S100B

From Wikipedia, the free encyclopedia

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

Symbol(s)

S100B; S100; NEF; S100beta

External IDs

OMIM: 176990 MGI: 98217 HomoloGene: 4567

Gene ontology
Molecular Function:	• calcium ion binding • zinc ion binding • kinase inhibitor activity • protein homodimerization activity • S100 beta binding • tau protein binding • calcium-dependent protein binding
Cellular Component:	• ruffle • extracellular region • nucleus • cytoplasm • cell soma
Biological Process:	• energy reserve metabolic process • cellular calcium ion homeostasis • induction of apoptosis • axonogenesis • central nervous system development • memory • cell proliferation • regulation of cytokine biosynthetic process • positive regulation of complement activation • astrocyte activation • hyperphosphorylation • regulation of long-term neuronal synaptic plasticity

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_006272 (mRNA)
NP_006263 (protein)

NM_009115 (mRNA)
NP_033141 (protein)

Location

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. 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]

[edit] References

^ Entrez Gene: S100B S100 calcium binding protein B.

[edit] 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. 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. 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. 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. 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. 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. 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. 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. 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. 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. PMID 8894274.