Biology:S100A7
 Generic protein structure example |
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 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.[3]
S100A7 is highly homologous to S100A7A (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
- ↑ "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. Nov 1991. doi:10.1111/1523-1747.ep12484041. PMID 1940442.
- ↑ 2.0 2.1 "Entrez Gene: S100A7 S100 calcium binding protein A7". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6278.
- ↑ Bulet, P., et al. 2004. Anti-microbial peptides: from invertebrates to vertebrates. Immunology Review 198:169–184.
- ↑ 4.0 4.1 "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. July 2008. doi:10.4049/jimmunol.181.2.1499. PMID 18606705.
- ↑ "Highly homologous hS100A15 and hS100A7 proteins are distinctly expressed in normal breast tissue and breast cancer". Cancer Lett. 277 (1): 101–7. May 2009. doi:10.1016/j.canlet.2008.11.032. PMID 19136201.
- ↑ "[Friend or Foe?--Psoriasin and Koebnerisin: multifunctional defence molecules in skin differentiation, tumorigenesis and inflammation]" (in de). Dtsch. Med. Wochenschr. 137 (10): 491–4. March 2012. doi:10.1055/s-0031-1299015. PMID 22374659.
- ↑ "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. May 2012. doi:10.1038/jid.2011.486. PMID 22402441.
- ↑ "S100A7 (Psoriasin)--mechanism of antibacterial action in wounds". J. Invest. Dermatol. 127 (4): 945–57. April 2007. doi:10.1038/sj.jid.5700663. PMID 17159909.
- ↑ "Psoriasin interacts with Jab1 and influences breast cancer progression". Cancer Res. 63 (8): 1954–61. April 2003. PMID 12702588.
- ↑ "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. July 2003. doi:10.1046/j.1523-1747.2003.12309.x. PMID 12839573.
- ↑ "Probable interaction between S100A7 and E-FABP in the cytosol of human keratinocytes from psoriatic scales". Mol. Cell. Biochem. 192 (1–2): 123–8. February 1999. doi:10.1023/A:1006894909694. PMID 10331666.
- ↑ "RanBPM interacts with psoriasin in vitro and their expression correlates with specific clinical features in vivo in breast cancer". BMC Cancer 2: 28. November 2002. doi:10.1186/1471-2407-2-28. PMID 12421467.
- ↑ "Psoriasin (S100A7) promotes migration of a squamous carcinoma cell line". J. Dermatol. Sci. 67 (3): 205–7. September 2012. doi:10.1016/j.jdermsci.2012.06.009. PMID 22795619.
Further reading
- "The S100 family of EF-hand calcium-binding proteins: functions and pathology". Trends Biochem. Sci. 21 (4): 134–40. 1996. doi:10.1016/S0968-0004(96)80167-8. PMID 8701470.
- "Psoriasin (S100A7)". Int. J. Biochem. Cell Biol. 30 (5): 567–71. 1998. doi:10.1016/S1357-2725(97)00066-6. PMID 9693957.
- "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes". Electrophoresis 13 (12): 960–9. 1992. doi:10.1002/elps.11501301199. PMID 1286667.
- "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. 1995. doi:10.1016/0888-7543(95)80005-7. PMID 7759097.
- "Psoriasin binds calcium and is upregulated by calcium to levels that resemble those observed in normal skin". J. Invest. Dermatol. 103 (3): 370–5. 1994. doi:10.1111/1523-1747.ep12395202. PMID 8077703.
- "Amino acid sequence analysis of human S100A7 (psoriasin) by tandem mass spectrometry". Biochem. Biophys. Res. Commun. 217 (1): 257–63. 1995. doi:10.1006/bbrc.1995.2772. PMID 8526920.
- "Bladder squamous cell carcinomas express psoriasin and externalize it to the urine". J. Urol. 155 (6): 2105–12. 1996. doi:10.1016/S0022-5347(01)66118-4. PMID 8618345.
- "EF-hands at atomic resolution: the structure of human psoriasin (S100A7) solved by MAD phasing". Structure 6 (4): 477–89. 1998. doi:10.1016/S0969-2126(98)00049-5. PMID 9562557.
- "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. 1999. doi:10.1021/bi982483d. PMID 10026247.
- "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. 1999. doi:10.1007/s004390050925. PMID 10190323.
- "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. 1999. doi:10.1042/0264-6021:3390419. PMID 10191275.
- "Probable interaction between S100A7 and E-FABP in the cytosol of human keratinocytes from psoriatic scales". Mol. Cell. Biochem. 192 (1–2): 123–8. 1999. doi:10.1023/A:1006894909694. PMID 10331666.
- "Psoriasin (S100A7) expression and invasive breast cancer". Am. J. Pathol. 155 (6): 2057–66. 1999. doi:10.1016/S0002-9440(10)65524-1. PMID 10595935.
- "Shotgun sequencing of the human transcriptome with ORF expressed sequence tags". Proc. Natl. Acad. Sci. U.S.A. 97 (7): 3491–6. 2000. doi:10.1073/pnas.97.7.3491. PMID 10737800. Bibcode: 2000PNAS...97.3491D.
- "S100A7, S100A10, and S100A11 are transglutaminase substrates". Biochemistry 40 (10): 3167–73. 2001. doi:10.1021/bi0019747. PMID 11258932.
- "Psoriasin expression in mammary epithelial cells in vitro and in vivo". Cancer Res. 62 (1): 43–7. 2002. PMID 11782356.
- "The TRC8 hereditary kidney cancer gene suppresses growth and functions with VHL in a common pathway". Oncogene 21 (22): 3507–16. 2002. doi:10.1038/sj.onc.1205437. PMID 12032852.
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