S100A6 – focus on recent developments

References

Acosta, S., Mayol, G., Rodríguez, E., Lavarino, C., de Preter, K., Kumps, C., Garcia, I., de Torres, C., and Mora, J. (2011). Identification of tumoral glial precursor cells in neuroblastoma. Cancer Lett. 312, 73–81.10.1016/j.canlet.2011.08.004Search in Google Scholar PubMed

Bartkowska, K., Swiatek, I., Aniszewska, A., Jurewicz, E., Turlejski, K., Filipek, A., and Djavadian, R.L. (2017). Stress-dependent changes in the CacyBP/SIP interacting protein S100A6 in the mouse brain. PLoS One 12, e0169760.10.1371/journal.pone.0169760Search in Google Scholar PubMed PubMed Central

Belt, E.J., Fijneman, R.J., van den Berg, E.G., Bril, H., Delis-van Diemen, P.M., Tijssen, M., van Essen, H.F., de Lange-de Klerk, E.S., Belien, J.A., Stockmann, H.B,, et al. (2011). Loss of lamin A/C expression in stage II and III colon cancer is associated with disease recurrence. Eur. J. Cancer 47, 1837–1845.10.1016/j.ejca.2011.04.025Search in Google Scholar PubMed

Bresnick, A.R., Weber, D.J., and Zimmer, D.B. (2015). S100 proteins in cancer. Nat. Rev. Cancer 15, 96–109.10.1038/nrc3893Search in Google Scholar PubMed PubMed Central

Cai, X.Y., Lu, L., Wang, Y.N., Jin, C., Zhang, R.Y., Zhang, Q., Chen, Q.J., and Shen, W.F. (2011). Association of increased S100B, S100A6 and S100P in serum levels with acute coronary syndrome and also with the severity of myocardial infarction in cardiac tissue of rat models with ischemia-reperfusion injury. Atherosclerosis 217, 536–542.10.1016/j.atherosclerosis.2011.05.023Search in Google Scholar PubMed

Capra, E., Beretta, R., Parazzi, V., Viganò, M., Lazzari, L., Baldi, A., and Giordano, R. (2012). Changes in the proteomic profile of adipose tissue-derived mesenchymal stem cells during passages. Proteome Sci. 10, 46.10.1186/1477-5956-10-46Search in Google Scholar PubMed PubMed Central

Chen, H., Xu, C., Jin, Q., and Liu, Z. (2014). S100 protein family in human cancer. Am. J. Cancer Res. 4, 89–115.Search in Google Scholar

Chen, X., Liu, X., Lang, H., Zhang, S., Luo, Y., and Zhang, J. (2015). S100 calcium-binding protein A6 promotes epithelial-mesenchymal transition through β-catenin in pancreatic cancer cell line. PLoS One 10, e0121319.10.1371/journal.pone.0121319Search in Google Scholar PubMed PubMed Central

Deloulme, J.C., Assard, N., Mbele, G.O., Mangin, C., Kuwano, R., and Baudier, J. (2000). S100A6 and S100A11 are specific targets of the calcium- and zinc-binding S100B protein in vivo. J. Biol. Chem. 275, 35302–35310.10.1074/jbc.M003943200Search in Google Scholar PubMed

Donato, R., Cannon, B.R., Sorci, G., Riuzzi, F., Hsu, K., Weber, D.J., and Geczy, C.L. (2013). Functions of S100 proteins. Curr. Mol. Med. 13, 24–57.10.2174/156652413804486214Search in Google Scholar

Duan, L., Wu, R., Zou, Z., Wang, H., Ye, L., Li, H., Yuan, S., Li, X, Zha, H., Sun, H., et al. (2014). S100A6 stimulates proliferation and migration of colorectal carcinoma cells through activation of the MAPK pathways. Int. J. Oncol. 44, 781–790.10.3892/ijo.2013.2231Search in Google Scholar PubMed

Fernandez-Fernandez, M.R., Rutherford, T.J., and Fersht, A.R. (2008) Members of the S100 family bind p53 in two distinct ways. Protein Sci. 17, 1663–1670.10.1110/ps.035527.108Search in Google Scholar

