17112295

Source:http://linkedlifedata.com/resource/pubmed/id/17112295

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0031325, umls-concept:C0043031, umls-concept:C0205464, umls-concept:C1332838, umls-concept:C1704259, umls-concept:C1705987
pubmed:issue	12
pubmed:dateCreated	2006-11-20
pubmed:abstractText	Warfarin is a widely prescribed anticoagulant for thromboembolic disorders and exhibits wide inter-individual differences in its pharmacodynamic effects. Warfarin exerts its anticoagulant effect by inhibiting the enzymatic activity of vitamin K 2,3-epoxide reductase complex, subunit 1 (VKORC1) which regenerates reduced vitamin K as an essential cofactor for the post-translational gamma-carboxylation of glutamic acid residues on coagulation factors II, VII, IX and X, and the anticoagulant proteins C, S and Z. Recent studies have shown polymorphisms in genes involved in the uptake of vitamin K (apolipoprotein E [ApoE]), reduction of vitamin K 2,3-epoxide (VKORC1), metabolism of warfarin (cytochrome P450 2C9 [CYP2C9]), and gamma carboxylation (gamma-glutamyl carboxylase [GGCX]) to influence the pharmacokinetics and pharmacodynamics of warfarin in patients from different ethnic backgrounds, resulting in variable warfarin dose requirements. Understanding the causal relationship of these polygenic influences on warfarin dose requirements in patients of different ethnicity may be vital in reducing inter-patient variability and optimising anticoagulant therapy.
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/7606849
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Anticoagulants, http://linkedlifedata.com/resource/pubmed/chemical/Aryl Hydrocarbon Hydroxylases, http://linkedlifedata.com/resource/pubmed/chemical/CALU protein, human, http://linkedlifedata.com/resource/pubmed/chemical/CYP2C9 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Carbon-Carbon Ligases, http://linkedlifedata.com/resource/pubmed/chemical/Epoxide Hydrolases, http://linkedlifedata.com/resource/pubmed/chemical/Mixed Function Oxygenases, http://linkedlifedata.com/resource/pubmed/chemical/Warfarin, http://linkedlifedata.com/resource/pubmed/chemical/glutamyl carboxylase, http://linkedlifedata.com/resource/pubmed/chemical/vitamin K epoxidase
pubmed:status	MEDLINE
pubmed:issn	0312-5963
pubmed:author	pubmed-author:BalramChowbayC, pubmed-author:JadaSrinivasa RaoSR, pubmed-author:LalSumanS, pubmed-author:LeeEdmund J DEJ, pubmed-author:LimWan-TeckWT, pubmed-author:XiangXiaoqiangX
pubmed:issnType	Print
pubmed:volume	45
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	1189-200
pubmed:dateRevised	2009-11-19
pubmed:meshHeading	pubmed-meshheading:17112295-Anticoagulants, pubmed-meshheading:17112295-Aryl Hydrocarbon Hydroxylases, pubmed-meshheading:17112295-Calcium-Binding Proteins, pubmed-meshheading:17112295-Carbon-Carbon Ligases, pubmed-meshheading:17112295-Epoxide Hydrolases, pubmed-meshheading:17112295-Humans, pubmed-meshheading:17112295-Mixed Function Oxygenases, pubmed-meshheading:17112295-Pharmacogenetics, pubmed-meshheading:17112295-Polymorphism, Genetic, pubmed-meshheading:17112295-Warfarin
pubmed:year	2006
pubmed:articleTitle	Pharmacogenetics of target genes across the warfarin pharmacological pathway.
pubmed:affiliation	National Cancer Centre, Laboratory of Clinical Pharmacology, Division of Medical Sciences, Singapore, Singapore.
pubmed:publicationType	Journal Article, Review, Research Support, Non-U.S. Gov't