S100A7

S100 calcium-binding protein A7

PDB rendering based on 1psr.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
SymbolsS100A7 ; PSOR1; S100A7c
External IDsOMIM: 600353 HomoloGene: 48150 GeneCards: S100A7 Gene
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez6278n/a
EnsemblENSG00000143556n/a
UniProtP31151n/a
RefSeq (mRNA)NM_002963n/a
RefSeq (protein)NP_002954n/a
Location (UCSC)Chr 1:
153.43 – 153.43 Mb		n/a
PubMed searchn/a

S100 calcium-binding protein A7 (S100A7), also known as psoriasin, is a protein that in humans is encoded by the S100A7 gene.[1]

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.[2]

S100A7 also displays antimicrobial properties. It is secreted by epithilial 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 E.coli strains from faecal matter but it does not usually result in an infection.[3]

S100A7 is highly homologous to S100A15 (koebnerisin) but distinct in expression, tissue distribution and function.[4][5][6][7]

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.[2] The expression of psoriasin is induced in skin wounds[8] through activation of the epidermal growth factor receptor.

Interactions

S100A7 has been shown to interact with COP9 constitutive photomorphogenic homolog subunit 5,[9] FABP5[10][11] and RANBP9.[12]

S100A7 interacts with RAGE (receptor of advanced glycated end products).[4][13]

References

  1. ↑ Madsen P, Rasmussen HH, Leffers H, Honoré B, Dejgaard K, Olsen E et al. (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. Vancouver style error (help)
  2. ↑ 2.0 2.1 "Entrez Gene: S100A7 S100 calcium binding protein A7".
  3. ↑ Bulet, P., et al. 2004. Anti-microbial peptides: from invertebrates to vertebrates. Immunology Review 198:169–184.
  4. ↑ 4.0 4.1 Wolf R, Howard OM, Dong HF, Voscopoulos C, Boeshans K, Winston J et al. (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.
  5. ↑ Wolf R, Voscopoulos C, Winston J, Dharamsi A, Goldsmith P, Gunsior M et al. (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.
  6. ↑ 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.
  7. ↑ Hegyi Z, Zwicker S, Bureik D, Peric M, Koglin S, Batycka-Baran A et al. (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.
  8. ↑ 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.
  9. ↑ Emberley ED, Niu Y, Leygue E, Tomes L, Gietz RD, Murphy LC et al. (April 2003). "Psoriasin interacts with Jab1 and influences breast cancer progression". Cancer Res. 63 (8): 1954–61. PMID 12702588.
  10. ↑ 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.
  11. ↑ 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.
  12. ↑ 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.
  13. ↑ 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

