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S100 calcium binding protein B

PDB rendering based on 1b4c.
Available structures
1b4c, 1cfp, 1dt7, 1mho, 1mq1, 1mwn, 1psb, 1qlk, 1sym, 1uwo, 1xyd, 2h61
Identifiers
Symbols S100B; S100; NEF; S100beta
External IDs OMIM176990 MGI98217 HomoloGene4567 GeneCards: S100B Gene
RNA expression pattern
PBB GE S100B 209686 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 6285 20203
Ensembl ENSG00000160307 ENSMUSG00000033208
UniProt P04271 Q3UY00
RefSeq (mRNA) NM_006272 NM_009115
RefSeq (protein) NP_006263 NP_033141
Location (UCSC) Chr 21:
46.84 - 46.85 Mb
Chr 10:
75.7 - 75.7 Mb
PubMed search [1] [2]

S100 calcium binding protein B or S100B is a protein of the S-100 protein family.

S100 proteins are localized in the cytoplasm and 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; however, this gene is located at 21q22.3.

S100B is glial-specific and is expressed primarily by astrocytes. Unfortunately not all astrocytes express S100B. It was shown that S100B is only expressed by a subtype of mature astrocytes that ensheath blood vessels and by NG2-expressing cells.

This protein may function in neurite extension, proliferation of melanoma cells, stimulation of Ca2+ fluxes, inhibition of PKC-mediated phosphorylation, astrocytosis and axonal proliferation, and inhibition of microtubule assembly. In the developing CNS it acts as a neurotrophic factor and neuronal survival protein. In the adult organism it is usually elevated due to nervous system damage, which makes it a potential clinical marker.

Chromosomal rearrangements and altered expression of this gene have been implicated in several neurological, neoplastic, and other types of diseases, including Alzheimer's disease, Down's syndrome, epilepsy, amyotrophic lateral sclerosis, melanoma, and type I diabetes.[1]

Interactions

S100B has been shown to interact with S100A11,[2] IQGAP1,[3] S100 calcium binding protein A1,[4][2][5] Tau protein,[6][7] S100A6,[2][5] PGM1,[8] VAV1,[9] AHNAK[10] and P53.[11]

References

  1. ^ "Entrez Gene: S100B S100 calcium binding protein B". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6285.  
  2. ^ a b c Deloulme, J C; Assard N, Mbele G O, Mangin C, Kuwano R, Baudier J (Nov. 2000). "S100A6 and S100A11 are specific targets of the calcium- and zinc-binding S100B protein in vivo". J. Biol. Chem. (UNITED STATES) 275 (45): 35302–10. doi:10.1074/jbc.M003943200. ISSN 0021-9258. PMID 10913138.  
  3. ^ Mbele, Gaelh Ouengue; Deloulme Jean Christophe, Gentil Benoît Jean, Delphin Christian, Ferro Myriam, Garin Jérôme, Takahashi Miyoko, Baudier Jacques (Dec. 2002). "The zinc- and calcium-binding S100B interacts and co-localizes with IQGAP1 during dynamic rearrangement of cell membranes". J. Biol. Chem. (United States) 277 (51): 49998–50007. doi:10.1074/jbc.M205363200. ISSN 0021-9258. PMID 12377780.  
  4. ^ Rual, Jean-François; Venkatesan Kavitha, Hao Tong, Hirozane-Kishikawa Tomoko, Dricot Amélie, Li Ning, Berriz Gabriel F, Gibbons Francis D, Dreze Matija, Ayivi-Guedehoussou Nono, Klitgord Niels, Simon Christophe, Boxem Mike, Milstein Stuart, Rosenberg Jennifer, Goldberg Debra S, Zhang Lan V, Wong Sharyl L, Franklin Giovanni, Li Siming, Albala Joanna S, Lim Janghoo, Fraughton Carlene, Llamosas Estelle, Cevik Sebiha, Bex Camille, Lamesch Philippe, Sikorski Robert S, Vandenhaute Jean, Zoghbi Huda Y, Smolyar Alex, Bosak Stephanie, Sequerra Reynaldo, Doucette-Stamm Lynn, Cusick Michael E, Hill David E, Roth Frederick P, Vidal Marc (Oct. 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature (England) 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.  
  5. ^ a b Yang, Q; O'Hanlon D, Heizmann C W, Marks A (Feb. 1999). "Demonstration of heterodimer formation between S100B and S100A6 in the yeast two-hybrid system and human melanoma". Exp. Cell Res. (UNITED STATES) 246 (2): 501–9. doi:10.1006/excr.1998.4314. ISSN 0014-4827. PMID 9925766.  
  6. ^ Yu, W H; Fraser P E (Apr. 2001). "S100beta interaction with tau is promoted by zinc and inhibited by hyperphosphorylation in Alzheimer's disease". J. Neurosci. (United States) 21 (7): 2240–6. PMID 11264299.  
  7. ^ Baudier, J; Cole R D (Apr. 1988). "Interactions between the microtubule-associated tau proteins and S100b regulate tau phosphorylation by the Ca2+/calmodulin-dependent protein kinase II". J. Biol. Chem. (UNITED STATES) 263 (12): 5876–83. ISSN 0021-9258. PMID 2833519.  
  8. ^ Landar, A; Caddell G, Chessher J, Zimmer D B (Sep. 1996). "Identification of an S100A1/S100B target protein: phosphoglucomutase". Cell Calcium (SCOTLAND) 20 (3): 279–85. ISSN 0143-4160. PMID 8894274.  
  9. ^ Fackler, O T; Luo W, Geyer M, Alberts A S, Peterlin B M (Jun. 1999). "Activation of Vav by Nef induces cytoskeletal rearrangements and downstream effector functions". Mol. Cell (UNITED STATES) 3 (6): 729–39. ISSN 1097-2765. PMID 10394361.  
  10. ^ Gentil, B J; Delphin C, Mbele G O, Deloulme J C, Ferro M, Garin J, Baudier J (Jun. 2001). "The giant protein AHNAK is a specific target for the calcium- and zinc-binding S100B protein: potential implications for Ca2+ homeostasis regulation by S100B". J. Biol. Chem. (United States) 276 (26): 23253–61. doi:10.1074/jbc.M010655200. ISSN 0021-9258. PMID 11312263.  
  11. ^ Lin, Jing; Yang Qingyuan, Yan Zhe, Markowitz Joseph, Wilder Paul T, Carrier France, Weber David J (Aug. 2004). "Inhibiting S100B restores p53 levels in primary malignant melanoma cancer cells". J. Biol. Chem. (United States) 279 (32): 34071–7. doi:10.1074/jbc.M405419200. ISSN 0021-9258. PMID 15178678.  