Filipek, A., Heizmann, C.W., and Kuźnicki, J. (1990). Calcyclin is a calcium and zinc binding protein. FEBS Lett. 264, 263–266.10.1016/0014-5793(90)80263-ISearch in Google Scholar

Filipek, A., Michowski, W., and Kuznicki, J. (2008) Involvement of S100A6 (calcyclin) and its binding partners in intracellular signaling pathways. Adv. Enzyme Regul. 48, 225–239.10.1016/j.advenzreg.2007.11.001Search in Google Scholar PubMed

Fritz, G., Botelho, H.M., Morozova-Roche, L.A., and Gomes, C.M. (2010). Natural and amyloid self-assembly of S100 proteins: structural basis of functional diversity. FEBS J. 277, 4578–4590.10.1111/j.1742-4658.2010.07887.xSearch in Google Scholar PubMed

Góral, A., Bieganowski, P., Prus, W., Krzemień-Ojak Ł., Kądziołka, B., Fabczak, H., and Filipek, A. (2016). Calcyclin binding protein/Siah-1 interacting protein is a Hsp90 binding chaperone. PLoS One 11, e0156507.10.1371/journal.pone.0156507Search in Google Scholar PubMed PubMed Central

Graczyk, A., Słomnicki, L.P., and Leśniak, W. (2013). S100A6 competes with the TAZ2 domain of p300 for binding to p53 and attenuates p53 acetylation. J. Mol. Biol. 425, 3488–3494.10.1016/j.jmb.2013.06.007Search in Google Scholar PubMed

Graczyk, A. and Leśniak, W. (2014). S100A6 expression in keratinocytes and its impact on epidermal differentiation. Int. J. Biochem. Cell. Biol. 57, 135–141.10.1016/j.biocel.2014.10.007Search in Google Scholar PubMed

Gross, S.R., Sin, C.G., Barraclough, R., and Rudland, P.S. (2014). Joining S100 proteins and migration: for better or for worse, in sickness and in health. Cell. Mol. Life Sci. 71, 1551–1579.10.1007/s00018-013-1400-7Search in Google Scholar PubMed

Halawi, A., Abbas, O., and Mahalingam, M. (2014). S100 proteins and the skin: a review. J. Eur. Acad. Dermatol. Venereol. 28, 405–414.10.1111/jdv.12237Search in Google Scholar PubMed

Harris, M.A, Yang. H., Low, B.E., Mukherjee, J., Guha, A., Bronson, R.T., Shultz, L.D., Israel, M.A., and Yun, K. (2008). Cancer stem cells are enriched in the side population cells in a mouse model of glioma. Cancer Res. 68, 10051–10059.10.1158/0008-5472.CAN-08-0786Search in Google Scholar PubMed PubMed Central

Imbalzano, E., Mandraffino, G., Casciaro, M., Quartuccio, S., Saitta, A., and Gangemi, S. (2016). Pathophysiological mechanism and therapeutic role of S100 proteins in cardiac failure: a systematic review. Heart Fail. Rev. 21, 463–473.10.1007/s10741-016-9529-8Search in Google Scholar

Ismail, M.F., El Boghdady, N.A, Shabayek, M.I., Awida, H.A., and Abozeed, H. (2016). Evaluation and screening of mRNA S100A genes as serological biomarkers in different stages of bladder cancer in Egypt. Tumour Biol. 37, 4621–4631.10.1007/s13277-015-4264-7Search in Google Scholar

Ito, M. and Kizawa, K. (2001). Expression of calcium-binding S100 proteins A4 and A6 in regions of the epithelial sac associated with the onset of hair follicle regeneration. J. Invest. Dermatol. 116, 956–963.10.1046/j.0022-202x.2001.01369.xSearch in Google Scholar

Jeong, J.A., Hong, S.H., Gang, E.J., Ahn, C., Hwang, S.H., Yang, I.H, Han, H., and Kim H. (2005). Differential gene expression profiling of human umbilical cord blood-derived mesenchymal stem cells by DNA microarray. Stem Cells 23, 584–593.10.1634/stemcells.2004-0304Search in Google Scholar