  • Schäfer BW, Heizmann CW (1996). "The S100 family of EF-hand calcium-binding proteins: functions and pathology". Trends Biochem. Sci. 21 (4): 134–40. doi:10.1016/S0968-0004(96)80167-8. PMID 8701470. Vancouver style error (help)
  • Watson PH, Leygue ER, Murphy LC (1998). "Psoriasin (S100A7)". Int. J. Biochem. Cell Biol. 30 (5): 567–71. doi:10.1016/S1357-2725(97)00066-6. PMID 9693957.
  • Rasmussen HH, van Damme J, Puype M, Gesser B, Celis JE, Vandekerckhove J (1992). "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes". Electrophoresis 13 (12): 960–9. doi:10.1002/elps.11501301199. PMID 1286667.
  • Schäfer BW, Wicki R, Engelkamp D, Mattei MG, Heizmann CW (1995). "Isolation of a YAC clone covering a cluster of nine S100 genes on human chromosome 1q21: rationale for a new nomenclature of the S100 calcium-binding protein family". Genomics 25 (3): 638–43. doi:10.1016/0888-7543(95)80005-7. PMID 7759097. Vancouver style error (help)
  • Hoffmann HJ, Olsen E, Etzerodt M, Madsen P, Thøgersen HC, Kruse T et al. (1994). "Psoriasin binds calcium and is upregulated by calcium to levels that resemble those observed in normal skin". J. Invest. Dermatol. 103 (3): 370–5. doi:10.1111/1523-1747.ep12395202. PMID 8077703. Vancouver style error (help)
  • Bürgisser DM, Siegenthaler G, Kuster T, Hellman U, Hunziker P, Birchler N et al. (1995). "Amino acid sequence analysis of human S100A7 (psoriasin) by tandem mass spectrometry". Biochem. Biophys. Res. Commun. 217 (1): 257–63. doi:10.1006/bbrc.1995.2772. PMID 8526920. Vancouver style error (help)
  • Celis JE, Rasmussen HH, Vorum H, Madsen P, Honoré B, Wolf H et al. (1996). "Bladder squamous cell carcinomas express psoriasin and externalize it to the urine". J. Urol. 155 (6): 2105–12. doi:10.1016/S0022-5347(01)66118-4. PMID 8618345. Vancouver style error (help)
  • Brodersen DE, Etzerodt M, Madsen P, Celis JE, Thøgersen HC, Nyborg J et al. (1998). "EF-hands at atomic resolution: the structure of human psoriasin (S100A7) solved by MAD phasing". Structure 6 (4): 477–89. doi:10.1016/S0969-2126(98)00049-5. PMID 9562557. Vancouver style error (help)
  • Brodersen DE, Nyborg J, Kjeldgaard M (1999). "Zinc-binding site of an S100 protein revealed. Two crystal structures of Ca2+-bound human psoriasin (S100A7) in the Zn2+-loaded and Zn2+-free states". Biochemistry 38 (6): 1695–704. doi:10.1021/bi982483d. PMID 10026247.
  • Semprini S, Capon F, Bovolenta S, Bruscia E, Pizzuti A, Fabrizi G et al. (1999). "Genomic structure, promoter characterisation and mutational analysis of the S100A7 gene: exclusion of a candidate for familial psoriasis susceptibility". Hum. Genet. 104 (2): 130–4. doi:10.1007/s004390050925. PMID 10190323.
  • Hagens G, Masouyé I, Augsburger E, Hotz R, Saurat JH, Siegenthaler G (1999). "Calcium-binding protein S100A7 and epidermal-type fatty acid-binding protein are associated in the cytosol of human keratinocytes". Biochem. J. 339 ( Pt 2) (2): 419–27. doi:10.1042/0264-6021:3390419. PMC 1220173. PMID 10191275. Vancouver style error (help)
  • Hagens G, Roulin K, Hotz R, Saurat JH, Hellman U, Siegenthaler G (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.
  • Al-Haddad S, Zhang Z, Leygue E, Snell L, Huang A, Niu Y et al. (1999). "Psoriasin (S100A7) expression and invasive breast cancer". Am. J. Pathol. 155 (6): 2057–66. doi:10.1016/S0002-9440(10)65524-1. PMC 1866920. PMID 10595935.
  • Dias Neto E, Correa RG, Verjovski-Almeida S, Briones MR, Nagai MA, da Silva W et al. (2000). "Shotgun sequencing of the human transcriptome with ORF expressed sequence tags". Proc. Natl. Acad. Sci. U.S.A. 97 (7): 3491–6. doi:10.1073/pnas.97.7.3491. PMC 16267. PMID 10737800.
  • Ruse M, Lambert A, Robinson N, Ryan D, Shon KJ, Eckert RL (2001). "S100A7, S100A10, and S100A11 are transglutaminase substrates". Biochemistry 40 (10): 3167–73. doi:10.1021/bi0019747. PMID 11258932.
  • Enerbäck C, Porter DA, Seth P, Sgroi D, Gaudet J, Weremowicz S et al. (2002). "Psoriasin expression in mammary epithelial cells in vitro and in vivo". Cancer Res. 62 (1): 43–7. PMID 11782356. Vancouver style error (help)
  • Gemmill RM, Bemis LT, Lee JP, Sozen MA, Baron A, Zeng C et al. (2002). "The TRC8 hereditary kidney cancer gene suppresses growth and functions with VHL in a common pathway". Oncogene 21 (22): 3507–16. doi:10.1038/sj.onc.1205437. PMID 12032852.