Spectrin alpha chain, erythrocyte is a protein that in humans is encoded by the SPTA1gene.
Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is a tetramer made up of alpha-beta dimers linked in a head-to-head arrangement. This gene is one member of a family of alpha-spectrin genes. The encoded protein is primarily composed of 22 spectrin repeats which are involved in dimer formation. It forms weaker tetramer interactions than non-erythrocytic alpha spectrin, which may increase the plasma membrane elasticity and deformability of red blood cells. Mutations in this gene result in a variety of hereditary red blood cell disorders, including elliptocytosis type 2, pyropoikilocytosis, and spherocytic hemolytic anemia.
^Ziemnicka-Kotula, D; Xu J, Gu H, Potempska A, Kim K S, Jenkins E C, Trenkner E, Kotula L (May. 1998). "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. (UNITED STATES) 273 (22): 13681–92. doi:10.1074/jbc.273.22.13681. ISSN0021-9258. PMID9593709.
Hentati A, Hu P, Asgharzadeh S, Siddique T (1993). "Dinucleotide repeat polymorphism at the human erythroid alpha spectrin (SPTA1) locus.". Hum. Mol. Genet.1 (3): 218. doi:10.1093/hmg/1.3.218-a. PMID1339473.
Kanzaki A, Rabodonirina M, Yawata Y, et al. (1992). "A deletional frameshift mutation of the beta-spectrin gene associated with elliptocytosis in spectrin Tokyo (beta 220/216).". Blood80 (8): 2115–21. PMID1391962.
Gallagher PG, Tse WT, Coetzer T, et al. (1992). "A common type of the spectrin alpha I 46-50a-kD peptide abnormality in hereditary elliptocytosis and pyropoikilocytosis is associated with a mutation distant from the proteolytic cleavage site. Evidence for the functional importance of the triple helical model of spectrin.". J. Clin. Invest.89 (3): 892–8. doi:10.1172/JCI115669. PMC442935. PMID1541680.
Speicher DW, Weglarz L, DeSilva TM (1992). "Properties of human red cell spectrin heterodimer (side-to-side) assembly and identification of an essential nucleation site.". J. Biol. Chem.267 (21): 14775–82. PMID1634521.
Alloisio N, Wilmotte R, Morlé L, et al. (1992). "Spectrin Jendouba: an alpha II/31 spectrin variant that is associated with elliptocytosis and carries a mutation distant from the dimer self-association site.". Blood80 (3): 809–15. PMID1638030.
Coetzer TL, Sahr K, Prchal J, et al. (1991). "Four different mutations in codon 28 of alpha spectrin are associated with structurally and functionally abnormal spectrin alpha I/74 in hereditary elliptocytosis.". J. Clin. Invest.88 (3): 743–9. doi:10.1172/JCI115371. PMC295451. PMID1679439.
Sahr KE, Laurila P, Kotula L, et al. (1990). "The complete cDNA and polypeptide sequences of human erythroid alpha-spectrin.". J. Biol. Chem.265 (8): 4434–43. PMID1689726.
Gallagher PG, Tse WT, Marchesi SL, et al. (1993). "A defect in alpha-spectrin mRNA accumulation in hereditary pyropoikilocytosis.". Trans. Assoc. Am. Physicians104: 32–9. PMID1845156.
Floyd PB, Gallagher PG, Valentino LA, et al. (1991). "Heterogeneity of the molecular basis of hereditary pyropoikilocytosis and hereditary elliptocytosis associated with increased levels of the spectrin alpha I/74-kilodalton tryptic peptide.". Blood78 (5): 1364–72. PMID1878597.
Garbarz M, Tse WT, Gallagher PG, et al. (1991). "Spectrin Rouen (beta 220-218), a novel shortened beta-chain variant in a kindred with hereditary elliptocytosis. Characterization of the molecular defect as exon skipping due to a splice site mutation.". J. Clin. Invest.88 (1): 76–81. doi:10.1172/JCI115307. PMC296005. PMID2056132.
Tse WT, Gallagher PG, Pothier B, et al. (1991). "An insertional frameshift mutation of the beta-spectrin gene associated with elliptocytosis in spectrin nice (beta 220/216).". Blood78 (2): 517–23. PMID2070088.