Ji, Y.F., Hunag, H., Jiang, F., Ni, R.Z., and Xiao, M.B. (2014). S100 family signaling network and related proteins in pancreatic cancer. Int. J. Mol. Med. 33, 769–776.10.3892/ijmm.2014.1633Search in Google Scholar

Joo, J.H., Kim, J.W., Lee, Y, Yoon, S.Y., Kim, J.H., Paik, S.G., and Choe, I.S. (2003). Involvement of NF-κB in the regulation of S100A6 gene expression in human hepatoblastoma cell line HepG2. Biochem. Biophys. Res. Commun. 307, 274–280.10.1016/S0006-291X(03)01199-9Search in Google Scholar

Jurewicz, E., Kasacka, I., Bankowski, E., and Filipek, A. (2014a). S100A6 and its extracellular targets in Wharton’s jelly of healthy and preeclamptic patients. Placenta 35, 386–391.10.1016/j.placenta.2014.03.017Search in Google Scholar PubMed

Jurewicz, E., Góral, A., and Filipek, A. (2014b). S100A6 is secreted from Wharton’s jelly mesenchymal stem cells and interacts with integrin β1. Int. J. Biochem. Cell Biol. 55, 298–303.10.1016/j.biocel.2014.09.015Search in Google Scholar PubMed

Kanojia, D., Zhou, W., Zhang, J., Jie, C., Lo, P.K., Wang, Q., and Chen, H. (2012). Proteomic profiling of cancer stem cells derived from primary tumors of HER2/Neu transgenic mice. Proteomics 12, 3407–3415.10.1002/pmic.201200103Search in Google Scholar PubMed

Kilańczyk, E., Filipek, S., Jastrzebska, B., and Filipek, A. (2009) CacyBP/SIP binds ERK1/2 and affects transcriptional activity of Elk-1. Biochem. Biophys. Res. Commun. 380, 54–59.10.1016/j.bbrc.2009.01.026Search in Google Scholar PubMed

Kilańczyk, E., Graczyk, A., Ostrowska, H., Kasacka, I., Leśniak, W., and Filipek A. (2012). S100A6 is transcriptionally regulated by β-catenin and interacts with a novel target, lamin A/C, in colorectal cancer cells. Cell Calcium 51, 470–477.10.1016/j.ceca.2012.04.005Search in Google Scholar

Klein, L.L., Freitag, B.C., Gibbs, R.S., Reddy, A.P., Nagalla, S.R., and Gravett, M.G. (2005). Detection of intra-amniotic infection in a rabbit model by proteomics-based amniotic fluid analysis. Am. J. Obst. Gynecol. 193, 1302–1306.10.1016/j.ajog.2005.06.017Search in Google Scholar

Kuźnicki, J. and Filipek, A. (1987). Purification and properties of a novel Ca²⁺-binding protein (10.5 kDa) from Ehrlich-ascites-tumour cells. Biochem. J. 247, 663–667.10.1042/bj2470663Search in Google Scholar

Kuźnicki, J., Kordowska, J., Puzianowska, M., and Woźniewicz, B.M. (1992). Calcyclin as a marker of human epithelial cells and fibroblasts. Exp. Cell Res. 200, 425–430.10.1016/0014-4827(92)90191-ASearch in Google Scholar

Landi, C., Bargagli, E., Bianchi, L., Gagliardi, A, Carleo, A., Bennett, D., Perari, M.G., Armini, A., Prasse, A., Rottoli, P., et al. (2013). Towards a functional proteomics approach to the comprehension of idiopathic pulmonary fibrosis, sarcoidosis, systemic sclerosis and pulmonary Langerhans cell histiocytosis. J. Proteomics 83, 60–75.10.1016/j.jprot.2013.03.006Search in Google Scholar PubMed

Leclerc, E. and Vetter, S.W. (2015). The role of S100 proteins and their receptor RAGE in pancreatic cancer. Biochim. Biophys. Acta 1852, 2706–2711.10.1016/j.bbadis.2015.09.022Search in Google Scholar PubMed PubMed Central

