Beta-synuclein
| SNCB | |||||||||||||||||||||||||||||||||||||||||||||||||||
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| Aliases | SNCB, entrez:6620, synuclein beta | ||||||||||||||||||||||||||||||||||||||||||||||||||
| External IDs | OMIM: 602569; MGI: 1889011; HomoloGene: 2320; GeneCards: SNCB; OMA:SNCB - orthologs | ||||||||||||||||||||||||||||||||||||||||||||||||||
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Beta-synuclein is a protein that in humans is encoded by the SNCB gene.[5][6][7]
The protein encoded by this gene is highly homologous to alpha-synuclein. These proteins are abundantly expressed in the brain and putatively inhibit phospholipase D2 selectively. The encoded protein, which may play a role in neuronal plasticity, is abundant in neurofibrillary lesions of patients with Alzheimer's disease. This protein has been shown to be highly expressed in the substantia nigra of the brain, a region of neuronal degeneration in patients with Parkinson's disease; however, no direct relation to Parkinson's disease has been established. Two transcript variants encoding the same protein have been found for this gene.[7]
Beta-synuclein is a synuclein protein found primarily in brain tissue and is seen mainly in presynaptic terminals. Beta-synuclein is predominantly expressed in the neocortex, hippocampus, striatum, thalamus, and cerebellum. It is not found in Lewy bodies, but it is associated with hippocampal pathology in PD and DLB.[8]
Beta-synuclein is suggested to be an inhibitor of alpha-synuclein aggregation, which occurs in neurodegenerative diseases such as Parkinson's disease. Thus, beta-synuclein may protect the central nervous system from the neurotoxic effects of alpha-synuclein and provide a novel treatment of neurodegenerative disorders.[9][10]
See also
[edit]References
[edit]- 1 2 3 GRCh38: Ensembl release 89: ENSG00000074317 – Ensembl, May 2017
- 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000034891 – Ensembl, May 2017
- ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ↑ Spillantini MG, Divane A, Goedert M (November 1995). "Assignment of human alpha-synuclein (SNCA) and beta-synuclein (SNCB) genes to chromosomes 4q21 and 5q35". Genomics. 27 (2): 379–381. doi:10.1006/geno.1995.1063. PMID 7558013.
- ↑ Lavedan C, Leroy E, Torres R, Dehejia A, Dutra A, Buchholtz S, et al. (January 1999). "Genomic organization and expression of the human beta-synuclein gene (SNCB)". Genomics. 54 (1): 173–175. doi:10.1006/geno.1998.5556. PMID 9806846.
- 1 2 "Entrez Gene: SNCB synuclein, beta".
- ↑ George JM (2002). "The synucleins". Genome Biology. 3 (1) REVIEWS3002. doi:10.1186/gb-2001-3-1-reviews3002. PMC 150459. PMID 11806835.
- ↑ Hashimoto M, Bar-On P, Ho G, Takenouchi T, Rockenstein E, Crews L, et al. (May 2004). "Beta-synuclein regulates Akt activity in neuronal cells. A possible mechanism for neuroprotection in Parkinson's disease". The Journal of Biological Chemistry. 279 (22): 23622–23629. doi:10.1074/jbc.M313784200. PMID 15026413.
- ↑ Hashimoto M, Rockenstein E, Mante M, Mallory M, Masliah E (October 2001). "beta-Synuclein inhibits alpha-synuclein aggregation: a possible role as an anti-parkinsonian factor". Neuron. 32 (2): 213–223. doi:10.1016/S0896-6273(01)00462-7. PMID 11683992. S2CID 14766899.
Further reading
[edit]- Jakes R, Spillantini MG, Goedert M (1994). "Identification of two distinct synucleins from human brain". FEBS Letters. 345 (1): 27–32. Bibcode:1994FEBSL.345...27J. doi:10.1016/0014-5793(94)00395-5. PMID 8194594. S2CID 36840279.
- Jensen PH, Hojrup P, Hager H, Nielsen MS, Jacobsen L, Olesen OF, et al. (April 1997). "Binding of Abeta to alpha- and beta-synucleins: identification of segments in alpha-synuclein/NAC precursor that bind Abeta and NAC". The Biochemical Journal. 323 ( Pt 2) (Pt 2): 539–546. doi:10.1042/bj3230539. PMC 1218353. PMID 9163350.
