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http://purl.uniprot.org/citations/21367861http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21367861http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21367861http://www.w3.org/2000/01/rdf-schema#comment"Human vitamin K 2,3-epoxide reductase complex subunit 1-like 1 (VKORC1L1), expressed in HEK 293T cells and localized exclusively to membranes of the endoplasmic reticulum, was found to support both vitamin K 2,3-epoxide reductase (VKOR) and vitamin K reductase enzymatic activities. Michaelis-Menten kinetic parameters for dithiothreitol-driven VKOR activity were: K(m) (μM) = 4.15 (vitamin K(1) epoxide) and 11.24 (vitamin K(2) epoxide); V(max) (nmol·mg(-1)·hr(-1)) = 2.57 (vitamin K(1) epoxide) and 13.46 (vitamin K(2) epoxide). Oxidative stress induced by H(2)O(2) applied to cultured cells up-regulated VKORC1L1 expression and VKOR activity. Cell viability under conditions of no induced oxidative stress was increased by the presence of vitamins K(1) and K(2) but not ubinquinone-10 and was specifically dependent on VKORC1L1 expression. Intracellular reactive oxygen species levels in cells treated with 2,3-dimethoxy-1,4-naphthoquinone were mitigated in a VKORC1L1 expression-dependent manner. Intracellular oxidative damage to membrane intrinsic proteins was inversely dependent on VKORC1L1 expression and the presence of vitamin K(1). Taken together, our results suggest that VKORC1L1 is responsible for driving vitamin K-mediated intracellular antioxidation pathways critical to cell survival."xsd:string
http://purl.uniprot.org/citations/21367861http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m110.210971"xsd:string
http://purl.uniprot.org/citations/21367861http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m110.210971"xsd:string
http://purl.uniprot.org/citations/21367861http://purl.uniprot.org/core/author"Muller J."xsd:string
http://purl.uniprot.org/citations/21367861http://purl.uniprot.org/core/author"Muller J."xsd:string
http://purl.uniprot.org/citations/21367861http://purl.uniprot.org/core/author"Oldenburg J."xsd:string
http://purl.uniprot.org/citations/21367861http://purl.uniprot.org/core/author"Oldenburg J."xsd:string
http://purl.uniprot.org/citations/21367861http://purl.uniprot.org/core/author"Muller C.R."xsd:string
http://purl.uniprot.org/citations/21367861http://purl.uniprot.org/core/author"Muller C.R."xsd:string
http://purl.uniprot.org/citations/21367861http://purl.uniprot.org/core/author"Hass M."xsd:string
http://purl.uniprot.org/citations/21367861http://purl.uniprot.org/core/author"Hass M."xsd:string
http://purl.uniprot.org/citations/21367861http://purl.uniprot.org/core/author"Watzka M."xsd:string
http://purl.uniprot.org/citations/21367861http://purl.uniprot.org/core/author"Watzka M."xsd:string
http://purl.uniprot.org/citations/21367861http://purl.uniprot.org/core/author"Kirfel G."xsd:string
http://purl.uniprot.org/citations/21367861http://purl.uniprot.org/core/author"Kirfel G."xsd:string
http://purl.uniprot.org/citations/21367861http://purl.uniprot.org/core/author"Bevans C.G."xsd:string
http://purl.uniprot.org/citations/21367861http://purl.uniprot.org/core/author"Bevans C.G."xsd:string
http://purl.uniprot.org/citations/21367861http://purl.uniprot.org/core/author"Marinova M."xsd:string
http://purl.uniprot.org/citations/21367861http://purl.uniprot.org/core/author"Marinova M."xsd:string
http://purl.uniprot.org/citations/21367861http://purl.uniprot.org/core/author"Westhofen P."xsd:string
http://purl.uniprot.org/citations/21367861http://purl.uniprot.org/core/author"Westhofen P."xsd:string
http://purl.uniprot.org/citations/21367861http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21367861http://purl.uniprot.org/core/date"2011"xsd:gYear