WordNet

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"
the 19th letter of the Roman alphabet (同)s

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蛋白(たんばく)質
sulfurの化学記号 / {略}South[ern]

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2012/12/10 03:21:10」(JST)

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Protein S is a vitamin K-dependent plasma glycoprotein synthesized in the endothelium. In the circulation, Protein S exists in two forms: a free form and a complex form bound to complement protein C4b-binding protein (C4BP). In humans, protein S is encoded by the PROS1 gene.^[1]^[2] In 1979, researchers in Seattle, Washington first discovered protein S and arbitrarily named it after the city of its discovery.^[3]^[4]

Function

The best characterized function of Protein S is its role in the anti coagulation pathway, where it functions as a cofactor to Protein C in the inactivation of Factors Va and VIIIa. Only the free form has cofactor activity.^[5]

Protein S can bind to negatively charged phospholipids via the carboxylated GLA domain. This property allows Protein S to function in the removal of cells which are undergoing apoptosis. Apoptosis is a form of cell death that is used by the body to remove unwanted or damaged cells from tissues. Cells which are apoptotic (i.e. in the process of apoptosis) no longer actively manage the distribution of phospholipids in their outer membrane and hence begin to display negatively charged phospholipids, such as phosphatidyl serine, on the cell surface. In healthy cells, an ATP (Adenosine triphosphate)-dependent enzyme removes these from the outer leaflet of the cell membrane. These negatively charged phospholipids are recognized by phagocytes such as macrophages. Protein S can bind to the negatively charged phospholipids and function as a bridging molecule between the apoptotic cell and the phagocyte. The bridging property of Protein S enhances the phagocytosis of the apoptotic cell, allowing it to be removed 'cleanly' without any symptoms of tissue damage such as inflammation occurring.

Pathology

Mutations in the PROS1 gene can lead to Protein S deficiency which is a rare blood disorder which can lead to an increased risk of thrombosis.^[6]^[7]

Interactions

Protein S has been shown to interact with Factor V.^[8]^[9]

References

^ Lundwall A, Dackowski W, Cohen E, Shaffer M, Mahr A, Dahlbäck B, Stenflo J, Wydro R (September 1986). "Isolation and sequence of the cDNA for human protein S, a regulator of blood coagulation". Proc. Natl. Acad. Sci. U.S.A. 83 (18): 6716–20. doi:10.1073/pnas.83.18.6716. PMC 386580. PMID 2944113. //www.ncbi.nlm.nih.gov/pmc/articles/PMC386580/.
^ Long GL, Marshall A, Gardner JC, Naylor SL (January 1988). "Genes for human vitamin K-dependent plasma proteins C and S are located on chromosomes 2 and 3, respectively". Somat. Cell Mol. Genet. 14 (1): 93–8. doi:10.1007/BF01535052. PMID 2829367.
^ Di Scipio RG, Hermodson MA, Yates SG, Davie EW (February 1977). "A comparison of human prothrombin, factor IX (Christmas factor), factor X (Stuart factor), and protein S". Biochemistry 16 (4): 698–706. doi:10.1021/bi00623a022. PMID 836809.
^ DiScipio RG, Davie EW (March 1979). "Characterization of protein S, a gamma-carboxyglutamic acid containing protein from bovine and human plasma". Biochemistry 18 (5): 899–904. doi:10.1021/bi00572a026. PMID 420821.
^ Castoldi E, Hackeng TM (September 2008). "Regulation of coagulation by protein S". Curr. Opin. Hematol. 15 (5): 529–36. doi:10.1097/MOH.0b013e328309ec97. PMID 18695379.
^ Beauchamp NJ, Dykes AC, Parikh N, Campbell Tait R, Daly ME (June 2004). "The prevalence of, and molecular defects underlying, inherited protein S deficiency in the general population". Br. J. Haematol. 125 (5): 647–54. doi:10.1111/j.1365-2141.2004.04961.x. PMID 15147381.
^ García de Frutos P, Fuentes-Prior P, Hurtado B, Sala N (September 2007). "Molecular basis of protein S deficiency". Thromb. Haemost. 98 (3): 543–56. PMID 17849042.
^ Heeb, M J; Kojima Y, Rosing J, Tans G, Griffin J H (Dec. 1999). "C-terminal residues 621-635 of protein S are essential for binding to factor Va". J. Biol. Chem. (UNITED STATES) 274 (51): 36187–92. doi:10.1074/jbc.274.51.36187. ISSN 0021-9258. PMID 10593904.
^ Heeb, M J; Mesters R M, Tans G, Rosing J, Griffin J H (Feb. 1993). "Binding of protein S to factor Va associated with inhibition of prothrombinase that is independent of activated protein C". J. Biol. Chem. (UNITED STATES) 268 (4): 2872–7. ISSN 0021-9258. PMID 8428962.

UpToDate Contents

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1. プロテインＳ欠乏症 protein s deficiency
2. 止血の概要 overview of hemostasis
3. 先天性血栓性素因のマネージメント management of inherited thrombophilia
4. 成人における門脈血栓症の疫学および病因 epidemiology and pathogenesis of portal vein thrombosis in adults
5. Factor V Leiden and activated protein C resistance: Clinical manifestations and diagnosis

English Journal

NMR mapping of protein conformational landscapes using coordinated behavior of chemical shifts upon ligand binding.

