Characterization of SNAP-25 gene from marine teleostean, Lateolabrax japonicus

Kui Chen; Xiaohang Huang; Yingmei Chai; Herbert Y. Gaisano

doi:10.1007/s00343-007-0378-0

Your Location：

Home >

Browse articles >

Characterization of SNAP-25 gene from marine teleostean, Lateolabrax japonicus

Updated：2023-05-16

- Characterization of SNAP-25 gene from marine teleostean, Lateolabrax japonicus
- Journal of Oceanology and Limnology Vol. 25, Issue 4, Pages: 378-385(2007)
- Affiliations：
  
  1. Institute of Oceanology Chinese Academy of Sciences
  2. The First Institute of Oceanography State Oceanic Administration
  3. Graduate University Chinese Academy of Sciences
  4. Department of Physiology University of Toronto
- Author bio：
- Funds：
- DOI：10.1007/s00343-007-0378-0
  CLC：
- Published：2007
- Accepted：
Scan QR Code
Chen, K., Huang, X., Chai, Y. et al. Characterization of SNAP-25 gene from marine teleostean, Lateolabrax japonicus, ., Chin. J. Ocean. Limnol. 25, 378–385 (2007). https://doi.org/10.1007/s00343-007-0378-0
DOI：

Chen, K., Huang, X., Chai, Y. et al. Characterization of SNAP-25 gene from marine teleostean, Lateolabrax japonicus, ., Chin. J. Ocean. Limnol. 25, 378–385 (2007). https://doi.org/10.1007/s00343-007-0378-0 DOI：

摘要

Abstract

The t-SNARE protein SNAP-25 (synaptosome-associated protein of 25 kDa) plays an essential role in regulating fusion between the vesicle and plasma membranes during exocytosis. To clone and characterize SNAP-25 gene

the first step in the functional study of SNARE proteins in marine teleostean

was to obtain the cDNA of sea perch SNAP-25 (SPsn25) by RT-PCR and RACE-PCR amplification of a Japanese sea perch. The full-length cDNA of 831bp contains a CDS of 615 bp

coding 204 amino acid residues

and a 5 UTR of 219bp. Bioinformatic analysis revealed that SPsn25 corresponds with SNAP-25a isoform and shares 91.1% identity with SNAP-25a of a goldfish and a zebrafish. The SPsn25 expression in both mRNA and protein levels in the Japanese sea perch had been identified through semi-quantitative RT-PCR and Western Blot assay. Together

these data again confirmed the nerve tissue specificity of the fish SNAP-25 gene expression.

关键词

Keywords

references

Bark, I. C., 1993. Structure of the chicken gene for SNAP-25 reveals duplicated exons encoding distinct isoforms of the protein. J. Mol. Biol. 233: 67–76.

Bark, I. C., K. M. Hahn, A. E. Ryabinin and M. Wilson, 1995. Differential expression of SNAP-25 protein isoforms during divergent vesicle fusion events neural development. Proc. Natl. Acad. Sci. USA: Neurobiol. 92: 1 510–1 514.

Bracher, A., J. Kadlec, H. Betz and W. Weissenhorn, 2002 X-ray structure of a neuronal complexin-SNARE complex from squid. J. Biol. Chem. 277: 26 517–26 523.

Chen, Y. A. and R. H. Scheller, 2001. SNARE-mediated membrane fusion. Nature: Mol. Cell Biol. 2: 98–106.

Fasshauer, D., R. B. Sutton, A. T. Brunger and R. Jahn, 1998. Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q-and R-SNAREs. Proc. Natl. Acad. Sci. USA: Neurobiol. 95: 15 781–15 786.

Fasshauer, D., A W. W. Antonin, M. Margittai, S. Pabst and R. Jahn, 1999. Mixed and non-cognate SNARE complexes-characterization of assembly and biophysical properties. J. Biol. Chem. 274: 15 440–15 446.

Gerst, J. E., 1999. Review: SNAREs and SNARE regulators in membrane fusion and exocytosis. Cell. Mol. Life Sci. 55: 707–734.

Hall, A. V., H. Antoniou, Y. Wang, A. H. Cheng, A. M. Arbus, S. L. Olson and W. C. Liu, 1994. Structural Organization of the Human Neuronal Nitric Oxide Synthase Gene (NOS1). J. Biol. Chem. 269: 33 082–33 090.

Hodel, A., 1998. Molecules in Focus SNAP-25. Inter. J. Biochem Cell Biol. 30: 1 069–1 073.

Huang, X. H., L. Sheu, Y. Tamori, W. S. Trimble and H. Y. Gaisano, 2001. Cholecystokinin-regulated exocytosis in rat pancreatic acinar cells is inhibited by a C-terminus truncated mutant of SNAP-23. Pancreas 23: 125–133.

