The protein encoded by this gene 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.[3] S100A11 is localized in the cytoplasm of resting human keratinocytes in vitro.[4]
S100A11, along with all 13 members of the S100 family, are located as a cluster on chromosome 1q21. The protein may function in motility, invasion, and tubulin polymerization. Chromosomal rearrangements and altered expression of this gene have been implicated in tumor metastasis.[2]
Suppression of S100A11 by small interfering RNA caused cells to apoptosis, and overexpression of S100A11 has been found to inhibit apoptosis in tumor cells.[5] Furthermore, the knock-down of S100A11 via siRNA reduces the sister-chromatid exchange and the viability of cells.
IL-8 and TNF-alpha induce S100A11 expression and release in chondrocytes in culture and exogenous S100A11 causes chondrocyte hypertrophy.[6]
It has been shown that S100A11 enhances the recombination activity of human RAD51in vitro. A knock-down leads to diffuse distribution of RAD54B.[7] These finding suggest a potential role of S100A11 in the process of homologous recombination repair of double-strand breaks.[8]
↑Wicki R, Marenholz I, Mischke D, Schäfer BW, Heizmann CW (December 1996). "Characterization of the human S100A12 (calgranulin C, p6, CAAF1, CGRP) gene, a new member of the S100 gene cluster on chromosome 1q21". Cell Calcium. 20 (6): 459–64. doi:10.1016/S0143-4160(96)90087-1. PMID8985590.
↑Sakaguchi M, Huh NH (October 2011). "S100A11, a dual growth regulator of epidermal keratinocytes". Amino Acids. 41 (4): 797–807. doi:10.1007/s00726-010-0747-4. PMID20872027.
↑Kanamori T, Takakura K, Mandai M, Kariya M, Fukuhara K, Sakaguchi M, Huh NH, Saito K, Sakurai T, Fujita J, Fujii S (October 2004). "Increased expression of calcium-binding protein S100 in human uterine smooth muscle tumours". Molecular Human Reproduction. 10 (10): 735–42. doi:10.1093/molehr/gah100. PMID15322223.
↑Cecil DL, Johnson K, Rediske J, Lotz M, Schmidt AM, Terkeltaub R (December 2005). "Inflammation-induced chondrocyte hypertrophy is driven by receptor for advanced glycation end products". Journal of Immunology. 175 (12): 8296–302. doi:10.4049/jimmunol.175.12.8296. PMID16339570.
↑Deloulme JC, Assard N, Mbele GO, Mangin C, Kuwano R, Baudier J (November 2000). "S100A6 and S100A11 are specific targets of the calcium- and zinc-binding S100B protein in vivo". The Journal of Biological Chemistry. 275 (45): 35302–10. doi:10.1074/jbc.M003943200. PMID10913138.
Further reading
Rasmussen HH, van Damme J, Puype M, Gesser B, Celis JE, Vandekerckhove J (December 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. PMID1286667.
Tomasetto C, Régnier C, Moog-Lutz C, Mattei MG, Chenard MP, Lidereau R, Basset P, Rio MC (August 1995). "Identification of four novel human genes amplified and overexpressed in breast carcinoma and localized to the q11-q21.3 region of chromosome 17". Genomics. 28 (3): 367–76. doi:10.1006/geno.1995.1163. PMID7490069.
Schäfer BW, Wicki R, Engelkamp D, Mattei MG, Heizmann CW (February 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. PMID7759097.
Tanaka M, Adzuma K, Iwami M, Yoshimoto K, Monden Y, Itakura M (March 1995). "Human calgizzarin; one colorectal cancer-related gene selected by a large scale random cDNA sequencing and northern blot analysis". Cancer Letters. 89 (2): 195–200. doi:10.1016/0304-3835(94)03687-E. PMID7889529.
Mailliard WS, Haigler HT, Schlaepfer DD (January 1996). "Calcium-dependent binding of S100C to the N-terminal domain of annexin I". The Journal of Biological Chemistry. 271 (2): 719–25. doi:10.1074/jbc.271.2.719. PMID8557678.
Inada H, Naka M, Tanaka T, Davey GE, Heizmann CW (September 1999). "Human S100A11 exhibits differential steady-state RNA levels in various tissues and a distinct subcellular localization". Biochemical and Biophysical Research Communications. 263 (1): 135–8. doi:10.1006/bbrc.1999.1319. PMID10486266.
Réty S, Osterloh D, Arié JP, Tabaries S, Seeman J, Russo-Marie F, Gerke V, Lewit-Bentley A (February 2000). "Structural basis of the Ca(2+)-dependent association between S100C (S100A11) and its target, the N-terminal part of annexin I". Structure. 8 (2): 175–84. doi:10.1016/S0969-2126(00)00093-9. PMID10673436.
Deloulme JC, Assard N, Mbele GO, Mangin C, Kuwano R, Baudier J (November 2000). "S100A6 and S100A11 are specific targets of the calcium- and zinc-binding S100B protein in vivo". The Journal of Biological Chemistry. 275 (45): 35302–10. doi:10.1074/jbc.M003943200. PMID10913138.
Ruse M, Lambert A, Robinson N, Ryan D, Shon KJ, Eckert RL (March 2001). "S100A7, S100A10, and S100A11 are transglutaminase substrates". Biochemistry. 40 (10): 3167–73. doi:10.1021/bi0019747. PMID11258932.
Bianchi R, Giambanco I, Arcuri C, Donato R (April 2003). "Subcellular localization of S100A11 (S100C) in LLC-PK1 renal cells: Calcium- and protein kinase c-dependent association of S100A11 with S100B and vimentin intermediate filaments". Microscopy Research and Technique. 60 (6): 639–51. doi:10.1002/jemt.10305. PMID12645011.
Mori M, Shimada H, Gunji Y, Matsubara H, Hayashi H, Nimura Y, Kato M, Takiguchi M, Ochiai T, Seki N (June 2004). "S100A11 gene identified by in-house cDNA microarray as an accurate predictor of lymph node metastases of gastric cancer". Oncology Reports. 11 (6): 1287–93. doi:10.3892/or.11.6.1287. PMID15138568.