ヘパリンコファクターII、ヘパリン補因子II
WordNet
- a polysaccharide produced in basophils (especially in the lung and liver) and that inhibits the activity of thrombin in coagulation of the blood; it (trade names Lipo-Hepin and Liquaemin) is used as an anticoagulant in the treatment of thrombosis and in heart surgery (同)Lipo-Hepin, Liquaemin
- the 9th letter of the Roman alphabet (同)i
- a substance (as a coenzyme) that must join with another to produce a given result
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Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2015/05/03 15:50:36」(JST)
[Wiki en表示]
Serpin peptidase inhibitor, clade D (heparin cofactor), member 1 |
PDB rendering based on 1jmj. |
Available structures |
PDB |
Ortholog search: PDBe, RCSB |
List of PDB id codes |
1JMJ, 1JMO
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Identifiers |
Symbols |
SERPIND1 ; D22S673; HC2; HCF2; HCII; HLS2; LS2; THPH10 |
External IDs |
OMIM: 142360 MGI: 96051 HomoloGene: 36018 GeneCards: SERPIND1 Gene |
Gene ontology |
Molecular function |
• endopeptidase inhibitor activity
• serine-type endopeptidase inhibitor activity
• heparin binding
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Cellular component |
• extracellular region
• extracellular space
• extracellular vesicular exosome
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Biological process |
• chemotaxis
• blood coagulation
• negative regulation of endopeptidase activity
• regulation of proteolysis
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Sources: Amigo / QuickGO |
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RNA expression pattern |
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More reference expression data |
Orthologs |
Species |
Human |
Mouse |
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Entrez |
3053 |
15160 |
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Ensembl |
ENSG00000099937 |
ENSMUSG00000022766 |
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UniProt |
P05546 |
P49182 |
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RefSeq (mRNA) |
NM_000185 |
NM_008223 |
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RefSeq (protein) |
NP_000176 |
NP_032249 |
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Location (UCSC) |
Chr 22:
21.13 – 21.14 Mb |
Chr 16:
17.33 – 17.34 Mb |
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PubMed search |
[1] |
[2] |
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Heparin cofactor II (HCII), a protein encoded by the SERPIND1 gene, is a coagulation factor that inhibits IIa, and is a cofactor for heparin and dermatan sulfate ("minor antithrombin"). [1]
The product encoded by this gene is a serine proteinase inhibitor which rapidly inhibits thrombin in the presence of dermatan sulfate or heparin. The gene contains five exons and four introns. This protein shares homology with antithrombin III and other members of the alpha 1-antitrypsin superfamily. Mutations in this gene are associated with heparin cofactor II deficiency.[1] Heparin Cofactor II deficiency can lead to increased thrombin generation and a hypercoagulable state.
References
- ^ a b "Entrez Gene: SERPIND1 serpin peptidase inhibitor, clade D (heparin cofactor), member 1".
Further reading
- Pizzo SV (1989). "Serpin receptor 1: a hepatic receptor that mediates the clearance of antithrombin III-proteinase complexes.". Am. J. Med. 87 (3B): 10S–14S. doi:10.1016/0002-9343(89)80524-8. PMID 2552799.
- Uszyński M (1992). "Tissue anticoagulants in the human placenta: preliminary study with a heparin-like anticoagulant and review of the literature.". Gynecol. Obstet. Invest. 32 (3): 129–33. doi:10.1159/000293013. PMID 1836773.
- Sutherland JS, Bhakta V, Filion ML, Sheffield WP (2006). "The transferable tail: fusion of the N-terminal acidic extension of heparin cofactor II to alpha1-proteinase inhibitor M358R specifically increases the rate of thrombin inhibition.". Biochemistry 45 (38): 11444–52. doi:10.1021/bi0609624. PMID 16981704.
- Giri TK, Tollefsen DM (2006). "Placental dermatan sulfate: isolation, anticoagulant activity, and association with heparin cofactor II.". Blood 107 (7): 2753–8. doi:10.1182/blood-2005-09-3755. PMC 1895383. PMID 16339402.