Nagy, G., I. Milosevic, D. Fasshauer, E. M. Müller, Bert L. de Groot, T. Lang, M. C. Wilson and J. B. Sørensen, 2005. Alternative Splicing of SNAP-25 Regulates Secretion through Nonconservative Substitutions in the SNARE Domain. Molecular Biology of the Cell 16: 5 675–5 685.

Oyler, G. A., G. A. Higgins, R. A. Hart, E. Battenberg, M. Billingsley, F. E. Bloom and M. C. Wilson, 1989. The identification of a novel synaptosomal-associated protein, SNAP-25, differentially expressed by neuronal subpopulations. J. Cell Biol. 109: 3 039–3 052.

Peterson, G. L., 1977. A simplification of the protein assay method of lowry et al. which is more generally applicable. Anal. Chem. 83: 346–356.

Risinger, C., E. Salaneck, C. Soderberg, M. Gates, J. H. Postlethwait and D. Larhammar, 1998. Cloning of two loci for synapse protein Snap25 in zebrafish: comparison of paralogous linkage groups suggests loss of one locus in the mammalian lineage. Journal of Neuroscience Research 54: 563–573.

Roth, D. and R. D. Burgoyne, 1994. SNAP-25 is present in a SNARE complex in adrenal chromaffin cells. FEBS Lett. 351: 207–210.

Sutton, R. B., D. Fasshauer, R. Jahn and A. T. Brunger, 1998. Crystal structure of a SNARE complex involved in synaptic exocytosisat 2.4A° resolution. Nature 395: 547–353.

Söllner, T., M. K. Bennett, S. W. Whiteheart, R. H. Scheller and J. E. Rothman, 1993a. A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation and fusion. Cell 75: 409–418.

Söllner, T., S. W. Whiteheart, M. Brunner, H. Erdjument-Bromage, S. Geromanos, P. Tempst and J. E. Rothman, 1993b. SNAP receptors implicated in vesicle targeting and fusion. Nature 362: 318–324.

Sørensen, J. B., G. Nagy, F. Varoqueaux, R. B. Nehring, N. Brose, M. C. Wilson and E. Neher, 2003. Differential control of the releasable vesicle pools by SNAP-25 splice variants and SNAP-23. Cell 114:75–86.

Trimble, W. S., D. M. Cowan and R. H. Scheller, 1988. VAMP-1: a synaptic vesicle-associated integral membrane protein. Proc. Nat. Acad. Sci. USA 85: 4 538–4 542.

Wang, Y., D. C. Newton, G. B. Robb, C. L. Kau, T. L. Miller, A. H. Cheung and A. V. Hall, 1999. RNA diversity has profound effects on the translation of neuronal nitric oxide synthase. Proc. Natl. Acad. Sci. USA: Neurobiol. 96: 12 150–12 155.

Wang, J. Y., S. G. Zhu and C. F. Xu, 2002. Biochemistry. Higher Educational Press, Beijing, China, p. 57–59. (in Chinese)

Wheeler, M., L. Sheu, M. Ghai, A. Bouquillon, G. Grondin, U. Weller and A. R. Beaudoin, 1996. Characterisation of SNARE protein expression in beta cell lines and pancreatic islets. Endocrinol. 137: 1 340–1 348.

Woodman, P. G., 1997. Review: The roles of NSF, SNAPs and SNAREs during membrane fusion. Biochm. Biophy. Acta. 1 357: 155–172.

Yano, T., 1996. The nonspecific immune system: humoral defense. In: Iwama G. and Nakanishi T. eds. The Fish Immune System: Organism Pathogen and Environment. Academic Press (San Diego), p.105–157.

Views

Downloads

CSCD

Alert me when the article has been cited

Submit

Tools

Publicity Resources

Relation of body weight and food consumption to metabolic rate of juvenile Japanese sea bass,Lateolabrax japonicus

Analysis Procedure and Numerical Simulation of Failure Probability of Turbine Disk Caused by Defects

Investigation on Interaction Mechanism Between Rim Sealing Flow and Mainstream Flow in High-Pressure Turbine

Performance Modelling of Geared Contra-RotatingPropfan Engine

Method of Point Selection for Fitting Ignition Probability Curve Based on Maximum Likelihood Estimation

Related Author

Xian Wei-wei

Zhu Xin-hua

Related Institution

No data

Address：Editorial Office of JOL, 88 Haijun Rd. Qingdao, 266000, China
Tel：+86-532-82898754 Email：jol@qdio.ac.cn
Technical support is provided by Beijing Founder electronics co., LTD 京ICP备09064830号-19 京公网安备11010802024621
It is recommended to read the content of this site in Chrome&IE9+. Please switch to extreme mode in browser 360.
Cookies We use cookies to help provide and enhance our service and tailor content. By continuing, you agree to the use of cookies.

⁰