-dependent insulin release in a dose-dependent manner. This effect is specific because peptides of the same composition but random sequence do not show the same effect. In contrast with this inhibitory effect on Ca(2+)-induced secretion, both peptides increase basal release. However, under the same conditions, SynA and SynB do not affect guanosine 5'-[gamma-thio]triphosphate-induced insulin release. These results demonstrate that specific portions of the H3 region of syntaxin-1 are involved in critical protein-protein interactions specifically during Ca(2+)-induced insulin secretion.
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