- Liu T, Qian WJ, Gritsenko MA et al. (2006). "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry.". J. Proteome Res. 4 (6): 2070–80. doi:10.1021/pr0502065. PMC 1850943. PMID 16335952.
- Rual JF, Venkatesan K, Hao T et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
- Schillinger M, Exner M, Sabeti S et al. (2005). "High plasma heparin cofactor II activity protects from restenosis after femoropopliteal stenting.". Thromb. Haemost. 92 (5): 1108–13. doi:10.1267/THRO04051108. PMID 15543340.
- Collins JE, Wright CL, Edwards CA et al. (2005). "A genome annotation-driven approach to cloning the human ORFeome.". Genome Biol. 5 (10): R84. doi:10.1186/gb-2004-5-10-r84. PMC 545604. PMID 15461802.
- Suzuki Y, Yamashita R, Shirota M et al. (2004). "Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions.". Genome Res. 14 (9): 1711–8. doi:10.1101/gr.2435604. PMC 515316. PMID 15342556.
- Corral J, Aznar J, Gonzalez-Conejero R et al. (2006). "Homozygous deficiency of heparin cofactor II: relevance of P17 glutamate residue in serpins, relationship with conformational diseases, and role in thrombosis.". Circulation 110 (10): 1303–7. doi:10.1161/01.CIR.0000140763.51679.D9. PMID 15337701.
- Fortenberry YM, Whinna HC, Gentry HR et al. (2004). "Molecular mapping of the thrombin-heparin cofactor II complex.". J. Biol. Chem. 279 (41): 43237–44. doi:10.1074/jbc.M406716200. PMID 15292227.
- Zhang F, Wu Y, Ma Q et al. (2004). "Studies on the effect of calcium in interactions between heparin and heparin cofactor II using surface plasmon resonance.". Clin. Appl. Thromb. Hemost. 10 (3): 249–57. doi:10.1177/107602960401000307. PMID 15247982.
- Anderson NL, Polanski M, Pieper R et al. (2004). "The human plasma proteome: a nonredundant list developed by combination of four separate sources.". Mol. Cell Proteomics 3 (4): 311–26. doi:10.1074/mcp.M300127-MCP200. PMID 14718574.
- Strausberg RL, Feingold EA, Grouse LH et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Noda A, Wada H, Kusiya F et al. (2003). "Plasma levels of heparin cofactor II (HCII) and thrombin-HCII complex in patients with disseminated intravascular coagulation.". Clin. Appl. Thromb. Hemost. 8 (3): 265–71. doi:10.1177/107602960200800311. PMID 12361205.
- Baglin TP, Carrell RW, Church FC et al. (2002). "Crystal structures of native and thrombin-complexed heparin cofactor II reveal a multistep allosteric mechanism.". Proc. Natl. Acad. Sci. U.S.A. 99 (17): 11079–84. doi:10.1073/pnas.162232399. PMC 123213. PMID 12169660.
- Cunningham MA, Bhakta V, Sheffield WP (2003). "Altering heparin cofactor II at VAL439 (P6) either impairs inhibition of thrombin or confers elastase resistance.". Thromb. Haemost. 88 (1): 89–97. PMID 12152684.
- Hayakawa Y, Hirashima Y, Kurimoto M et al. (2002). "Contribution of basic residues of the A helix of heparin cofactor II to heparin- or dermatan sulfate-mediated thrombin inhibition.". FEBS Lett. 522 (1-3): 147–50. doi:10.1016/S0014-5793(02)02930-7. PMID 12095635.
- Mitchell JW, Church FC (2002). "Aspartic acid residues 72 and 75 and tyrosine-sulfate 73 of heparin cofactor II promote intramolecular interactions during glycosaminoglycan binding and thrombin inhibition.". J. Biol. Chem. 277 (22): 19823–30. doi:10.1074/jbc.M200630200. PMID 11856753.
