S100B

S100B
Gene ontology
Molecular function	calcium ion binding S100 protein binding protein homodimerization activity zinc ion binding metal ion binding calcium-dependent protein binding protein binding identical protein binding tau protein binding signaling receptor binding RAGE receptor binding
Cellular component	cytoplasm ruffle extracellular region neuronal cell body perinuclear region of cytoplasm nucleus extracellular space
Biological process	axonogenesis response to glucocorticoid memory negative regulation of skeletal muscle cell differentiation central nervous system development astrocyte differentiation positive regulation of synaptic transmission positive regulation of cell population proliferation regulation of cell shape positive regulation of apoptotic process learning or memory positive regulation of I-kappaB kinase/NF-kappaB signaling regulation of neuronal synaptic plasticity response to methylmercury cell population proliferation innate immune response cellular response to hypoxia long-term potentiation positive regulation of myelination
Sources:Amigo / QuickGO

Ensembl				ENSG00000160307	ENSMUSG00000033208
UniProt	P04271	P50114
RefSeq (mRNA)	NM_006272	NM_009115
RefSeq (protein)	NP_006263	NP_033141
Location (UCSC)	Chr 21: 46.6 – 46.61 Mb	Chr 10: 76.09 – 76.1 Mb
PubMed search	[3]	[4]

Wikidata

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S100 calcium-binding protein B (S100B) is a protein of the S100 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.

Function

S100B is glial-specific and is expressed primarily by astrocytes, but not all astrocytes express S100B. It has been shown that S100B is only expressed by a subtype of mature astrocytes that ensheath blood vessels and by NG2-expressing cells.^[5]

This protein may function in

and neuronal survival protein. In the adult organism it is usually elevated due to nervous system damage, which makes it a potential clinical marker.

Clinical significance

It has been suggested that the regulation of S100B by melittin has potential for the treatment of epilepsy.^[7]

Diagnostic use

S100B is secreted by astrocytes or can spill from injured cells and enter the extracellular space or bloodstream. Serum levels of S100B increase in patients during the acute phase of brain damage. Over the last decade, S100B has emerged as a candidate peripheral biomarker of

). However, more importantly, S100B levels have been reported to rise prior to any detectable changes in intracerebral pressure, neuroimaging, and neurological examination findings. Thus, the major advantage of using S100B is that elevations in serum or CSF levels provide a sensitive measure for determining CNS injury at the molecular level before gross changes develop, enabling timely delivery of crucial medical intervention before irreversible damage occurs. S100B serum levels are elevated before seizures suggesting that BBB leakage may be an early event in seizure development. [8] An extremely important application of serum S100B testing is in the selection of patients with minor head injury who do not need further neuroradiological evaluation, as studies comparing CT scans and S100B levels have demonstrated S100B values below 0.12 ng/mL are associated with low risk of obvious neuroradiological changes (such as intracranial hemorrhage or brain swelling) or significant clinical sequelae.^[9] The excellent negative predictive value of S100B in several neurological conditions is due to the fact that serum S100B levels reflect blood–brain barrier permeability changes even in absence of neuronal injury.^[10][11] In addition, S100B, which is also present in human melanocytes, is a reliable marker for melanoma malignancy both in bioptic tissue and in serum.^[12][13]

Interactions

S100B has been shown to

with:

• AHNAK,^[14]
• IMPA1,^[15]
• IQGAP1,^[16]
• MAPT,^[17][18] and
• P53,^[19]
• PGM1,^[20]
• S100A1,^[21][22]
• S100A6,^[22][23]
• S100A11,^[23]
• VAV1.^[24]

References

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, Bianchi R, Giambanco I, Agneletti AL, Donato R (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.
  S2CID 25531839
  .
• 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, Lang J, Gerlach R, Zimmermann M, Seifert V (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.
  S2CID 25932611
  .
• Morii K, Tanaka R, Takahashi Y, Minoshima S, Fukuyama R, Shimizu N, Kuwano R (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, Neilson KM, Baumal R, Dunn RJ, Marks A (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, Allore R, Marks A (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, Neilson K, Willard HF, Cox DR, Marks A, Dunn RJ (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, Lukas TJ, Watterson DM (1985). "Characterization of human brain S100 protein fraction: amino acid sequence of S100 beta". J. Neurochem. 45 (3): 700–5.
  S2CID 46028228
  .
• 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, Fuldner RA, Bult CJ, Lee NH, Kirkness EF, Weinstock KG, Gocayne JD, White O (1995). "Initial assessment of human gene diversity and expression patterns based upon 83 million nucleotides of cDNA sequence" (PDF). Nature. 377 (6547 Suppl): 3–174.
  PMID 7566098
  .
• Schäfer BW, Wicki R, Engelkamp D, Mattei MG, Heizmann CW (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, Buck S, Zhang X, Yarowsky P, Gearhart JD, Hilt DC (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, Erne P, Heizmann CW (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
  .
• Argandoña EG, Bengoetxea H, Lafuente JV (2009). "Physical exercise is required for environmental enrichment to offset the quantitative effects of dark-rearing on the S-100β astrocytic density in the rat visual cortex".
  PMID 19500177
  .
• 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
  .

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