S100A7
Available structures
PDBHuman UniProt search: PDBe RCSB
Identifiers
AliasesS100A7, PSOR1, S100A7c, S100 calcium binding protein A7
External IDsOMIM: 600353 HomoloGene: 48150 GeneCards: S100A7
Orthologs
SpeciesHumanMouse
Entrez

6278

n/a

Ensembl

ENSG00000143556

n/a

UniProt

P31151

n/a

RefSeq (mRNA)

NM_002963

n/a

RefSeq (protein)

NP_002954

n/a

Location (UCSC)Chr 1: 153.46 – 153.46 Mbn/a
PubMed search[2]n/a
Wikidata
View/Edit Human

S100 calcium-binding protein A7 (S100A7), also known as psoriasin, is a protein that in humans is encoded by the S100A7 gene.[3]

Function

S100A7 is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a wide range of cells, and involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. S100 genes include at least 13 members which are located as a cluster on chromosome 1q21. This protein differs from the other S100 proteins of known structure in its lack of calcium binding ability in one EF-hand at the N-terminus. The protein functions as a prominent antimicrobial peptide mainly against E. coli.[4]

S100A7 also displays antimicrobial properties. It is secreted by epithelial cells of the skin and is a key antimicrobial protein against Escherichia coli by disrupting their cell membranes. This is the reason that in countries with poor sanitation, human skin is exposed to E. coli strains from faecal matter but it does not usually result in an infection.[5]

S100A7 is highly homologous to S100A7A (koebnerisin) but distinct in expression, tissue distribution and function.[6][7][8][9]

Clinical significance

This protein is markedly over-expressed in the skin lesions of psoriatic patients, but is excluded as a candidate gene for familial psoriasis susceptibility.[4] The expression of psoriasin is induced in skin wounds[10] through activation of the epidermal growth factor receptor.

Interactions

S100A7 has been shown to interact with COP9 constitutive photomorphogenic homolog subunit 5,[11] FABP5[12][13] and RANBP9.[14]

S100A7 interacts with RAGE (receptor of advanced glycated end products).[6][15]

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000143556 - Ensembl, May 2017
  2. ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. ↑ Madsen P, Rasmussen HH, Leffers H, Honoré B, Dejgaard K, Olsen E, Kiil J, Walbum E, Andersen AH, Basse B (Nov 1991). "Molecular cloning, occurrence, and expression of a novel partially secreted protein "psoriasin" that is highly up-regulated in psoriatic skin". J. Invest. Dermatol. 97 (4): 701–12. doi:10.1111/1523-1747.ep12484041. PMID 1940442.
  4. 1 2 "Entrez Gene: S100A7 S100 calcium binding protein A7".
  5. ↑ Bulet, P., et al. 2004. Anti-microbial peptides: from invertebrates to vertebrates. Immunology Review 198:169–184.
  6. 1 2 Wolf R, Howard OM, Dong HF, Voscopoulos C, Boeshans K, Winston J, Divi R, Gunsior M, Goldsmith P, Ahvazi B, Chavakis T, Oppenheim JJ, Yuspa SH (July 2008). "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". J. Immunol. 181 (2): 1499–506. doi:10.4049/jimmunol.181.2.1499. PMC 2435511. PMID 18606705.
  7. ↑ Wolf R, Voscopoulos C, Winston J, Dharamsi A, Goldsmith P, Gunsior M, Vonderhaar BK, Olson M, Watson PH, Yuspa SH (May 2009). "Highly homologous hS100A15 and hS100A7 proteins are distinctly expressed in normal breast tissue and breast cancer". Cancer Lett. 277 (1): 101–7. doi:10.1016/j.canlet.2008.11.032. PMC 2680177. PMID 19136201.
  8. ↑ Zwicker S, Bureik D, Ruzicka T, Wolf R (March 2012). "[Friend or Foe?--Psoriasin and Koebnerisin: multifunctional defence molecules in skin differentiation, tumorigenesis and inflammation]". Dtsch. Med. Wochenschr. (in German). 137 (10): 491–4. doi:10.1055/s-0031-1299015. PMID 22374659. S2CID 196460709.
  9. ↑ Hegyi Z, Zwicker S, Bureik D, Peric M, Koglin S, Batycka-Baran A, Prinz JC, Ruzicka T, Schauber J, Wolf R (May 2012). "Vitamin D analog calcipotriol suppresses the Th17 cytokine-induced proinflammatory S100 "alarmins" psoriasin (S100A7) and koebnerisin (S100A15) in psoriasis". J. Invest. Dermatol. 132 (5): 1416–24. doi:10.1038/jid.2011.486. PMID 22402441.
  10. ↑ Lee KC, Eckert RL (April 2007). "S100A7 (Psoriasin)--mechanism of antibacterial action in wounds". J. Invest. Dermatol. 127 (4): 945–57. doi:10.1038/sj.jid.5700663. PMID 17159909.
  11. ↑ Emberley ED, Niu Y, Leygue E, Tomes L, Gietz RD, Murphy LC, Watson PH (April 2003). "Psoriasin interacts with Jab1 and influences breast cancer progression". Cancer Res. 63 (8): 1954–61. PMID 12702588.
  12. ↑ Ruse M, Broome AM, Eckert RL (July 2003). "S100A7 (psoriasin) interacts with epidermal fatty acid binding protein and localizes in focal adhesion-like structures in cultured keratinocytes". J. Invest. Dermatol. 121 (1): 132–41. doi:10.1046/j.1523-1747.2003.12309.x. PMID 12839573.
  13. ↑ Hagens G, Roulin K, Hotz R, Saurat JH, Hellman U, Siegenthaler G (February 1999). "Probable interaction between S100A7 and E-FABP in the cytosol of human keratinocytes from psoriatic scales". Mol. Cell. Biochem. 192 (1–2): 123–8. doi:10.1023/A:1006894909694. PMID 10331666. S2CID 24171894.
  14. ↑ Emberley ED, Gietz RD, Campbell JD, HayGlass KT, Murphy LC, Watson PH (November 2002). "RanBPM interacts with psoriasin in vitro and their expression correlates with specific clinical features in vivo in breast cancer". BMC Cancer. 2: 28. doi:10.1186/1471-2407-2-28. PMC 137593. PMID 12421467.
  15. ↑ Winston J, Wolf R (September 2012). "Psoriasin (S100A7) promotes migration of a squamous carcinoma cell line". J. Dermatol. Sci. 67 (3): 205–7. doi:10.1016/j.jdermsci.2012.06.009. PMID 22795619.

Further reading

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