- Böhme C, Nimtz M, Grabenhorst E et al. (2002). "Tyrosine sulfation and N-glycosylation of human heparin cofactor II from plasma and recombinant Chinese hamster ovary cells and their effects on heparin binding.". Eur. J. Biochem. 269 (3): 977–88. doi:10.1046/j.0014-2956.2001.02732.x. PMID 11846800.
PDB gallery
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1jmj: Crystal Structure of Native Heparin Cofactor II
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1jmo: Crystal Structure of the Heparin Cofactor II-S195A Thrombin Complex
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External links
- The MEROPS online database for peptidases and their inhibitors: I04.019
- Heparin Cofactor II at the US National Library of Medicine Medical Subject Headings (MeSH)
- He L, Vicente C, Westrick R, Eitzman D, Tollefsen D (2002). "Heparin cofactor II inhibits arterial thrombosis after endothelial injury.". J Clin Invest 109 (2): 213–9. doi:10.1172/JCI13432. PMC 150836. PMID 11805133.
Serpins
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inhibitory |
- Alpha 1-antichymotrypsin
- Alpha 1-antitrypsin
- Alpha 2-antiplasmin
- Antithrombin
- C1-inhibitor
- Heparin cofactor II
- Protein C inhibitor
- Plasminogen activator inhibitor-1
- Plasminogen activator inhibitor-2
- Protein Z-related protease inhibitor
- SERPINA1
- SERPINA2
- SERPINA3
- SERPINA4
- SERPINA5
- SERPINA6
- SERPINA7
- SERPINA8
- SERPINA9
- SERPINA14
- SERPINB1
- SERPINB2
- SERPINB3
- SERPINB4
- SERPINB5
- SERPINB6
- SERPINB7
- SERPINB8
- SERPINB9
- SERPINB13
- SERPINC1
- SERPIND1
- SERPINE1
- SERPINE2
- SERPINE2
- SERPINF1
- SERPING1
- SERPINH1
- SERPINI1
- SERPINI2
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Cross class inhibitory |
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noninhibitory |
- Heat shock protein 47
- Maspin
- Ovalbumin
- SERPINF1
- Thyroxine-binding globulin
- Transcortin
- SERPINF1
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see also disorders of globin and globulin proteins
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Proteins: Globular proteins
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Serum globulins |
Alpha globulins
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serpins:
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- alpha-1 (Alpha 1-antichymotrypsin, Alpha 1-antitrypsin)
- alpha-2 (Alpha 2-antiplasmin)
- Antithrombin (Heparin cofactor II)
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carrier proteins:
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- alpha-1 (Transcortin)
- alpha-2 (Ceruloplasmin)
- Retinol binding protein
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other:
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- alpha-1 (Orosomucoid)
- alpha-2 (alpha-2-Macroglobulin, Haptoglobin)
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Beta globulins
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carrier proteins:
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- Sex hormone-binding globulin
- Transferrin
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other:
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- Angiostatin
- Hemopexin
- Beta-2 microglobulin
- Factor H
- Plasminogen
- Properdin
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Gamma globulin
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Other
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- Fibronectin (fFN-Fetal fibronectin)
- Macroglobulin/Microglobulin
- Transcobalamin
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Other globulins |
- Beta-lactoglobulin
- Thyroglobulin
- Alpha-lactalbumin
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Albumins |
Egg white
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- Conalbumin
- Ovalbumin
- Avidin
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Serum albumin
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- Human serum albumin
- Bovine serum albumin
- Prealbumin
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Other
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- C-reactive protein
- Lactalbumin (Alpha-lactalbumin)
- Parvalbumin
- Ricin
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- see also disorders of globin and globulin proteins
Index of proteins
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Description |
- Proteins
- Membrane
- Globular
- Antibodies
- Fibrous
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UpToDate Contents
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English Journal
- Retention of Thrombin Inhibitory Activity by Recombinant Serpins Expressed as Integral Membrane Proteins Tethered to the Surface of Mammalian Cells.
