シスタチン
- 関
- oryzacystatin
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出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2014/03/28 16:42:33」(JST)
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Proteinase inhibitor I25, cystatin |
Crystal structure of an immunomodulatory salivary cystatin from the soft tick Ornithodoros moubata from PDB entry 3L0R.[1]
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Identifiers |
Symbol |
Prot_inh_cystat |
Pfam |
PF00031 |
Pfam clan |
CL0121 |
InterPro |
IPR000010 |
SMART |
SM00043 |
PROSITE |
PDOC00259 |
Available protein structures: |
Pfam |
structures |
PDB |
RCSB PDB; PDBe; PDBj |
PDBsum |
structure summary |
|
The cystatins are a family of cysteine protease inhibitors which share a sequence homology and a common tertiary structure of an alpha helix lying on top of an anti-parallel beta strand. The family is subdivided as described below.
Cystatins show similarity to fetuins, kininogens, histidine-rich glycoproteins and cystatin-related proteins.[2][3][4] Cystatins mainly inhibit peptidase enzymes (another term for proteases) belonging to peptidase families C1 (papain family) and C13 (legumain family). They are know to mis-fold to form amyloid deposits and are implicated in several diseases.
Contents
- 1 Types
- 2 See also
- 3 References
- 4 Further reading
- 5 External links
Types[edit]
The cystatin family includes:
- The Type 1 cystatins, which are intracellular and are present in the cytosol of many cell types, but can also appear in body fluids at significant concentrations. They are single-chain polypeptides of about 100 residues, which have neither disulfide bonds nor carbohydrate side-chains. Type 1 cystatins are also known as Stefins (after the Stefan Institute where they were first discovered [5])
- The Type 2 cystatins, which are mainly extracellular secreted polypeptides are largely acidic, contain four conserved cysteine residues known to form two disulfide bonds, may be glycosylated and/or phosphorylated. They are synthesised with a 19- to 28-residue signal peptide. They are broadly distributed and found in most body fluids.
- The Type 3 cystatins, which are multidomain proteins. The mammalian representatives of this group are the kininogens. There are three different kininogens in mammals: H- (high-molecular-mass, IPR002395) and L- (low-molecular-mass) kininogen, which are found in a number of species, and T-kininogen, which is found only in rats.
- Unclassified cystatins. These are cystatin-like proteins found in a range of organisms: plant phytocystatins, fetuin in mammals, insect cystatins, and a puff adder venom cystatin, which inhibits metalloproteases of the MEROPS peptidase family M12 (astacin/adamalysin). Also, a number of the cystatin-like proteins have been shown to be devoid of inhibitory activity.
Human cystatins[edit]
- CST1, CST2, CST3, CST4, CST5, CST6, CST7, CST8, CST9, CST11, CSTA, CSTB
See also[edit]
- Cystatin C - a novel marker of kidney function.
References[edit]
- ^ ; Salát J, Paesen GC, Rezácová P, Kotsyfakis M, Kovárová Z, Sanda M, Majtán J, Grunclová L, Horká H, Andersen JF, Brynda J, Horn M, Nunn MA, Kopácek P, Kopecký J, Mares M (June 2010). "Crystal structure and functional characterization of an immunomodulatory salivary cystatin from the soft tick Ornithodoros moubata". Biochem. J. 429 (1): 103–12. doi:10.1042/BJ20100280. PMID 20545626. ; rendered with PyMOL
- ^ Rawlings ND, Barrett AJ (1990). "Evolution of proteins of the cystatin superfamily". J. Mol. Evol. 30 (1): 60–71. doi:10.1007/BF02102453. PMID 2107324.
- ^ Abrahamson M, Alvarez-fernandez M, Nathanson CM (2003). "Cystatins". Biochem. Soc. Symp. (70): 179–199. PMID 14587292.
- ^ Bode W, Turk V (1991). "The cystatins: protein inhibitors of cysteine proteinases". FEBS Lett. 285 (2): 213–219. doi:10.1016/0014-5793(91)80804-C. PMID 1855589.
