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S100 protein

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S100/ICaBP type calcium binding domain
Structure of the S100B protein. Based on PyMOL rendering of PDB 1b4c.
Identifiers
SymbolS_100
PfamPF01023
InterProIPR013787
PROSITEPDOC00275
SCOP21cnp / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
PDB1yutB:9-52 1yuuA:9-52 1yusB:9-52

1yurA:9-52 1k8uA:5-50 1k9pA:5-50 1k96A:5-50 1k9kA:5-50 1cnpB:5-50 1a03A:5-50 2cnpB:5-50 1jwdB:5-50 1m31A:5-48 1k2hB:5-48 1cfpB:4-47 1psbA:4-47 1mho :4-47 1uwoA:4-47 1mq1B:4-47 1b4cB:4-47 1symA:4-47 1qlkB:4-47 1xydB:4-47 1dt7B:4-47 1mwnA:4-47 1j55A:4-47 1ozoA:4-47 1ksoA:5-48 1irjH:8-51 1xk4K:8-51 1gqmI:4-47 1odbD:4-47 1e8aB:4-47 1clb :5-46 1ig5A:5-46 2bca :5-46 1qx2B:5-46 1bod :5-46 1b1gA:5-46 1kcyA:5-46 1ht9A:5-46 2bcb :5-46 1n65A:5-46 1boc :5-46 3icb :5-46 1kqvA:5-46 1ksmA:5-46 1cdn :5-46 4icb :5-46 1igvA:5-46 1d1oA:5-46 1cb1 :4-46 1a4pB:5-45 1bt6A:5-45 1nshB:7-50 1v4zA:10-19 1v50A:10-19 1qlsA:8-51 1mr8B:5-48 1psrB:6-46

2psr :6-46 3psrA:6-46

The S100 proteins are a family of low-molecular-weight proteins found in vertebrates and characterized by two calcium-binding sites that have helix-loop-helix ("EF-hand type") conformation. There are at least 21 different S100 proteins.[1] They are encoded by a family of genes whose symbols use the S100 prefix, for example, S100A1, S100A2, S100A3. They are also considered as Damage-associated molecular pattern molecules (DAMPs)

Structure

Most S100 proteins are homodimeric, consisting of two identical polypeptides, which are held together by non-covalent bonds. S100 proteins are structurally similar to calmodulin. On the other hand they differ from calmodulin on the other features. For instance, their expression pattern is cell-specific, i.e. they are expressed in particular cell types. Their expression depends on environmental factors. To contrast, calmodulin is a ubiquitous and universal intracellular Ca2+ receptor widely expressed in many cells.

Normal function

S100 proteins are normally present in cells derived from the neural crest (Schwann cells, and melanocytes), chondrocytes, adipocytes, myoepithelial cells, macrophages, Langerhans cells,[2][3] dendritic cells,[4] and keratinocytes. It may be present in some breast epithelial cells.

S100 proteins have been implicated in a variety of intracellular and extracellular functions.[5] S100 proteins are involved in regulation of protein phosphorylation, transcription factors, Ca2+ homeostasis, the dynamics of cytoskeleton constituents, enzyme activities, cell growth and differentiation, and the inflammatory response. S100A7 (psoriasin) and S100A15 have been found to act as cytokines in inflammation, particularly in autoimmune skin conditions such as psoriasis.[6]

Pathology

S100 immunostain marking the sustentacular cells in a paraganglioma.

Several members of the S100 protein family are useful as markers for certain tumors and epidermal differentiation. It can be found in melanomas,[7] 100% of schwannomas, 100% of neurofibromas (weaker than schwannomas), 50% of malignant peripheral nerve sheath tumors (may be weak and/or focal), paraganglioma stromal cells, histiocytoma and clear cell sarcomas. Further, S100 proteins are markers for inflammatory diseases and can mediate inflammation and act as antimicrobials.[8]

S100 proteins have been used in the lab as cell markers for anatomic pathology.

Human genes

CRNN; FLG; FLG2; HRNR; RPTN; S100G; TCHH; THHL1;

Nomenclature

The "S100" symbol prefix is derived from the fact that these proteins are soluble in 100%, i.e. saturated, ammonium sulfate at neutral pH. The symbol has often been hyphenated,[9] but current gene and protein nomenclature, such as HGNC nomenclature, does not use hyphens in symbols.

