Synonyms
S100 Protein Family Members
S100A1, S100A2, S100A3, S100A4, S100A5, S100A6, S100A7, S100A8, S100A9, S100A10, S100A11, S100A12, S100A13, S100A14, S100A15, S100A16, S100B, S100P, S100G, S100Z, trichohylin, filaggrin, filaggrin-2, cornulin, repetin
Historical Background/General: S100 Family
S100 proteins were first discovered in 1965 by Moore as a major protein fraction (0.6% of total soluble protein) isolated from bovine brain (Moore 1965). The protein was given the name S100 due to its high solubility in saturated ammonium sulfate. Later experiments showed the S100 protein fraction constituted two different dimeric species comprised of two β protomers (S100B) or an α, β heterodimer (Isobe et al. 1977). Early members of the S100 protein family were frequently given suffixes based on their localization or molecular size and included S100P (placental), S100C (cardiac or calgizzarin), p11 (11 kDa), and MRP8/MRP14 (myeloid regulatory proteins, 8 and...
References
Bhattacharya S, Large E, Heizmann CW, Hemmings B, Chazin WJ. Structure of the Ca2+/S100B/NDR kinase peptide complex: insights into S100 target specificity and activation of the kinase. Biochemistry. 2003;42:14416–26.
Bhattacharya S, Bunick CG, Chazin WJ. Target selectivity in EF-hand calcium binding proteins. Biochim Biophys Acta. 2004;1742:69–79.
Donato R. S100: a multigenic family of calcium-modulated proteins of the EF-hand type with intracellular and extracellular functional roles. Int J Biochem Cell Biol. 2001;33:637–68.
Drohat AC, Baldisseri DM, Rustandi RR, Weber DJ. Solution structure of calcium-bound rat S100B (betabeta) as determined by nuclear magnetic resonance spectroscopy. Biochemistry. 1998;37:2729–40.
Engelkamp D, Schafer BW, Mattei MG, Erne P, Heizmann CW. 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. Proc Natl Acad Sci U S A. 1993;90:6547–51.
Gerke V, Moss SE. Annexins: from structure to function. Physiol Rev. 2002;82:331–71.
Harpio R, Einarsson R. S100 proteins as cancer biomarkers with focus on S100B in malignant melanoma. Clin Biochem. 2004;37:512–8.
Isobe T, Nakajima T, Okuyama T. Reinvestigation of extremely acidic proteins in bovine brain. Biochim Biophys Acta. 1977;494:222–32.
Liu Y, Buck DC, Neve KA. Novel interaction of the dopamine D2 receptor and the Ca2+ binding protein S100B: role in D2 receptor function. Mol Pharmacol. 2008;74:371–8.
Malik S, Revington M, Smith SP, Shaw GS. Analysis of the structure of human apo-S100B at low temperature indicates a unimodal conformational distribution is adopted by calcium-free S100 proteins. Proteins. 2008;73:28–42.
Marenholz I, Heizmann CW, Fritz G. S100 proteins in mouse and man: from evolution to function and pathology (including an update of the nomenclature). Biochem Biophys Res Commun. 2004;322:1111–22.
Moore BWA. soluble protein characteristic of the nervous system. Biochem Biophys Res Commun. 1965;19:739–44.
Murao S, Collart F, Huberman E. A protein complex expressed during terminal differentiation of monomyelocytic cells is an inhibitor of cell growth. Cell Growth Differ. 1990;1:447–54.
Odink K, Cerletti N, Bruggen J, Clerc RG, Tarcsay L, Zwadlo G, Gerhards G, Schlegel R, Sorg C. Two calcium-binding proteins in infiltrate macrophages of rheumatoid arthritis. Nature. 1987;330:80–2.
Potts BCM, Smith J, Akke M, Macke TJ, Okazaki K, Hidaka H, Case DA, Chazin WJ. The structure of calcyclin reveals a novel homodimeric fold for S100 Ca2+-binding proteins. Nat Struct Biol. 1995;2:790–6.
Sakaguchi M, Miyazaki M, Takaishi M, Sakaguchi Y, Makino E, Kataoka N, Yamada H, Namba M, Huh NH. S100C/A11 is a key mediator of Ca(2+)-induced growth inhibition of human epidermal keratinocytes. J Cell Biol. 2003;163:825–35.
Salama I, Malone PS, Mihaimeed F, Jones JL. A review of the S100 proteins in cancer. Eur J Surg Oncol. 2008;34:357–64.
Santamaria-Kisiel L, Rintala-Dempsey AC, Shaw GS. Calcium-dependent and -independent interactions of the S100 protein family. Biochem J. 2006;396:201–14.
Sorci G, Agneletti AL, Donato R. Effects of S100A1 and S100B on microtubule stability. An in vitro study using triton-cytoskeletons from astrocyte and myoblast cell lines. Neuroscience. 2000;99:773–783.
Treves S, Scutari E, Robert M, Groh S, Ottolia M, Prestipino G, Ronjat M, Zorzato F. Interaction of S100A1 with the Ca2+ release channel (ryanodine receptor) of skeletal muscle. Biochemistry. 1997;36:11496–503.
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Dempsey, B.R., Rintala-Dempsey, A.C., Shaw, G.S. (2012). S100 Proteins. In: Choi, S. (eds) Encyclopedia of Signaling Molecules. Springer, New York, NY. https://doi.org/10.1007/978-1-4419-0461-4_426
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DOI: https://doi.org/10.1007/978-1-4419-0461-4_426
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