Leclerc, E., Fritz, G., Vetter, S.W., and Heizmann, C.W. (2009). Binding of S100 proteins to RAGE: an update. Biochim. Biophys. Acta 1793, 993–1007.10.1016/j.bbamcr.2008.11.016Search in Google Scholar PubMed

Lee, Y.S., Chen, P.W., Tsai, P.J., Su, S.H., and Liao, P.C. (2006). Proteomics analysis revealed changes in rat bronchoalveolar lavage fluid proteins associated with oil mist exposure. Proteomics 6, 2236–2250.10.1002/pmic.200500347Search in Google Scholar PubMed

Lerchenmüller, C., Heißenberg, J., Damilano, F., Bezzeridis, V.J., Krämer, I., Bochaton-Piallat, M.L., Hirschberg, K., Busch, M., Katus, H.A., Peppel, K., et al. (2016). S100A6 regulates endothelial cell cycle progression by attenuating antiproliferative signal transducers and activators of transcription 1 signaling. Arterioscler. Thromb. Vasc. Biol. 36, 1854–1867.10.1161/ATVBAHA.115.306415Search in Google Scholar PubMed PubMed Central

Leśniak, W. and Filipek, A. (1996). Ca²⁺-dependent interaction of calcyclin with membrane. Biochem. Biophys. Res. Commun. 220, 269–273.10.1006/bbrc.1996.0394Search in Google Scholar PubMed

Leśniak, W. and Graczyk-Jarzynka, A. (2015). The S100 proteins in epidermis: topology and function. Biochim. Biophys. Acta 1850, 2563–2572.10.1016/j.bbagen.2015.09.015Search in Google Scholar

Leśniak, W., Jezierska, A., and Kuźnicki, J. (2000). Upstream stimulatory factor is involved in the regulation of the human calcyclin (S100A6) gene. Biochim. Biophys. Acta 1517, 73–81.10.1016/S0167-4781(00)00259-1Search in Google Scholar

Leśniak, W., Słomnicki, Ł.P., and Kuźnicki, J. (2007). Epigenetic control of the S100A6 (calcyclin) gene expression. J. Invest. Dermatol 127, 2307–2314.10.1038/sj.jid.5700879Search in Google Scholar PubMed

Leśniak, W., Słomnicki, Ł.P., and Filipek, A. (2009). S100A6 – new facts and features. Biochem. Biophys. Res. Commun. 390, 1087–1092.10.1016/j.bbrc.2009.10.150Search in Google Scholar PubMed

Li, Z., Tang, M., Ling, B., Liu, S., Zheng, Y., Nie, C., Yuan, Z., Zhou, L., Guo, G., Tong, A., et al. (2014). Increased expression of S100A6 promotes cell proliferation and migration in human hepatocellular carcinoma. J. Mol. Med. (Berl) 92, 291–303.10.1007/s00109-013-1104-3Search in Google Scholar PubMed

Li, Y., Wagner, E.R., Yan, Z., Wang, Z., Luther, G., Jiang, W., Ye, J., Wei, Q., Wang, J., Zhao, L., et al. (2015). The calcium-binding protein S100A6 accelerates human osteosarcoma growth by promoting cell proliferation and inhibiting osteogenic differentiation. Cell. Physiol. Biochem. 37, 2375–2392.10.1159/000438591Search in Google Scholar PubMed

Li, A, Shi, D., Xu, B., Wang, J., Tang, Y.L., Xiao, W., Shen, G., Deng, W., and Zhao, C. (2017). S100A6 promotes cell proliferation in human nasopharyngeal carcinoma via the p38/MAPK signaling pathway. Mol. Carcinog. 56, 972–984.10.1002/mc.22563Search in Google Scholar PubMed

Liu, Z., Zhang, X., Chen, M., Cao, Q., and Huang, D. (2015). Effect of S100A6 over-expression on β-catenin in endometriosis. J. Obstet. Gynaecol. Res. 41, 1457–1462.10.1111/jog.12729Search in Google Scholar PubMed

