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SPTA1  -  spectrin, alpha, erythrocytic 1

Homo sapiens

Synonyms: EL2, Erythroid alpha-spectrin, HPP, HS3, SPH3, ...
 
 
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Disease relevance of SPTA1

 

High impact information on SPTA1

 

Biological context of SPTA1

  • Importantly, CD1, SPTA1, OR, and FCERIA belong to multigene families, which have paralogues in the other three regions [8].
  • Close linkage of PUM and SPTA within chromosome band 1q21 [9].
  • Suspended T and B lymphoid cell lines (Jurkat and Raji, respectively) were exposed to low frequency ULS (750 KHz) at an intensity level of 54.6 W/cm(2) spatial peak temporal average (SPTA) at focal area, which was found to be the optimal physical parameter to induce apoptosis in these malignant cell lines [10].
  • The frequency of sister chromatid exchanges (SCE) is unchanged in Chinese hamster ovarian cells insonated with a stationary transducer for 1-30 minutes at an SPTA intensity of 0.1 W/cm2 [11].
 

Anatomical context of SPTA1

  • Overlapping human erythroid alpha-spectrin cDNA clones were isolated from lambda gt11 libraries constructed from cDNAs of human fetal liver and erythroid bone marrow [12].
  • In the macropinosomes of NIH 3T3 cells, Hssh3bp1 associates with a 200-kDa protein that crossreacts with a monoclonal antibody to the erythroid alpha-spectrin SH3 domain [13].
  • We studied the localization of p230, an immunoanalogue of erythroid alpha-spectrin, in normal and psoriatic human epidermis and in cultured human keratinocytes [14].
  • Suspensions of human blood cells, cells of a human leukemic cell line (Reh) and mixtures of nucleated cells with erythrocytes were exposed to continuous ultrasound of 782 kHz at a SPTA intensity of 15 W/cm2 [15].
  • The irradiation of bilayer lipid membranes with continuous ultrasound of a frequency of 8.2 MHz and a spacial peak time average (SPTA) intensity of 0.4 W/cm2 reduces the thickness of the unstirred layer up to 40% of its initial value under our conditions [16].
 

Other interactions of SPTA1

  • 1. Whereas in HS, the SPTA1 and SPTB gene mutations tend to abolish the synthesis of the corresponding chains, in HE/HP, they hinder spectrin tetramerization [17].
  • The mutations responsible for HE and HPP, lie in the SPTA1 and SPTB gene, and in the EPB41 gene encoding protein 4 [18].
  • Nine families were examined for linkage on chromosome 1 between the hypervariable gene PUM and the alpha-spectrin (SPTA) gene using DNA probes [9].
 