See also

References

  1. ^ Marenholz I, Heizmann CW, Fritz G (October 2004). "S100 proteins in mouse and man: from evolution to function and pathology (including an update of the nomenclature)". Biochem. Biophys. Res. Commun. 322 (4): 1111–22. doi:10.1016/j.bbrc.2004.07.096. PMID 15336958.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  2. ^ Wilson, AJ; Maddox, PH; Jenkins, D (January 1991). "CD1a and S100 antigen expression in skin Langerhans cells in patients with breast cancer". The Journal of pathology. 163 (1): 25–30. PMID 2002421.
  3. ^ Coppola, D; Fu, L; Nicosia, SV; Kounelis, S; Jones, M (May 1998). "Prognostic significance of p53, bcl-2, vimentin, and S100 protein-positive Langerhans cells in endometrial carcinoma". Human pathology. 29 (5): 455–62. PMID 9596268.
  4. ^ Shinzato, M; Shamoto, M; Hosokawa, S; Kaneko, C; Osada, A; Shimizu, M; Yoshida, A (May 1995). "Differentiation of Langerhans cells from interdigitating cells using CD1a and S-100 protein antibodies". Biotechnic & histochemistry : official publication of the Biological Stain Commission. 70 (3): 114–8. PMID 7548432.
  5. ^ Donato R (April 2003). "Intracellular and extracellular roles of S100 proteins". Microsc. Res. Tech. 60 (6): 540–51. doi:10.1002/jemt.10296. PMID 12645002.
  6. ^ Wolf R, Howard OM, Dong HF, Voscopoulos C, Boeshans K, Winston J, et al. (2008). "Chemotactic activity of S100A7 (Psoriasin) is mediated by the receptor for advanced glycation end products and potentiates inflammation with highly homologous but functionally distinct S100A15". J Immunol. 181 (2): 1499–506. doi:10.4049/jimmunol.181.2.1499. PMC 2435511. PMID 18606705.
  7. ^ Nonaka D, Chiriboga L, Rubin BP (November 2008). "Differential expression of S100 protein subtypes in malignant melanoma, and benign and malignant peripheral nerve sheath tumors". J. Cutan. Pathol. 35 (11): 1014–9. doi:10.1111/j.1600-0560.2007.00953.x. PMID 18547346.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  8. ^ Wolf R, Ruzicka T, Yuspa SH (July 2010). "Novel S100A7 (psoriasin)/S100A15 (koebnerisin) subfamily: highly homologous but distinct in regulation and function". Amino Acids. 41 (4): 789–96. doi:10.1007/s00726-010-0666-4. PMID 20596736.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  9. ^ Elsevier, Dorland's Illustrated Medical Dictionary, Elsevier.

Further reading

  • Wolf R, Voscopoulos CJ, FitzGerald PC, et al. (2006). "The mouse S100A15 ortholog parallels genomic organization, structure, gene expression, and protein-processing pattern of the human S100A7/A15 subfamily during epidermal maturation". J. Invest. Dermatol. 126 (7): 1600–8. doi:10.1038/sj.jid.5700210. PMID 16528363.
  • Ronald Wolf, O. M. Zack Howard, Hui-Fang Dong, Christopher Voscopoulos, Karen Boeshans, Jason Winston, Rao Divi, Michele Gunsior, Paul Goldsmith, Bijan Ahvazi, Triantafyllos Chavakis, Joost J. Oppenheim and Stuart H. Yuspa (2010). "Chemotactic Activity of S100A7 (Psoriasin) Is Mediated by the Receptor for Advanced Glycation End Products and Potentiates Inflammation with Highly Homologous but Functionally Distinct S100A15". The Journal of Immunology. 181 (2): 1499–1506.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  • Ronald Wolf, Francesca Mascia, Alif Dharamsi, O. M. Zack Howard, Christophe Cataisson, Val Bliskovski, Jason Winston, Lionel Feigenbaum, Ulrike Lichti, Thomas Ruzicka Triantafyllos Chavakis, and Stuart H. Yuspa. (2010). "Gene from a Psoriasis Susceptibility Locus Primes the Skin for Inflammation". Science Translational Medicine. 2 (61): 61ra90. doi:10.1126/scitranslmed.3001108. PMID 21148126.{{cite journal}}: CS1 maint: multiple names: authors list (link)
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