αII-スペクトリン
(sptan1 から転送)
出典: フリー百科事典『ウィキペディア（Wikipedia）』 (2024/05/07 13:52 UTC 版)
αII-スペクトリン（αII-spectrin）、スペクトリンα2（spectrin α2）またはSPTAN1（spectrin alpha, non-erythrocytic 1）は、ヒトではSPTAN1遺伝子にコードされるタンパク質である[5][6][7]。αII-スペクトリンはさまざまな組織で発現しており、心筋のZ線構造、コスタメア、筋鞘で高度に発現している。αII-スペクトリンの変異は早期乳児てんかん性脳症（EIEE、発達性てんかん性脳症（DEE）、大田原症候群）5と関係しており、αII-スペクトリンはギラン・バレー症候群と乳児の先天性心疾患のバイオマーカーとして有用である可能性がある。
- ^ a b c GRCh38: Ensembl release 89: ENSG00000197694 - Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000057738 - Ensembl, May 2017
- ^ Human PubMed Reference:
- ^ Mouse PubMed Reference:
- ^ a b “Comparison of nonerythroid alpha-spectrin genes reveals strict homology among diverse species”. Mol Cell Biol 8 (1): 1–9. (February 1988). doi:10.1128/MCB.8.1.1. PMC 363070. PMID 3336352.
- ^ Leto, T. L.; Fortugno-Erikson, D.; Barton, D.; Yang-Feng, T. L.; Francke, U.; Harris, A. S.; Morrow, J. S.; Marchesi, V. T. et al. (1988). “Entrez Gene: SPTAN1 spectrin, alpha, non-erythrocytic 1 (alpha-fodrin)”. Molecular and Cellular Biology 8 (1): 1–9. doi:10.1128/MCB.8.1.1. PMC 363070. PMID 3336352.
- ^ “cDNA cloning, sequencing and chromosome mapping of a non-erythroid spectrin, human alpha-fodrin”. Differentiation 34 (1): 68–78. (1987). doi:10.1111/j.1432-0436.1987.tb00052.x. PMID 3038643.
- ^ a b c “Characterization and expression of a heart-selective alternatively spliced variant of alpha II-spectrin, cardi+, during development in the rat”. Journal of Molecular and Cellular Cardiology 48 (6): 1050–9. (Jun 2010). doi:10.1016/j.yjmcc.2010.01.001. PMC 3537504. PMID 20114050.
- ^ “Brain and muscle express a unique alternative transcript of alphaII spectrin”. Biochemistry 38 (48): 15721–30. (Nov 1999). doi:10.1021/bi991458k. PMID 10625438.
- ^ “Mapping the human erythrocyte beta-spectrin dimer initiation site using recombinant peptides and correlation of its phasing with the alpha-actinin dimer site”. The Journal of Biological Chemistry 271 (12): 6636–44. (Mar 1996). doi:10.1074/jbc.271.12.6636. PMID 8636080.
- ^ a b “Cardiac myofibrillogenesis inside intact embryonic hearts”. Developmental Biology 318 (2): 236–46. (Jun 2008). doi:10.1016/j.ydbio.2008.03.011. PMC 2496890. PMID 18455713.
- ^ “The transitional junction: a new functional subcellular domain at the intercalated disc”. Molecular Biology of the Cell 17 (4): 2091–100. (Apr 2006). doi:10.1091/mbc.E05-12-1109. PMC 1415289. PMID 16481394.
- ^ “Not just a plasma membrane protein: in cardiac muscle cells alpha-II spectrin also shows a close association with myofibrils”. Journal of Muscle Research and Cell Motility 25 (2): 119–26. (2004). doi:10.1023/b:jure.0000035892.77399.51. PMID 15360127.
- ^ “Alpha-spectrin in detergent-extracted whole-mount cytoskeletons of chicken embryo heart fibroblasts”. The Histochemical Journal 25 (9): 678–86. (Sep 1993). doi:10.1007/bf00157882. PMID 8226104.
- ^ “Spectrin alpha II and beta II isoforms interact with high affinity at the tetramerization site”. The Biochemical Journal 374 (Pt 3): 613–24. (Sep 2003). doi:10.1042/BJ20030507. PMC 1223645. PMID 12820899.
- ^ a b “The spectrin-associated cytoskeleton in mammalian heart”. Frontiers in Bioscience 10 (1–3): 3020–33. (1 September 2005). doi:10.2741/1759. PMID 15970557.
- ^ “Role of an alternatively spliced form of alphaII-spectrin in localization of connexin 43 in cardiomyocytes and regulation by stress-activated protein kinase”. Journal of Molecular and Cellular Cardiology 42 (3): 572–81. (Mar 2007). doi:10.1016/j.yjmcc.2006.11.018. PMC 1983066. PMID 17276456.
- ^ “AlphaII-spectrin is critical for cell adhesion and cell cycle”. The Journal of Biological Chemistry 284 (4): 2409–18. (Jan 2009). doi:10.1074/jbc.M801324200. PMID 18978357.
