Biology:S100A2
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Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
S100 calcium-binding protein A2 (S100A2) is a protein that in humans is encoded by the S100A2 gene[1] and it is located on chromosome 1q21 with other S100 proteins.
Tissue and subcellular distribution
S100A2, also known as CaN19 or S100L was first isolated from bovine lung tissue.[2] However, in human tissue it was discovered several years later, in the mammary epithelial cells.[3] Under normal circumstances it is highly expressed in human lungs, prostate, kidneys, hair follicles and salivary and mammary glands.[4] S100A2 is predominantly found in the nucleus, which is not very common in other S100 proteins. Moreover, it can also be found in the cytoplasm, and its distribution is rather diffuse. Its occurrence in cytoplasm is most likely dependent on calcium levels in the cell.[5][6][7] In the extracellular environment, it can be found as a homodimer in vivo and in vitro, but it also exists in monomeric, polymeric and multimeric forms. In multimeric form, it functions as a RAGE receptor ligand.[8]
Function
S100A2 is important in cytoskeleton organization.[9] Also, S100A2 is induced by p53, which it interacts and participates in the transcription of p21.[7][10] It also plays a role in differentiation, regeneration of tissues and healing[11][12] and it was shown it attract eosinophils by chemotaxis.[13]
Clinical significance
Its expression is reduced in many types of cancer, thereby distinguishing the cancerous expression profile of the other proteins of the S100 group.[14][15][16] It has been reported that S100A2 is downregulated in lung, kidney, prostate cancer and melanoma.[14] Chromosomal rearrangements and altered expression of this gene have also been implicated in breast cancer.[17][16][6] In addition, its decline is associated with poor prognosis, disease progression, increased occurrence of metastasis and increased patient mortality.[18] Although in most cancers it has been found in reduced levels, there are studies that show that in some cases it is overproduced.[19][20]
References
- ↑ "Six S100 genes are clustered on human chromosome 1q21: identification of two genes coding for the two previously unreported calcium-binding proteins S100D and S100E". Proceedings of the National Academy of Sciences of the United States of America 90 (14): 6547–51. July 1993. doi:10.1073/pnas.90.14.6547. PMID 8341667. Bibcode: 1993PNAS...90.6547E.
- ↑ "Isolation of a new member of the S100 protein family: amino acid sequence, tissue, and subcellular distribution". The Journal of Cell Biology 108 (2): 569–78. February 1989. doi:10.1083/jcb.108.2.569. PMID 2521861.
- ↑ "Positive selection of candidate tumor-suppressor genes by subtractive hybridization". Proceedings of the National Academy of Sciences of the United States of America 88 (7): 2825–9. April 1991. doi:10.1073/pnas.88.7.2825. PMID 1849277. Bibcode: 1991PNAS...88.2825L.
- ↑ "S100A2 in cancerogenesis: a friend or a foe?". Amino Acids 41 (4): 849–61. October 2011. doi:10.1007/s00726-010-0623-2. PMID 20521072.
- ↑ "Differential responses of S100A2 to oxidative stress and increased intracellular calcium in normal, immortalized, and malignant human keratinocytes" (in en). The Journal of Investigative Dermatology 119 (5): 1196–201. November 2002. doi:10.1046/j.1523-1747.2002.19520.x. PMID 12445212.
- ↑ 6.0 6.1 "Expression pattern of S100 calcium-binding proteins in human tumors". International Journal of Cancer 68 (3): 325–32. November 1996. doi:10.1002/(SICI)1097-0215(19961104)68:3<325::AID-IJC10>3.0.CO;2-7. PMID 8903474.
- ↑ 7.0 7.1 "The calcium-binding protein S100A2 interacts with p53 and modulates its transcriptional activity". The Journal of Biological Chemistry 280 (32): 29186–93. August 2005. doi:10.1074/jbc.M505000200. PMID 15941720.
- ↑ "Biochemical characterization of S100A2 in human keratinocytes: subcellular localization, dimerization, and oxidative cross-linking". The Journal of Investigative Dermatology 115 (3): 477–85. September 2000. doi:10.1046/j.1523-1747.2000.00078.x. PMID 10951287.
- ↑ Martonosi, Anthony N. (1983). "The Regulation of Cytoplasmic Ca2+ Concentration in Muscle and Nonmuscle Cells". Muscle and Nonmuscle Motility (Elsevier): 233–357. doi:10.1016/b978-0-12-673001-2.50011-2. ISBN 9780126730012. https://archive.org/details/musclenonmusclem0001unse/page/233.
- ↑ "Transcriptional activation of the tumor suppressor and differentiation gene S100A2 by a novel p63-binding site". Nucleic Acids Research 36 (9): 2969–80. May 2008. doi:10.1093/nar/gkn132. PMID 18388131.
- ↑ "Molecular basis of S100 proteins interacting with the p53 homologs p63 and p73". Oncogene 29 (14): 2024–35. April 2010. doi:10.1038/onc.2009.490. PMID 20140014.
- ↑ "Enhancement of wound healing by topical treatment with epidermal growth factor". The New England Journal of Medicine 321 (2): 76–9. July 1989. doi:10.1056/NEJM198907133210203. PMID 2659995.
- ↑ "Novel specific chemtactic receptor for S100L protein on guinea pig eosinophils". Biochemical and Biophysical Research Communications 220 (3): 871–4. March 1996. doi:10.1006/bbrc.1996.0496. PMID 8607858.
