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Gene Review

S100A7A  -  S100 calcium binding protein A7A

Homo sapiens

Synonyms: NICE-2, Protein S100-A7A, S100 calcium-binding protein A15, S100 calcium-binding protein A7-like 1, S100 calcium-binding protein A7A, ...
 
 
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Disease relevance of S100A7A

  • S100A15 (koebernisin)   is proinflammatory through a yet to identified Gi protein-coupled receptor. The enhanced expression of the 11.2 kDa S100A15 (koebnerisin) in psoriasis and epithelial cancers suggests that it contributes to the disease pathogenesis and could provide a molecular target for therapy [1] [2] [3] [4].
 

High impact information on S100A7A

  • We used PCR to amplify an indel within intron 1 of the S100A7a (koebnerisin) and S100A7c (psoriasin) genes that gave the same two expected product sizes using 40 human DNA samples and 1 chimpanzee sample, therefore confirming the presence of the region 1 and 3 duplication in these species [5].
  • Human S100A15 (koebnerisin) is a novel member of the S100 family of EF-hand calcium-binding proteins and was recently identified in psoriasis, where it is significantly upregulated in lesional skin [1].
  • By sequence comparison, we have mapped the novel gene, named S100A15, to the S100 gene cluster within the epidermal differentiation complex (chromosome 1q21) [6].
 

Analytical, diagnostic and therapeutic context of S100A7A

  • In situ hybridization of the S100A15 (koebnerisin) revealed a markedly increased staining of basal and suprabasal epidermal layers of psoriatic skin compared with healthy tissue [6].
  • Sequence analysis of a 650-bp cDNA fragment (clone 110) that was highly up-regulated in lesional skin revealed homology to a noncoding cDNA (NICE-2) [6].
  • Purification, crystallization and preliminary X-ray diffraction of human S100A15 (koebnerisin) [1].
  • Northern blot hybridization and semiquantitative RT-PCR analysis confirmed the S100A15 (koebnerisin) overexpression in psoriasis, showing different levels of expression of the S100A15 mRNA isoforms [6].

References

  1. Purification, crystallization and preliminary X-ray diffraction of human S100A15. Boeshans, K.M., Wolf, R., Voscopoulos, C., Gillette, W., Esposito, D., Mueser, T.C., Yuspa, S.H., Ahvazi, B. Acta Crystallograph. Sect. F Struct. Biol. Cryst. Commun. (2006) [Pubmed]
  2. Chemotactic activity of S100A7 (Psoriasin) is mediated by the receptor for advanced glycation end products and potentiates inflammation with highly homologous but functionally distinct S100A15. Wolf, R., Howard, O.M., Dong, H.F., Voscopoulos, C., Boeshans, K., Winston, J., Divi, R., Gunsior, M., Goldsmith, P., Ahvazi, B., Chavakis, T., Oppenheim, J.J., Yuspa, S.H. J. Immunol. (2008) [Pubmed]
  3. Highly homologous hS100A15 and hS100A7 proteins are distinctly expressed in normal breast tissue and breast cancer. Wolf, R., Voscopoulos, C., Winston, J., Dharamsi, A., Goldsmith, P., Gunsior, M., Vonderhaar, B.K., Olson, M., Watson, P.H., Yuspa, S.H. Cancer. Lett. (2009) [Pubmed]
  4. Novel S100A7 (psoriasin)/S100A15 (koebnerisin) subfamily: highly homologous but distinct in regulation and function. Wolf, R., Ruzicka, T., Yuspa, S.H. Amino. Acids. (2010) [Pubmed]
  5. Genomic and phylogenetic analysis of the S100A7 (Psoriasin) gene duplications within the region of the S100 gene cluster on human chromosome 1q21. Kulski, J.K., Lim, C.P., Dunn, D.S., Bellgard, M. J. Mol. Evol. (2003) [Pubmed]
  6. Molecular cloning and characterization of alternatively spliced mRNA isoforms from psoriatic skin encoding a novel member of the S100 family. Wolf, R., Mirmohammadsadegh, A., Walz, M., Lysa, B., Tartler, U., Remus, R., Hengge, U., Michel, G., Ruzicka, T. FASEB J. (2003) [Pubmed]
 
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