Ludvigsen, M., Jacobsen, C., Maunsbach, A.B., and Honoré, B. (2009). Identification and characterization of novel ERC-55 interacting proteins: evidence for the existence of several ERC-55 splicing variants; including the cytosolic ERC-55-C. Proteomics 9, 5267–5287.10.1002/pmic.200900321Search in Google Scholar PubMed

Maletzki, C., Bodammer, P., Breitrück, A., and Kerkhoff C. (2012). S100 proteins as diagnostic and prognostic markers in colorectal and hepatocellular carcinoma. Hepat. Mon. 12, e7240.10.5812/hepatmon.7240Search in Google Scholar PubMed PubMed Central

Mignone, J.L., Roig-Lopez, J.L, Fedtsova, N., Schones, D.E., Manganas, L.N., Maletic-Savatic, M., Keyes, W.M., Mills, A.A., Gleiberman, A., Zhang, M.Q., et al. (2007). Neural potential of a stem cell population in the hair follicle. Cell Cycle 6, 2161–2170.10.4161/cc.6.17.4593Search in Google Scholar

Moravkova, P., Kohoutova, D., Rejchrt, S., Cyrany, J., and Bures, J. (2016). Role of S100 proteins in colorectal, carcinogenesis. Gastroenterol. Res. Pract. 2016, 2632703.10.1155/2016/2632703Search in Google Scholar

Moroz, O.V., Wilson, K.S., and Bronstein, I.B. (2011). The role of zinc in the S100 proteins: insights from the X-ray structures. Amino Acids 41, 761–772.10.1007/s00726-010-0540-4Search in Google Scholar

Nishi, M., Matsumoto, K., Kobayashi, M., Yanagita, K., Matsumoto, T., Nagashio, R., Ishii, D., Fujita, T., Sato, Y., and Iwamura, M. (2014). Serum expression of S100A6 is a potential detection marker in patients with urothelial carcinoma in the urinary bladder. Biomed. Res. 35, 351–356.10.2220/biomedres.35.351Search in Google Scholar

Ouji, Y., Yoshikawa, M., Nishiofuku, M., Ouji-Sageshima, N., Kubo, A., and Ishizaka, S. (2010). Effects of Wnt-10b on proliferation and differentiation of adult murine skin-derived CD34 and CD49f double-positive cells. J. Biosci. Bioeng. 110, 2217–2122.10.1016/j.jbiosc.2010.01.020Search in Google Scholar

Patgaonkar, M., Aranha, C., Bhonde, G., and Reddy, K.V. (2011). Identification and characterization of anti-microbial peptides from rabbit vaginal fluid. Vet. Immunol. Immunopathol. 139, 176–186.10.1016/j.vetimm.2010.10.012Search in Google Scholar

Persson, A.I., Petritsch, C., Swartling, F.J., Itsara, M., Sim, F.J., Auvergne, R., Goldenberg, D.D., Vandenberg, S.R., Nguyen, K.N., Yakovenko, S., et al. (2010). Non-stem cell origin for oligodendroglioma. Cancer Cell 18, 669–682.10.1016/j.ccr.2010.10.033Search in Google Scholar

Rehman, I., Cross, S.S., Catto, J.W., Leiblich, A., Mukherjee, A., Azzouzi, A.R., Leung, H.Y., and Hamdy, F.C. (2005). Promoter hyper-methylation of calcium binding proteins S100A6 and S100A2 in human prostate cancer. Prostate 65, 322–330.10.1002/pros.20302Search in Google Scholar

Rijsewijk, F., Schuermann, M., Wagenaar, E., Parren, P., Weigel, D., and Nusse, R. (1987). The Drosophila homolog of the mouse mammary oncogene int-1 is identical to the segment polarity gene wingless. Cell 50, 649–657.10.1016/0092-8674(87)90038-9Search in Google Scholar

Sastry, M., Ketchem, R.R., Crescenzi, O., Weber, C., Lubienski, M.J., Hidaka, H., and Chazin, W.J. (1998). The three-dimensional structure of Ca²⁺-bound calcyclin: implications for Ca²⁺-signal transduction by S100 proteins. Structure 6, 223–231.10.1016/S0969-2126(98)00023-9Search in Google Scholar