- Pronin AN, Morris AJ, Surguchov A, Benovic JL (2000). "Synucleins are a novel class of substrates for G protein-coupled receptor kinases". The Journal of Biological Chemistry. 275 (34): 26515–26522. doi:10.1074/jbc.M003542200. PMID 10852916.
- Rockenstein E, Hansen LA, Mallory M, Trojanowski JQ, Galasko D, Masliah E (September 2001). "Altered expression of the synuclein family mRNA in Lewy body and Alzheimer's disease". Brain Research. 914 (1–2): 48–56. doi:10.1016/S0006-8993(01)02772-X. PMID 11578596. S2CID 35448948.
- Tanji K, Mori F, Nakajo S, Imaizumi T, Yoshida H, Hirabayashi T, et al. (September 2001). "Expression of beta-synuclein in normal human astrocytes". NeuroReport. 12 (13): 2845–2848. doi:10.1097/00001756-200109170-00018. PMID 11588588. S2CID 84671534.
- Uversky VN, Li J, Souillac P, Millett IS, Doniach S, Jakes R, et al. (April 2002). "Biophysical properties of the synucleins and their propensities to fibrillate: inhibition of alpha-synuclein assembly by beta- and gamma-synucleins". The Journal of Biological Chemistry. 277 (14): 11970–11978. doi:10.1074/jbc.M109541200. PMID 11812782.
- Ihara M, Tomimoto H, Kitayama H, Morioka Y, Akiguchi I, Shibasaki H, et al. (June 2003). "Association of the cytoskeletal GTP-binding protein Sept4/H5 with cytoplasmic inclusions found in Parkinson's disease and other synucleinopathies". The Journal of Biological Chemistry. 278 (26): 24095–24102. doi:10.1074/jbc.M301352200. PMID 12695511.
- Fung KM, Rorke LB, Giasson B, Lee VM, Trojanowski JQ (August 2003). "Expression of alpha-, beta-, and gamma-synuclein in glial tumors and medulloblastomas". Acta Neuropathologica. 106 (2): 167–175. doi:10.1007/s00401-003-0718-x. PMID 12783249. S2CID 39712533.
- da Costa CA, Masliah E, Checler F (2003). "Beta-synuclein displays an antiapoptotic p53-dependent phenotype and protects neurons from 6-hydroxydopamine-induced caspase 3 activation: cross-talk with alpha-synuclein and implication for Parkinson's disease". The Journal of Biological Chemistry. 278 (39): 37330–37335. doi:10.1074/jbc.M306083200. PMID 12867415.
- Ohtake H, Limprasert P, Fan Y, Onodera O, Kakita A, Takahashi H, et al. (September 2004). "Beta-synuclein gene alterations in dementia with Lewy bodies". Neurology. 63 (5): 805–811. doi:10.1212/01.wnl.0000139870.14385.3c. PMC 1808539. PMID 15365127.
- Snyder H, Mensah K, Hsu C, Hashimoto M, Surgucheva IG, Festoff B, et al. (March 2005). "beta-Synuclein reduces proteasomal inhibition by alpha-synuclein but not gamma-synuclein". The Journal of Biological Chemistry. 280 (9): 7562–7569. doi:10.1074/jbc.M412887200. PMID 15591046.
- Sung YH, Eliezer D (2006). "Secondary structure and dynamics of micelle bound β- and γ-synuclein". Protein Science. 15 (5): 1162–1174. doi:10.1110/ps.051803606. PMC 2242515. PMID 16597821.
- Fan Y, Limprasert P, Murray IV, Smith AC, Lee VM, Trojanowski JQ, et al. (October 2006). "Beta-synuclein modulates alpha-synuclein neurotoxicity by reducing alpha-synuclein protein expression". Human Molecular Genetics. 15 (20): 3002–3011. doi:10.1093/hmg/ddl242. PMID 16959793.
- Myslinski E, Gérard MA, Krol A, Carbon P (2007). "A genome scale location analysis of human Staf/ZNF143-binding sites suggests a widespread role for human Staf/ZNF143 in mammalian promoters". The Journal of Biological Chemistry. 281 (52): 39953–39962. doi:10.1074/jbc.M608507200. PMID 17092945.
- Sung YH, Eliezer D (2007). "Residual structure, backbone dynamics, and interactions within the synuclein family". Journal of Molecular Biology. 372 (3): 689–707. doi:10.1016/j.jmb.2007.07.008. PMC 2094134. PMID 17681534.
External links
[edit]- Human SNCB genome location and SNCB gene details page in the UCSC Genome Browser.