Analytical, diagnostic and therapeutic context of SPTA1

References

  1. Loss of heterozygosity on chromosome 1q in human breast cancer. Chen, L.C., Dollbaum, C., Smith, H.S. Proc. Natl. Acad. Sci. U.S.A. (1989) [Pubmed]
  2. Mutation at position -12 of intron 45 (c-->t) plays a prevalent role in the partial skipping of exon 46 from the transcript of allele alphaLELY in erythroid cells. Wilmotte, R., Marechal, J., Delaunay, J. Br. J. Haematol. (1999) [Pubmed]
  3. Significant admixture linkage disequilibrium across 30 cM around the FY locus in African Americans. Lautenberger, J.A., Stephens, J.C., O'Brien, S.J., Smith, M.W. Am. J. Hum. Genet. (2000) [Pubmed]
  4. The exon 46-encoded sequence is essential for stability of human erythroid alpha-spectrin and heterodimer formation. Wilmotte, R., Harper, S.L., Ursitti, J.A., Maréchal, J., Delaunay, J., Speicher, D.W. Blood (1997) [Pubmed]
  5. Partial characterization and assignment of the gene for protoporphyrinogen oxidase and variegate porphyria to human chromosome 1q23. Roberts, A.G., Whatley, S.D., Daniels, J., Holmans, P., Fenton, I., Owen, M.J., Thompson, P., Long, C., Elder, G.H. Hum. Mol. Genet. (1995) [Pubmed]
  6. Dinucleotide repeat polymorphism at the human erythroid alpha spectrin (SPTA1) locus. Hentati, A., Hu, P., Asgharzadeh, S., Siddique, T. Hum. Mol. Genet. (1992) [Pubmed]
  7. Comparison of nonerythroid alpha-spectrin genes reveals strict homology among diverse species. Leto, T.L., Fortugno-Erikson, D., Barton, D., Yang-Feng, T.L., Francke, U., Harris, A.S., Morrow, J.S., Marchesi, V.T., Benz, E.J. Mol. Cell. Biol. (1988) [Pubmed]
  8. Genomic anatomy of a premier major histocompatibility complex paralogous region on chromosome 1q21-q22. Shiina, T., Ando, A., Suto, Y., Kasai, F., Shigenari, A., Takishima, N., Kikkawa, E., Iwata, K., Kuwano, Y., Kitamura, Y., Matsuzawa, Y., Sano, K., Nogami, M., Kawata, H., Li, S., Fukuzumi, Y., Yamazaki, M., Tashiro, H., Tamiya, G., Kohda, A., Okumura, K., Ikemura, T., Soeda, E., Mizuki, N., Kimura, M., Bahram, S., Inoko, H. Genome Res. (2001) [Pubmed]
  9. Close linkage of PUM and SPTA within chromosome band 1q21. Middleton-Price, H., Gendler, S., Malcolm, S. Ann. Hum. Genet. (1988) [Pubmed]
  10. Induction of apoptosis by ultrasound application in human malignant lymphoid cells: role of mitochondria-caspase pathway activation. Firestein, F., Rozenszajn, L.A., Shemesh-Darvish, L., Elimelech, R., Radnay, J., Rosenschein, U. Ann. N. Y. Acad. Sci. (2003) [Pubmed]
  11. Temporal peak intensity as a critical parameter in ultrasound dosimetry. Barnett, S.B., Kossoff, G. Journal of ultrasound in medicine : official journal of the American Institute of Ultrasound in Medicine. (1984) [Pubmed]
  12. The complete cDNA and polypeptide sequences of human erythroid alpha-spectrin. Sahr, K.E., Laurila, P., Kotula, L., Scarpa, A.L., Coupal, E., Leto, T.L., Linnenbach, A.J., Winkelmann, J.C., Speicher, D.W., Marchesi, V.T. J. Biol. Chem. (1990) [Pubmed]
  13. Human spectrin Src homology 3 domain binding protein 1 regulates macropinocytosis in NIH 3T3 cells. Xu, J., Ziemnicka, D., Merz, G.S., Kotula, L. J. Cell. Sci. (2000) [Pubmed]
  14. Distribution of p230, an alpha-spectrin-related polypeptide in normal and psoriatic epidermis and in cultured human keratinocytes. Kariniemi, A.L., Lehto, V.P., Virtanen, I. Br. J. Dermatol. (1984) [Pubmed]
  15. Cell membrane damage by ultrasound at different cell concentrations. Ellwart, J.W., Brettel, H., Kober, L.O. Ultrasound in medicine & biology. (1988) [Pubmed]
  16. Effects of ultrasound on the steady-state transmembrane pH gradient and the permeability of acetic acid through bilayer lipid membranes. Pohl, P., Rosenfeld, E., Millner, R. Biochim. Biophys. Acta (1993) [Pubmed]
  17. Molecular basis of red cell membrane disorders. Delaunay, J. Acta Haematol. (2002) [Pubmed]
  18. Red blood cell membrane defects. Iolascon, A., Perrotta, S., Stewart, G.W. Reviews in clinical and experimental hematology. (2003) [Pubmed]
  19. Dinucleotide repeat polymorphism at the human erythroid alpha-spectrin (SPTA1) mRNA gene detected using PCR. Bodfish, P., Warne, D., Nyberg, K., Spurr, N.K. Hum. Mol. Genet. (1992) [Pubmed]
 
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