Sbroggiò, M., Ferretti, R., Percivalle, E., Gutkowska, M., Zylicz, A., Michowski, W., Kuznick,i J., Accornero, F., Pacchioni, B., Lanfranchi, G., et al. (2008) The mammalian CHORD-containing protein melusin is a stress response protein interacting with Hsp90 and Sgt1. FEBS Lett. 582, 1788–1794.10.1016/j.febslet.2008.04.058Search in Google Scholar

Shimamoto, S., Takata, M., Tokuda, M., Oohira, F., Tokumitsu, H., and Kobayashi, R. (2008) Interactions of S100A2 and S100A6 with the tetratricopeptide repeat proteins, Hsp90/Hsp70-organizing protein and kinesin light chain. J. Biol. Chem. 283, 28246–28258.10.1074/jbc.M801473200Search in Google Scholar

Shimamoto, S., Kubota, Y., Tokumitsu, H., and Kobayashi, R. (2010). S100 proteins regulate the interaction of Hsp90 with cyclophilin 40 and FKBP52 through their tetratricopeptide repeats. FEBS Lett. 584, 1119–1125.10.1016/j.febslet.2010.02.055Search in Google Scholar

Shimamoto, S., Tsuchiya, M., Yamaguchi, F., Kubota, Y., Tokumitsu, H., and Kobayashi, R. (2014). Ca²⁺/S100 proteins inhibit the interaction of FKBP38 with Bcl-2 and Hsp90. Biochem. J. 458, 141–152.10.1042/BJ20130924Search in Google Scholar

Słomnicki, Ł.P., Nawrot, B., and Leśniak, W. (2009) S100A6 binds p53 and affects its activity. Int. J. Biochem. Cell Biol. 41, 784–790.10.1016/j.biocel.2008.08.007Search in Google Scholar

Spiechowicz, M., Zylicz, A., Bieganowski, P., Kuznicki, J., and Filipek, A. (2007). Hsp70 is a new target of Sgt1 – an interaction modulated by S100A6. Biochem. Biophys. Res. Commun. 357, 1148–1153.10.1016/j.bbrc.2007.04.073Search in Google Scholar

Stradal, T.B. and Gimona, M. (1999). Ca²⁺-dependent association of S100A6 (Calcyclin) with the plasma membrane and the nuclear envelope. J. Biol. Chem. 274, 31593–31596.10.1074/jbc.274.44.31593Search in Google Scholar

Takata, M., Shimamoto, S., Yamaguchi, F., Tokuda, M., Tokumitsu, H., and Kobayashi, R. (2010). Regulation of nuclear localization signal-importin α interaction by Ca²⁺/S100A6. FEBS Lett. 584, 4517–4523.10.1016/j.febslet.2010.09.052Search in Google Scholar

Taylor, G., Lehrer, M.S., Jensen, P.J., Sun, T.T., and Lavker, R.M. (2000). Involvement of follicular stem cells in forming not only the follicle but also the epidermis. Cell 102, 451–461.10.1016/S0092-8674(00)00050-7Search in Google Scholar

van Dieck, J., Brandt, T., Teufel, D.P., Veprintsev, D.B., Joerger, A.C., and Fersht, A.R. (2010a). Molecular basis of S100 proteins interacting with the p53 homologs p63 and p73. Oncogene 29, 2024–2035.10.1038/onc.2009.490Search in Google Scholar PubMed

van Dieck, J., Lum, J.K., Teufel, D.P., and Fersht, A.R. (2010b). S100 proteins interact with the N-terminal domain of MDM2. FEBS Lett. 584, 3269–3274.10.1016/j.febslet.2010.06.024Search in Google Scholar PubMed

Wang, T., Liang, Y., Thakur, A., Zhang, S., Yang, T., Chen, T., Gao, L., Chen, M., and Ren, H. (2016). Diagnostic significance of S100A2 and S100A6 levels in sera of patients with non-small cell lung cancer. Tumour Biol. 37, 2299–2304.10.1007/s13277-015-4057-zSearch in Google Scholar PubMed

