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Sökning: id:"swepub:oai:DiVA.org:uu-169793" > Amidoxime Reductase...

LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00003654naa a2200361 4500
001oai:DiVA.org:uu-169793
003SwePub
008120306s2012 | |||||||||||000 ||eng|
009oai:prod.swepub.kib.ki.se:124163667
0247 a https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-1697932 URI
0247 a https://doi.org/10.1074/jbc.M111.3282372 DOI
0247 a http://kipublications.ki.se/Default.aspx?queryparsed=id:1241636672 URI
040 a (SwePub)uud (SwePub)ki
041 a engb eng
042 9 SwePub
072 7a ref2 swepub-contenttype
072 7a art2 swepub-publicationtype
1001 a Neve, Etienne P Au Karolinska Institutet4 aut
2451 0a Amidoxime Reductase System Containing Cytochrome b5 Type B (CYB5B) and MOSC2 Is of Importance for Lipid Synthesis in Adipocyte Mitochondria
264 1c 2012
338 a print2 rdacarrier
520 a Reduction of hydroxylamines and amidoximes is important for drug activation and detoxification of aromatic and heterocyclic amines. Such a reductase system was previously found to be of high activity in adipose tissue and liver, and furthermore, in vitro studies using recombinant truncated and purified enzymes suggested the participation of cytochrome b(5) reductase (CYB5R), cytochrome b(5) (CYB5), and molybdenum cofactor sulfurase C-terminal containing 1 and 2 (MOSC1 and -2). Here, we show that purified rat liver outer mitochondrial membrane contains high amidoxime reductase activity and that MOSC2 is exclusively localized to these membranes. Moreover, using the same membrane fraction, we could show direct binding of a radiolabeled benzamidoxime substrate to MOSC2. Following differentiation of murine 3T3-L1 cells into mature adipocytes, the MOSC2 levels as well as the amidoxime reductase activity were increased, indicating that the enzyme is highly regulated under lipogenic conditions. siRNA-mediated down-regulation of MOSC2 and the mitochondrial form of cytochrome b(5) type B (CYB5B) significantly inhibited the reductase activity in the differentiated adipocytes, whereas down-regulation of MOSC1, cytochrome b(5) type A (CYB5A), CYB5R1, CYB5R2, or CYB5R3 had no effect. Down-regulation of MOSC2 caused impaired lipid synthesis. These results demonstrate for the first time the direct involvement of MOSC2 and CYB5B in the amidoxime reductase activity in an intact cell system. We postulate the presence of a novel reductive enzyme system of importance for lipid synthesis that is exclusively localized to the outer mitochondrial membrane and is composed of CYB5B, MOSC2, and a third unknown component (a CYB5B reductase).
7001 a Nordling, Åsau Section of Pharmacogenetics, Department of Physiology and Pharmacology, Karolinska Institutet, SE-17177 Stockholm4 aut
7001 a Andersson, Tommy Bu AstraZeneca Research and Development, Pepparedsleden 1, SE-431 83 Mölndal4 aut
7001 a Hellman, Ulfu Uppsala universitet,Ludwiginstitutet för cancerforskning4 aut0 (Swepub:uu)ulfhm
7001 a Diczfalusy, Ulfu Karolinska Institutet4 aut
7001 a Johansson, Ingeru Karolinska Institutet4 aut
7001 a Ingelman-Sundberg, Magnusu Karolinska Institutet4 aut
7102 a Karolinska Institutetb Section of Pharmacogenetics, Department of Physiology and Pharmacology, Karolinska Institutet, SE-17177 Stockholm4 org
7730 t Journal of Biological Chemistryg 287:9, s. 6307-6317q 287:9<6307-6317x 0021-9258x 1083-351X
8564 8u https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-169793
8564 8u https://doi.org/10.1074/jbc.M111.328237
8564 8u http://kipublications.ki.se/Default.aspx?queryparsed=id:124163667

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