Cembran A1, Kim J, Gao J, Veglia G.Author information 1Department of Biochemistry, Biophysics & Molecular Biology, University of Minnesota, 6-155 Jackson Hall, MN 55455, USA. vegli001@umn.edu.AbstractProteins exist as an ensemble of conformers that are distributed on free energy landscapes resembling folding funnels. While the most stable conformers populate low energy basins, protein function is often carried out through low-populated conformational states that occupy high energy basins. Ligand binding shifts the populations of these states, changing the distribution of these conformers. Understanding how the equilibrium among the states is altered upon ligand binding, interaction with other binding partners, and/or mutations and post-translational modifications is of critical importance for explaining allosteric signaling in proteins. Here, we propose a statistical analysis of the linear trajectories of NMR chemical shifts (CONCISE, COordiNated ChemIcal Shifts bEhavior) for the interpretation of protein conformational equilibria. CONCISE enables one to quantitatively measure the population shifts associated with ligand titrations and estimate the degree of collectiveness of the protein residues' response to ligand binding, giving a concise view of the structural transitions. The combination of CONCISE with thermocalorimetric and kinetic data allows one to depict a protein's approximate conformational energy landscape. We tested this method with the catalytic subunit of cAMP-dependent protein kinase A, a ubiquitous enzyme that undergoes conformational transitions upon both nucleotide and pseudo-substrate binding. When complemented with chemical shift covariance analysis (CHESCA), this new method offers both collective response and residue-specific correlations for ligand binding to proteins.
Physical chemistry chemical physics : PCCP.Phys Chem Chem Phys.2014 Apr 14;16(14):6508-18. doi: 10.1039/c4cp00110a. Epub 2014 Mar 7.
Proteins exist as an ensemble of conformers that are distributed on free energy landscapes resembling folding funnels. While the most stable conformers populate low energy basins, protein function is often carried out through low-populated conformational states that occupy high energy basins. Ligand
PMID 24604024

Fibrin-based biomaterials: Modulation of macroscopic properties through rational design at the molecular level.

Brown AC1, Barker TH2.Author information 1The School of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, GA 30332, USA; The Wallace H. Coulter Department of Biomedical Engineering, Georgia Institute of Technology and Emory University, Atlanta, GA 30332, USA.2The Wallace H. Coulter Department of Biomedical Engineering, Georgia Institute of Technology and Emory University, Atlanta, GA 30332, USA; The Parker H. Petit Institute for Bioengineering and Biosciences, Georgia Institute of Technology, Atlanta, GA 30332, USA. Electronic address: thomas.barker@bme.gatech.edu.AbstractFibrinogen is one of the primary components of the coagulation cascade and rapidly forms an insoluble matrix following tissue injury. In addition to its important role in hemostasis, fibrin acts as a scaffold for tissue repair and provides important cues for directing cell phenotype following injury. Because of these properties and the ease of polymerization of the material, fibrin has been widely utilized as a biomaterial for over a century. Modifying the macroscopic properties of fibrin, such as elasticity and porosity, has been somewhat elusive until recently, yet with a molecular-level rational design approach it can now be somewhat easily modified through alterations of molecular interactions key to the protein's polymerization process. This review outlines the biochemistry of fibrin and discusses methods for modification of molecular interactions and their application to fibrin based biomaterials.
Acta biomaterialia.Acta Biomater.2014 Apr;10(4):1502-1514. doi: 10.1016/j.actbio.2013.09.008. Epub 2013 Sep 19.
Fibrinogen is one of the primary components of the coagulation cascade and rapidly forms an insoluble matrix following tissue injury. In addition to its important role in hemostasis, fibrin acts as a scaffold for tissue repair and provides important cues for directing cell phenotype following injury
PMID 24056097

Japanese Journal

Non-pungency in a Japanese Chili Pepper Landrace (Capsicum annuum) is Caused by a Novel Loss-of-function Pun1 Allele

The Horticulture Journal advpub(0), 2018
NAID 130005153886

Identification and Characterization of Plasma Membrane Intrinsic Protein (PIP) Aquaporin Genes in Petals of Opening Carnation Flowers

The Horticulture Journal advpub(0), 2017
NAID 130005152905

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★リンクテーブル★

リンク元	「プロテインS」「PS」
拡張検索	「acyl-carrier protein S-acetyltransferase」「90-kDa ribosomal protein S6 kinase」「70-kDa ribosomal protein S6 kinase」「acyl-carrier protein S-malonyltransferase」「protein S deficiency」
関連記事	「S」

「プロテインS」

Protein S (alpha)
	; PDB rendering based on 1z6c.
Available structures
PDB	Ortholog search: PDBe, RCSB
List of PDB id codes
	1Z6C
Identifiers
Symbols	PROS1; PROS; PS21; PS22; PS23; PS24; PS25; PSA; THPH5; THPH6
External IDs	OMIM: 176880 MGI: 1095733 HomoloGene: 264 GeneCards: PROS1 Gene
Gene Ontology
Molecular function	• endopeptidase inhibitor activity; • calcium ion binding;
Cellular component	• Golgi membrane; • extracellular region; • endoplasmic reticulum membrane; • Golgi lumen; • platelet alpha granule lumen;
Biological process	• platelet degranulation; • proteolysis; • blood coagulation; • negative regulation of endopeptidase activity; • peptidyl-glutamic acid carboxylation; • platelet activation; • regulation of complement activation; • fibrinolysis; • post-translational protein modification; • cellular protein metabolic process; • innate immune response; • leukocyte migration;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs
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