Wasik, U., Kadziolka, B., Kilanczyk, E., and Filipek, A. (2016) Influence of S100A6 on CacyBP/SIP phosphorylation and Elk-1 transcriptional activity in neuroblastoma NB2a cells. J. Cell Biochem. 117, 126–131.10.1002/jcb.25257Search in Google Scholar PubMed

Wei, B.R., Hoover, S,B,, Ross, M.M., Zhou, W., Meani, F., Edwards, J.B., Spehalski, E.I., Risinger, J.I., Alvord, W.G., Quiñones, O.A., et al. (2009). Serum S100A6 concentration predicts peritoneal tumor burden in mice with epithelial ovarian cancer and is associated with advanced stage in patients. PLoS One 4, e7670.10.1371/journal.pone.0007670Search in Google Scholar PubMed PubMed Central

Willis, N.D., Cox, T.R., Rahman-Casans, S.F., Smith, K., Przyborski, S.A., van den Brandt, P., van Engeland, M., Weijenberg, M., Wilson, R.G., de Bruine, A., et al. (2008). Lamin A/C is a risk biomarker in colorectal cancer. PLoS One 3, e2988.10.1371/journal.pone.0002988Search in Google Scholar PubMed PubMed Central

Yamada, J. and Jinno, S. (2014). S100A6 (calcyclin) is a novel marker of neural stem cells and astrocyte precursors in the subgranular zone of the adult mouse hippocampus. Hippocampus 24, 89–101.10.1002/hipo.22207Search in Google Scholar PubMed

Yamaguchi, F., Umeda, Y., Shimamoto, S., Tsuchiya, M., Tokumitsu, H., Tokuda, M., and Kobayashi, R. (2012). S100 proteins modulate protein phosphatase 5 function: a link between Ca²⁺ signal transduction and protein dephosphorylation. J. Biol. Chem. 287, 13787–13798.10.1074/jbc.M111.329771Search in Google Scholar PubMed PubMed Central

Yamaguchi, F., Yamamura, S., Shimamoto, S., Tokumitsu, H., Tokuda, M., and Kobayashi, R. (2014). Suramin is a novel activator of PP5 and biphasically modulates S100-activated PP5 activity. Appl. Biochem. Biotechnol. J172, 237–247.10.1007/s12010-013-0522-6Search in Google Scholar PubMed

Yammani, R.R. (2012). S100 proteins in cartilage: role in arthritis. Biochim. Biophys. Acta 1822, 600–606.10.1016/j.bbadis.2012.01.006Search in Google Scholar PubMed PubMed Central

Yang, Q., O’Hanlon, D., Heizmann, C.W., and Marks, A. (1999). Demonstration of heterodimer formation between S100B and S100A6 in the yeast two-hybrid system and human melanoma. Exp. Cell Res. 246, 501–509.10.1006/excr.1998.4314Search in Google Scholar PubMed

Yatime, L., Betzer, C., Jensen, R.K., Mortensen, S., Jensen, P.H., and Andersen, G.R. (2016). The structure of the RAGE:S100A6 complex reveals a unique mode of homodimerization for S100 proteins. Structure 24, 2043–2052.10.1016/j.str.2016.09.011Search in Google Scholar PubMed

Zackular, J.P., Chazin, W.J., and Skaar, E.P. (2015). Nutritional immunity: S100 proteins at the host-pathogen interface. J. Biol. Chem. 290, 18991–18998.10.1074/jbc.R115.645085Search in Google Scholar PubMed PubMed Central

Zhang, S.P., Wu, Z.Z., Wu, Y.W., Su, S.B., and Tong J. (2010). [Mechanism study of adaptive response in high background radiation area of Yangjiang in China]. Zhonghua Yu Fang Yi Xue Za Zhi 44, 815–819.Search in Google Scholar

Zhang, J., Zhang, K., Jiang, X., and Zhang, J. (2014). S100A6 as a potential serum prognostic biomarker and therapeutic target in gastric cancer. Digest. Dis. Sci. 59, 2136–2144.10.1007/s10620-014-3137-zSearch in Google Scholar PubMed