- Gierczak RF, Sutherland JS, Bhakta V, Toltl LJ, Liaw PC, Sheffield WP.SourceDepartments of Pathology and Molecular Medicine, McMaster University, Hamilton, Ontario Medicine, McMaster University, Hamilton, Ontario Canadian Blood Services, Research and Development, Hamilton, Ontario Northern Ontario School of Medicine, Sudbury, Ontario, Canada.
- Journal of thrombosis and haemostasis : JTH.J Thromb Haemost.2011 Oct 4. doi: 10.1111/j.1538-7836.2011.04524.x. [Epub ahead of print]
- Background:?Serpins form a widely distributed protein superfamily but no integral membrane serpins have been described. Objectives: To anchor three serpins (α(1) -proteinase inhibitor (α(1) PI M358R), antithrombin (AT) and heparin cofactor II (HCII)) in the plasma membranes of transfected mammal
- PMID 21972922
- Ascidian dermatan sulfates attenuate metastasis, inflammation and thrombosis by inhibition of P-selectin.
- Kozlowski EO, Pavao MS, Borsig L.SourceInstitute of Physiology, University of Zurich and Zurich Center for Integrative Human Physiology, Zurich, Switzerland.
- Journal of thrombosis and haemostasis : JTH.J Thromb Haemost.2011 Sep;9(9):1807-15. doi: 10.1111/j.1538-7836.2011.04401.x.
- BACKGROUND: Cancer-associated thrombosis and enduring inflammation are strongly associated with cancer progression and metastasis. Heparin is the mostly clinically used anticoagulant/antithrombotic drug, and has recently been shown to exhibit antimetastatic and anti-inflammatory activities that are
- PMID 21676168
Japanese Journal
- Plasma heparin cofactor II activity is inversely associated with left atrial volume and diastolic dysfunction in humans with cardiovascular risk factors
- ISE Takayuki,AIHARA Ken-ichi,SUMITOMO UEDA Yuka,YOSHIDA Sumiko,IKEDA Yasumasa,YAGI Shusuke,IWASE Takashi,YAMADA Hirotsugu,AKAIKE Masashi,SATA Masataka,MATSUMOTO Toshio
- Hypertension research : clinical and experimental : official journal of the Japanese Society of Hypertension 34(2), 225-231, 2011-02-01
- NAID 10031163157
- Plasma heparin cofactor II activity is inversely associated with left atrial volume and diastolic dysfunction in humans with cardiovascular risk factors
- Ise Takayuki,Aihara Ken-ichi,Sumitomo-Ueda Yuka,Yoshida Sumiko,Ikeda Yasumasa,Yagi Shusuke,Iwase Takashi,Yamada Hirotsugu,Akaike Masashi,Sata Masataka,Matsumoto Toshio
- HYPERTENSION RESEARCH 34(2), 225-231, 2011
- NAID 120005179918
- Heparin Cofactor II Attenuates Vascular Remodeling in Humans and Mice
- Circulation journal : official journal of the Japanese Circulation Society 74(8), 1518-1523, 2010-07-25
- … Heparin cofactor II (HCII), a serine protease inhibitor (serpin), inactivates thrombin action in the subendothelial layer of the vascular wall. …
- NAID 10026565241
Related Links
- Heparin cofactor II, a protein encoded by the SERPIND1 gene, is a coagulation factor that inhibits IIa, and is a cofactor for heparin and dermatan sulfate ("minor antithrombin"). [1] The product encoded by this gene is a serine ...
- Information about Heparin cofactor II in Free online English dictionary. What is Heparin cofactor II? Meaning of Heparin cofactor II medical term. What does Heparin cofactor II mean? Printer Friendly Dictionary, Encyclopedia and ...
★リンクテーブル★
[★]
- 英
- heparin cofactor II, HC II, HC-II
- 関
- トロンビン
[★]
- 英
- heparin cofactor II
- 関
- ヘパリンコファクターII
[★]
ヘパリンコファクターII欠損症
[★]
[★]