Further reading

  • Schäfer BW, Heizmann CW (1996). "The S100 family of EF-hand calcium-binding proteins: functions and pathology.". Trends Biochem. Sci. 21 (4): 134–40. PMID 8701470.  
  • Garbuglia M, Verzini M, Sorci G, et al. (2000). "The calcium-modulated proteins, S100A1 and S100B, as potential regulators of the dynamics of type III intermediate filaments.". Braz. J. Med. Biol. Res. 32 (10): 1177–85. PMID 10510252.  
  • Rothermundt M, Peters M, Prehn JH, Arolt V (2003). "S100B in brain damage and neurodegeneration.". Microsc. Res. Tech. 60 (6): 614–32. doi:10.1002/jemt.10303. PMID 12645009.  
  • Michetti F, Gazzolo D (2004). "S100B testing in pregnancy.". Clin. Chim. Acta 335 (1-2): 1–7. doi:10.1016/S0009-8981(03)00243-2. PMID 12927678.  
  • Raabe A, Kopetsch O, Woszczyk A, et al. (2004). "Serum S-100B protein as a molecular marker in severe traumatic brain injury.". Restor. Neurol. Neurosci. 21 (3-4): 159–69. PMID 14530578.  
  • Sen J, Belli A (2007). "S100B in neuropathologic states: the CRP of the brain?". J. Neurosci. Res. 85 (7): 1373–80. doi:10.1002/jnr.21211. PMID 17348038.  
  • Morii K, Tanaka R, Takahashi Y, et al. (1991). "Structure and chromosome assignment of human S100 alpha and beta subunit genes.". Biochem. Biophys. Res. Commun. 175 (1): 185–91. doi:10.1016/S0006-291X(05)81218-5. PMID 1998503.  
  • Allore RJ, Friend WC, O'Hanlon D, et al. (1990). "Cloning and expression of the human S100 beta gene.". J. Biol. Chem. 265 (26): 15537–43. PMID 2394738.  
  • Duncan AM, Higgins J, Dunn RJ, et al. (1989). "Refined sublocalization of the human gene encoding the beta subunit of the S100 protein (S100B) and confirmation of a subtle t(9;21) translocation using in situ hybridization.". Cytogenet. Cell Genet. 50 (4): 234–5. doi:10.1159/000132767. PMID 2530061.  
  • Baudier J, Cole RD (1988). "Interactions between the microtubule-associated tau proteins and S100b regulate tau phosphorylation by the Ca2+/calmodulin-dependent protein kinase II.". J. Biol. Chem. 263 (12): 5876–83. PMID 2833519.  
  • Allore R, O'Hanlon D, Price R, et al. (1988). "Gene encoding the beta subunit of S100 protein is on chromosome 21: implications for Down syndrome.". Science 239 (4845): 1311–3. doi:10.1126/science.2964086. PMID 2964086.  
  • Jensen R, Marshak DR, Anderson C, et al. (1985). "Characterization of human brain S100 protein fraction: amino acid sequence of S100 beta.". J. Neurochem. 45 (3): 700–5. doi:10.1111/j.1471-4159.1985.tb04048.x. PMID 4031854.  
  • Baudier J, Glasser N, Haglid K, Gerard D (1984). "Purification, characterization and ion binding properties of human brain S100b protein.". Biochim. Biophys. Acta 790 (2): 164–73. PMID 6487634.  
  • Adams MD, Kerlavage AR, Fleischmann RD, et al. (1995). "Initial assessment of human gene diversity and expression patterns based upon 83 million nucleotides of cDNA sequence.". Nature 377 (6547 Suppl): 3–174. PMID 7566098.  
  • Schäfer BW, Wicki R, Engelkamp D, et al. (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. PMID 7759097.  
  • Reeves RH, Yao J, Crowley MR, et al. (1994). "Astrocytosis and axonal proliferation in the hippocampus of S100b transgenic mice.". Proc. Natl. Acad. Sci. U.S.A. 91 (12): 5359–63. doi:10.1073/pnas.91.12.5359. PMID 8202493.  
  • Engelkamp D, Schäfer BW, Mattei MG, et al. (1993). "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. 90 (14): 6547–51. doi:10.1073/pnas.90.14.6547. PMID 8341667.  
  • Peña LA, Brecher CW, Marshak DR (1997). "beta-Amyloid regulates gene expression of glial trophic substance S100 beta in C6 glioma and primary astrocyte cultures.". Brain Res. Mol. Brain Res. 34 (1): 118–26. doi:10.1016/0169-328X(95)00145-I. PMID 8750867.  
  • Landar A, Caddell G, Chessher J, Zimmer DB (1997). "Identification of an S100A1/S100B target protein: phosphoglucomutase.". Cell Calcium 20 (3): 279–85. doi:10.1016/S0143-4160(96)90033-0. PMID 8894274.  

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

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