SPTAN1

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Template:Short description Template:Cs1 config An Error has occurred retrieving Wikidata item for infobox Alpha II-spectrin, also known as Spectrin alpha chain, brain is a protein that in humans is encoded by the SPTAN1 gene.[1][2][3] Alpha II-spectrin is expressed in a variety of tissues, and is highly expressed in cardiac muscle at Z-disc structures, costameres and at the sarcolemma membrane. Mutations in alpha II-spectrin have been associated with early infantile epileptic encephalopathy-5, and alpha II-spectrin may be a valuable biomarker for Guillain–Barré syndrome and infantile congenital heart disease.

Structure

Alternate splicing of alpha II-spectrin has been documented and results in multiple transcript variants; specifically, cardiomyocytes have four identified alpha II-spectrin splice variants.[4][5] As opposed to alpha I-spectrin that is principally found in erythrocytes,[6] alpha II-spectrin is expressed in most tissues. In cardiac tissue, alpha II-spectrin is found in myocytes at Z-discs, costameres, and the sarcolemma membrane,[7][8][9] and in cardiac fibroblasts along the surface of the cytoskeletal network.[10] Alpha II-spectrin most commonly exists in a heterodimer with alpha II and beta II spectrin subunits; and dimers typically self-associate and heterotetramerize.[1][11][12]

Function

The spectrins are a family of widely distributed cytoskeletal proteins which are involved in actin crosslinking, cell adhesion, intercellular communication and cell cycle regulation.[13][14][15] Though a role in cardiac muscle is not well understood, it is likely that alpha II-spectrin is involved in organizing sub-sarcolemmal domains and stabilizing sarcolemmal membranes against the stresses associated with continuous cardiac contraction.[12] Functional diversity of alpha II-spectrin is manifest through its four splice variants. First, a cardiac-specific, 21 amino acid sequence insert in the 21st spectrin repeat, termed alpha II-cardi+, was identified as an insert that modulates affinity of alpha II-spectrin for binding beta-spectrins and regulates myocyte growth and differentiation.[4] Secondly, another insert of 20 amino acids in the 10th spectrin repeat, termed SH3i+, contains protein kinase A and protein kinase C phosphorylation sites and modulates Ca2+-dependent cleavage of spectrin and protein-protein interaction properties.[16] Thirdly, an insert of five amino acids in the fifteenth spectrin motif bears a highly antigenic epitope resembling an ankyrin-like p53 binding protein binding site.[4][17] Fourthly, a six amino acid insert in the twenty-first spectrin motif with unknown function has been reported.[7][18]

Alpha II-spectrin gene expression has been shown to be upregulated in cardiac fibroblasts in response to Angiotensin II-induced cardiac remodeling.[19]

In animal models of disease and injury, alpha II-spectrin has been implicated in diverse functions. In a canine model of hypothermic circulatory arrest, alpha II-spectrin breakdown products have shown to be relevant markers of neurologic injury post-cardiac surgery.[20]

Clinical significance

Mutations in SPTAN1 are the cause of early infantile epileptic encephalopathy-5.[21]

Alpha II-spectrin has shown promising utility as a biomarker for brain necrosis and apoptosis in infants with congenital heart disease; breakdown products of alpha II-spectrin have been detected in the serum of neonates in the perioperative period and following open-heart surgery.[22] Elevated protein expression of alpha II-spectrin has been detected in cerebrospinal fluid in patients with Guillain–Barré syndrome.[23]

Interactions

SPTAN1 has been shown to interact with:

See also

References

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  1. ^ a b Page Module:Citation/CS1/styles.css has no content.Leto TL, Fortugno-Erikson D, Barton D, Yang-Feng TL, Francke U, Harris AS, et al. (February 1988). "Comparison of nonerythroid alpha-spectrin genes reveals strict homology among diverse species". Molecular and Cellular Biology. 8 (1): 1–9. doi:10.1128/MCB.8.1.1. PMC 363070. PMID 3336352.
  2. ^ Page Module:Citation/CS1/styles.css has no content.Leto TL, Fortugno-Erikson D, Barton D, Yang-Feng TL, Francke U, Harris AS, et al. (Jan 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.
  3. ^ Page Module:Citation/CS1/styles.css has no content.McMahon AP, Giebelhaus DH, Champion JE, Bailes JA, Lacey S, Carritt B, et al. (1987). "cDNA cloning, sequencing and chromosome mapping of a non-erythroid spectrin, human alpha-fodrin". Differentiation; Research in Biological Diversity. 34 (1): 68–78. doi:10.1111/j.1432-0436.1987.tb00052.x. PMID 3038643.
  4. ^ a b c Page Module:Citation/CS1/styles.css has no content.Zhang Y, Resneck WG, Lee PC, Randall WR, Bloch RJ, Ursitti JA (Jun 2010). "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): 1050–1059. doi:10.1016/j.yjmcc.2010.01.001. PMC 3537504. PMID 20114050.
  5. ^ Page Module:Citation/CS1/styles.css has no content.Cianci CD, Zhang Z, Pradhan D, Morrow JS (Nov 1999). "Brain and muscle express a unique alternative transcript of alphaII spectrin". Biochemistry. 38 (48): 15721–15730. doi:10.1021/bi991458k. PMID 10625438.
  6. ^ Page Module:Citation/CS1/styles.css has no content.Ursitti JA, Kotula L, DeSilva TM, Curtis PJ, Speicher DW (Mar 1996). "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): 6636–6644. doi:10.1074/jbc.271.12.6636. PMID 8636080.
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  10. ^ Page Module:Citation/CS1/styles.css has no content.Sormunen R (Sep 1993). "Alpha-spectrin in detergent-extracted whole-mount cytoskeletons of chicken embryo heart fibroblasts". The Histochemical Journal. 25 (9): 678–686. doi:10.1007/bf00157882. PMID 8226104. S2CID 34132236.
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  30. ^ Page Module:Citation/CS1/styles.css has no content.Herrmann H, Wiche G (January 1987). "Plectin and IFAP-300K are homologous proteins binding to microtubule-associated proteins 1 and 2 and to the 240-kilodalton subunit of spectrin". Journal of Biological Chemistry. 262 (3): 1320–1325. doi:10.1016/S0021-9258(19)75789-5. PMID 3027087.
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Further reading

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