- ^ “alphaII-Spectrin interacts with five groups of functionally important proteins in the nucleus”. Cell Biology International 30 (11): 866–78. (Nov 2006). doi:10.1016/j.cellbi.2006.06.005. PMID 16889989.
- ^ “c-Src binds alpha II spectrin's Src homology 3 (SH3) domain and blocks calpain susceptibility by phosphorylating Tyr1176”. The Journal of Biological Chemistry 278 (9): 7735–41. (Feb 2003). doi:10.1074/jbc.M210988200. PMID 12446661.
- ^ “Ankyrin binds to the 15th repetitive unit of erythroid and nonerythroid beta-spectrin”. The Journal of Cell Biology 115 (1): 267–77. (Oct 1991). doi:10.1083/jcb.115.1.267. PMC 2289929. PMID 1833409.
- ^ “Caenorhabditis elegans beta-G spectrin is dispensable for establishment of epithelial polarity, but essential for muscular and neuronal function”. The Journal of Cell Biology 149 (4): 915–30. (May 2000). doi:10.1083/jcb.149.4.915. PMC 2174577. PMID 10811831.
- ^ “Identification of differentially expressed genes induced by angiotensin II in rat cardiac fibroblasts”. Clinical and Experimental Pharmacology & Physiology 33 (1–2): 41–6. (2006). doi:10.1111/j.1440-1681.2006.04321.x. PMID 16445697.
- ^ “Alpha II-spectrin breakdown products serve as novel markers of brain injury severity in a canine model of hypothermic circulatory arrest”. The Annals of Thoracic Surgery 88 (2): 543–50. (Aug 2009). doi:10.1016/j.athoracsur.2009.04.016. PMC 3412404. PMID 19632410.
- ^ “Early onset West syndrome with severe hypomyelination and coloboma-like optic discs in a girl with SPTAN1 mutation”. Epilepsia 53 (6): e106–10. (Jun 2012). doi:10.1111/j.1528-1167.2012.03437.x. PMID 22429196.
- ^ “Detection of alpha II-spectrin breakdown products in the serum of neonates with congenital heart disease*”. Pediatric Critical Care Medicine 15 (3): 229–35. (Mar 2014). doi:10.1097/PCC.0000000000000059. PMC 4059536. PMID 24395002.
- ^ “Proteome analysis of cerebrospinal fluid in Guillain–Barré syndrome (GBS)”. Journal of Neuroimmunology 185 (1–2): 190–4. (Apr 2007). doi:10.1016/j.jneuroim.2007.01.022. PMID 17367871.
- ^ “Identification of a candidate human spectrin Src homology 3 domain-binding protein suggests a general mechanism of association of tyrosine kinases with the spectrin-based membrane skeleton”. J. Biol. Chem. 273 (22): 13681–92. (May 1998). doi:10.1074/jbc.273.22.13681. PMID 9593709.
- ^ a b “Human alpha spectrin II and the FANCA, FANCC, and FANCG proteins bind to DNA containing psoralen interstrand cross-links”. Biochemistry 40 (24): 7025–34. (June 2001). doi:10.1021/bi002917g. PMID 11401546.
- ^ a b “Human alpha spectrin II and the Fanconi anemia proteins FANCA and FANCC interact to form a nuclear complex”. J. Biol. Chem. 274 (46): 32904–8. (November 1999). doi:10.1074/jbc.274.46.32904. PMID 10551855.
- ^ “Nonerythroid alphaII spectrin is required for recruitment of FANCA and XPF to nuclear foci induced by DNA interstrand cross-links”. J. Cell Sci. 116 (Pt 5): 823–35. (March 2003). doi:10.1242/jcs.00294. PMID 12571280.
- ^ “Interaction of the C-terminal domain of delta glutamate receptor with spectrin in the dendritic spines of cultured Purkinje cells”. Neurosci. Res. 34 (4): 281–7. (September 1999). doi:10.1016/s0168-0102(99)00061-9. PMID 10576550.
- ^ a b “Cutting edge: integration of human T lymphocyte cytoskeleton by the cytolinker plectin”. J. Immunol. 167 (2): 641–5. (July 2001). doi:10.4049/jimmunol.167.2.641. PMID 11441066.
- ^ “Plectin and IFAP-300K are homologous proteins binding to microtubule-associated proteins 1 and 2 and to the 240-kilodalton subunit of spectrin”. J. Biol. Chem. 262 (3): 1320–5. (January 1987). PMID 3027087.
- ^ “Synaptic scaffolding proteins in rat brain. Ankyrin repeats of the multidomain Shank protein family interact with the cytoskeletal protein alpha-fodrin”. J. Biol. Chem. 276 (43): 40104–12. (October 2001). doi:10.1074/jbc.M102454200. PMID 11509555.
[続きの解説]
「αII-スペクトリン」の続きの解説一覧
- 1 αII-スペクトリンとは
- 2 αII-スペクトリンの概要
- 3 構造
- 4 相互作用
- αII-スペクトリンのページへのリンク