- ^ Machleidt, W.; Borchart, U.; Fritz, H.; Brzin, J.; Ritonja, A.; Turk, V. (1983). "Protein inhibitors of cysteine proteinases. II. Primary structure of stefin, a cytosolic protein inhibitor of cysteine proteinases from human polymorphonuclear granulocytes". Hoppe-Seyler's Zeitschrift fur physiologische Chemie 364 (11): 1481–1486. doi:10.1515/bchm2.1983.364.2.1481. PMID 6689312. edit
Further reading[edit]
- Cystatin: a protein that flips out! QUite Interesting PDB Structure article at PDBe
- Lee C, Bongcam-Rudloff E, Sollner C, Jahnen-Dechent W, Claesson-Welsh L (2009). "Type 3 cystatins; fetuins, kininogen and histidine-rich glycoprotein". Front. Biosci. 14 (14): 2911–22. doi:10.2741/3422. PMID 19273244.
External links[edit]
- Cystatins at the US National Library of Medicine Medical Subject Headings (MeSH)
This article incorporates text from the public domain Pfam and InterPro IPR000010
UpToDate Contents
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English Journal
- Analysis of protein expression changes of the Vero E6 cells infected with classic PEDV strain CV777 by using quantitative proteomic technique.
- Sun D1, Shi H2, Guo D3, Chen J2, Shi D2, Zhu Q3, Zhang X2, Feng L4.
- Journal of virological methods.J Virol Methods.2015 Jun 15;218:27-39. doi: 10.1016/j.jviromet.2015.03.002. Epub 2015 Mar 14.
- Recent outbreaks of porcine epidemic diarrhea virus (PEDV) have caused widespread concern. The identification of proteins associated with PEDV infection might provide insight into PEDV pathogenesis and facilitate the development of novel antiviral strategies. We analyzed the differential protein pro
- PMID 25783682
- A correlation study of telomere length in peripheral blood leukocytes and kidney function with age.
- Zhang WG1, Wang Y1, Hou K1, Jia LP2, Ma J2, Zhao DL1, Zhu SY3, Bai XJ4, Cai GY1, Wang YP5, Sun XF1, Chen XM1.
- Molecular medicine reports.Mol Med Rep.2015 Jun;11(6):4359-64. doi: 10.3892/mmr.2015.3292. Epub 2015 Feb 2.
- The current study aimed to investigate the association between telomere length in peripheral blood leukocytes and kidney function in various age groups of a healthy population. A total of 139 healthy individuals were divided into five groups according to their age: 35‑44, 45‑54, 55‑64, 65‑74
- PMID 25646618
- AT2R Agonist, Compound 21, Is Reno-Protective Against Type 1 Diabetic Nephropathy.
- Koulis C1, Chow BS1, McKelvey M1, Steckelings UM1, Unger T1, Thallas-Bonke V1, Thomas MC1, Cooper ME1, Jandeleit-Dahm KA1, Allen TJ2.
- Hypertension.Hypertension.2015 May;65(5):1073-81. doi: 10.1161/HYPERTENSIONAHA.115.05204. Epub 2015 Mar 16.
- The hemodynamic and nonhemodynamic effects of angiotensin II on diabetic complications are considered to be primarily mediated by the angiotensin II type 1 receptor subtype. However, its biological and functional effect mediated through the angiotensin II type 2 receptor subtype is still unclear. Ac
- PMID 25776077
Japanese Journal
- Cystatin C-Based eGFR Is a Superior Prognostic Parameter to Creatinine-Based eGFR in Post-Endovascular Therapy Peripheral Artery Disease Patients
- Circulation journal : official journal of the Japanese Circulation Society 79(11), 2480-2486, 2015-11
- NAID 40020625252
- 質量分析を利用した臨床検査 (第110回生涯教育講座)
- 島根医学 : the journal of the Shimane Medical Association 35(3), 130-136, 2015-09
- NAID 40020662579
- Hypothalamic-pituitary-adrenal axis activity is associated with the prevalence of chronic kidney disease in diabetic patients
Related Links
- Types [edit] The cystatin family includes: The Type 1 cystatins, which are intracellular and are present in the cytosol of many cell types, but can also appear in body fluids at significant concentrations. They are single-chain ...
- 【メタ解析】 [1] Feng Y, Zhang Y, Li G, Wang L. The relationship of cystatin-C change and the prevalence of death or dialysis need after acute kidney injury: a meta-analysis. Nephrology (Carlton) [Epub ...
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