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any of a large group of nitrogenous organic compounds that are essential constituents of living cells; consist of polymers of amino acids; essential in the diet of animals for growth and for repair of tissues; can be obtained from meat and eggs and milk and legumes; "a diet high in protein"

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蛋白(たんばく)質

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/02/14 02:16:57」(JST)

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The S-100 proteins (often styled without the hyphen, S100) 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 S-100 proteins.^[1] Their name is derived from the fact that these proteins are soluble in 100%, i.e. saturated ammonium sulfate at neutral pH. They are encoded by a family of genes whose symbols use the S100 prefix, for example, S100A1, S100A2, S100A3.

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

S-100 is normally present in cells derived from the neural crest (Schwann cells, and melanocytes), chondrocytes, adipocytes, myoepithelial cells, macrophages, Langerhans cells, dendritic cells, and keratinocytes. It may be present in some breast epithelial cells.

S100 proteins have been implicated in a variety of intracellular and extracellular functions.^[2] 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.^[3]

Pathology

S100 immunostain marking the sustentacular cells in a paraganglioma.

Several members of the S-100 protein family are useful as markers for certain tumors and epidermal differentiation. It can be found in melanomas,^[4] 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.^[5]

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

Human genes

S100A1, S100A2, S100A3, S100A4, S100A5, S100A6, S100A7 (psoriasin), S100A8, S100A9, S100A10, S100A11, S100A12, S100A13, S100A14(S100A14), S100A15 Koebnerisin, (S100A15), S100A16
S100B
S100P
S100Z(S100Z)

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

References

^ 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.
^ 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.
^ 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.
^ 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.
^ 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.

External links

S100 Proteins at the US National Library of Medicine Medical Subject Headings (MeSH)

UpToDate Contents

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1. 肺ランゲルハンス細胞組織球症 pulmonary langerhans cell histiocytosis
2. 心臓手術の神経学的合併症の予防 prevention of neurologic complications of cardiac surgery
3. 皮膚黒色腫におけるtumor node metastasis（TNM）病期分類法およびその他の予後因子 tumor node metastasis tnm staging system and other prognostic factors in cutaneous melanoma
4. クロイツフェルト・ヤコブ病 creutzfeldt jakob disease
5. 組織球性肉腫 histiocytic sarcoma

English Journal

Proteome analysis identified human neutrophil membrane tubulovesicular extensions (cytonemes, membrane tethers) as bactericide trafficking.

Galkina SI, Fedorova NV, Serebryakova MV, Romanova JM, Golyshev SA, Stadnichuk VI, Baratova LA, Sud'ina GF, Klein T.SourceLomonosov Moscow State University A.N. Belozersky Institute of Physico-Chemical Biology, Moscow, Russia.
Biochimica et biophysica acta.Biochim Biophys Acta.2012 Nov;1820(11):1705-14. Epub 2012 Jul 2.
BACKGROUND: Following adhesion to fibronectin neutrophils can develop membrane tubulovesicular extensions (TVEs) that can be 200nm wide and several cell diameters long. TVEs attach neutrophils to the other cells, substrata or bacteria over distance. To understand the physiological significance of TV
PMID 22766193

Receptor for advanced glycation endproducts (RAGE) deficiency protects against MPTP toxicity.

Teismann P, Sathe K, Bierhaus A, Leng L, Martin HL, Bucala R, Weigle B, Nawroth PP, Schulz JB.SourceDepartment of Neurodegeneration and Restorative Research, Center of Molecular Physiology of the Brain (CMPB) and Center of Neurological Medicine, University of Göttingen, Göttingen, Germany; School of Medical Sciences, Institute of Medical Sciences, University of Aberdeen, Aberdeen, Scotland.
Neurobiology of aging.Neurobiol Aging.2012 Oct;33(10):2478-90. Epub 2012 Jan 9.
Parkinson's disease (PD) is a common neurodegenerative disorder of unknown pathogenesis characterized by the loss of nigrostriatal dopaminergic neurons. Oxidative stress, microglial activation and inflammatory responses seem to contribute to the pathogenesis. The receptor for advanced glycation endp
PMID 22227007

Japanese Journal

Intracranial Rosai-Dorfman Disease - a Case Report and a Review of the Literature

Yamauchi Taishi,Hayashi Tomayoshi,Matsuo Takayuki,Matsumoto Miki,Kinoshita Naoe,Abe Kuniko,Nagata Izumi
Acta medica Nagasakiensia 57(2), 57-63, 2012-07
… The histiocytes were immunoreactive for S-100 protein and CD68 and negativefor CD1a, leading to the diagnosis of intracranial RDD. …
NAID 120004418971

Intracranial Rosai-Dorfman Disease - a Case Report and a Review of the Literature

Yamauchi Taishi .et.al
Acta medica Nagasakiensia 57(2), 57-63, 2012-07
… The histiocytes were immunoreactive for S-100 protein and CD68 and negative for CD1a, leading to the diagnosis of intracranial RDD. …
NAID 110009442922

Related Pictures

★リンクテーブル★

リンク元	「S-100蛋白」
関連記事	「S10」

「S-100蛋白」

Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

S-100/ICaBP type calcium binding domain
	Structure of the S100B protein. Based on PyMOL rendering of PDB 1b4c.
Identifiers
Symbol	S_100
Pfam	PF01023
InterPro	IPR013787
PROSITE	PDOC00275
SCOP	1cnp
SUPERFAMILY	1cnp
Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

　　[★]

英: S100 protein
同: S-100タンパク、S100蛋白質、S-100
関: [[]]

悪性黒色腫のマーカー
下垂体前葉の嫌色素性細胞である folliculostellate cell

英: S-100 protein

「S10」

　　[★]

肺区域

後肺底区：名前の通り下葉の背側を占めるが、解剖図譜には背側の内側～内側に回り込んで下行大動脈溝(左)、あるいは食道溝(右)まで前に及ぶように描いてある。よって内側胸膜に接する。

[pmid15336958-1] 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.

[pmid12645002-2] 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.

[pmid18606705-3] 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.

[pmid18547346-4] 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.

[pmid20596736-5] 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.

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案内

S100 protein