- ↑ 14.0 14.1 "Differential expression patterns of S100A2, S100A4 and S100A6 during progression of human malignant melanoma". International Journal of Cancer 74 (4): 464–9. August 1997. doi:10.1002/(SICI)1097-0215(19970822)74:4<464::AID-IJC19>3.0.CO;2-9. PMID 9291441.
- ↑ "Differential expression of S100A2 and S100A4 during progression of human prostate adenocarcinoma". Journal of Clinical Oncology 21 (1): 106–12. January 2003. doi:10.1200/JCO.2003.03.024. PMID 12506178.
- ↑ 16.0 16.1 "Expression of calcium-binding protein S100A2 in breast lesions". British Journal of Cancer 83 (11): 1473–9. December 2000. doi:10.1054/bjoc.2000.1488. PMID 11076656.
- ↑ "Entrez Gene: S100A2 S100 calcium binding protein A2". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6273.
- ↑ "S100A2 expression as a predictive marker for late cervical metastasis in stage I and II invasive squamous cell carcinoma of the oral cavity". Oncology Reports 14 (6): 1493–8. December 2005. doi:10.3892/or.14.6.1493. PMID 16273244.
- ↑ "Overexpression of S100A2 protein as a prognostic marker for patients with stage I non small cell lung cancer". International Journal of Cancer 116 (2): 285–90. August 2005. doi:10.1002/ijc.21035. PMID 15800916.
- ↑ "Overexpression of the S100A2 protein as a prognostic marker for patients with stage II and III colorectal cancer". International Journal of Oncology 48 (3): 975–82. March 2016. doi:10.3892/ijo.2016.3329. PMID 26783118.
Further reading
- "The S100 family of EF-hand calcium-binding proteins: functions and pathology". Trends in Biochemical Sciences 21 (4): 134–40. April 1996. doi:10.1016/S0968-0004(96)80167-8. PMID 8701470.
- "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes". Electrophoresis 13 (12): 960–9. December 1992. doi:10.1002/elps.11501301199. PMID 1286667.
- "Down-regulation of a member of the S100 gene family in mammary carcinoma cells and reexpression by azadeoxycytidine treatment". Proceedings of the National Academy of Sciences of the United States of America 89 (6): 2504–8. March 1992. doi:10.1073/pnas.89.6.2504. PMID 1372446. Bibcode: 1992PNAS...89.2504L.
- "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. February 1995. doi:10.1016/0888-7543(95)80005-7. PMID 7759097.
- "Ca2+-dependent interaction of S100A2 with muscle and nonmuscle tropomyosins". Journal of Cell Science 110 ( Pt 5) (5): 611–21. March 1997. doi:10.1242/jcs.110.5.611. PMID 9092943.
- "Immunohistochemical localization of the Ca2+ binding S100 proteins in normal human skin and melanocytic lesions". The British Journal of Dermatology 137 (1): 39–43. July 1997. doi:10.1111/j.1365-2133.1997.tb03698.x. PMID 9274623.
- "A model for target protein binding to calcium-activated S100 dimers". FEBS Letters 421 (3): 175–9. January 1998. doi:10.1016/S0014-5793(97)01535-4. PMID 9468301.
- "Repression of the candidate tumor suppressor gene S100A2 in breast cancer is mediated by site-specific hypermethylation". Cell Calcium 22 (4): 243–54. October 1997. doi:10.1016/S0143-4160(97)90063-4. PMID 9481475.
- "Binding of Ca2+ and Zn2+ to human nuclear S100A2 and mutant proteins". The Journal of Biological Chemistry 273 (30): 18826–34. July 1998. doi:10.1074/jbc.273.30.18826. PMID 9668057.
- "Subcellular distribution of S100 proteins in tumor cells and their relocation in response to calcium activation". Histochemistry and Cell Biology 111 (6): 453–9. June 1999. doi:10.1007/s004180050381. PMID 10429967.
- "Mapping the zinc ligands of S100A2 by site-directed mutagenesis". The Journal of Biological Chemistry 275 (18): 13219–27. May 2000. doi:10.1074/jbc.275.18.13219. PMID 10788426.
- "S100 proteins in Corpora amylacea from normal human brain". Brain Research 867 (1–2): 280–8. June 2000. doi:10.1016/S0006-8993(00)02393-3. PMID 10837826.
- "Biochemical characterization of S100A2 in human keratinocytes: subcellular localization, dimerization, and oxidative cross-linking". The Journal of Investigative Dermatology 115 (3): 477–85. September 2000. doi:10.1046/j.1523-1747.2000.00078.x. PMID 10951287.
- "The Ca2+-binding S100A2 protein is differentially expressed in epithelial tissue of glandular or squamous origin". Histology and Histopathology 17 (1): 123–30. January 2002. doi:10.14670/HH-17.123. PMID 11813862.
- "Expression and prognostic significance of S100A2 protein in squamous cell carcinoma of the esophagus". Oncology Reports 9 (3): 503–10. 2002. doi:10.3892/or.9.3.503. PMID 11956617.
- "Differential responses of S100A2 to oxidative stress and increased intracellular calcium in normal, immortalized, and malignant human keratinocytes". The Journal of Investigative Dermatology 119 (5): 1196–201. November 2002. doi:10.1046/j.1523-1747.2002.19520.x. PMID 12445212.
- "Identification of S100A2 as a target of the DeltaNp63 oncogenic pathway". Clinical Cancer Research 9 (11): 4282–5. September 2003. PMID 14519656.
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