Source:http://linkedlifedata.com/resource/pubmed/id/16112079
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2005-11-2
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pubmed:abstractText |
Mouse 8S-lipoxygenase (8-LOX) metabolizes arachidonic acid (AA) specifically to 8S-hydroperoxyeicosatetraenoic acid (8S-HPETE), which will be readily reduced under physiological circumstances to 8S-hydroxyeicosatetraenoic acid (8S-HETE), a natural agonist of peroxisome proliferator-activated receptor alpha (PPAR alpha). Here, we investigated whether 8-LOX could further oxygenate AA and whether the products could activate PPARs. The purified recombinant 8-LOX converted AA exclusively to 8S-HPETE and then to (8S,15S)-dihydroperoxy-5Z,9E,11Z,13E-eicosatetraenoic acid (8S,15S-diHPETE). The kcat/Km values for 8S-HPETE and AA were 3.3x10(3) and 2.7x10(4) M(-1) s(-1), respectively. 8-LOX also dioxygenated 8S-HETE and 15S-H(P)ETE specifically to the corresponding 8S,15S-disubstituted derivatives. By contrast, 15-LOX-2, a human homologue of 8-LOX, produced 8S,15S-diH(P)ETE from 8S-H(P)ETE but not from AA nor 15S-H(P)ETE. 8S,15S-diHETE activated PPAR alpha more strongly than 8S-HETE did. The present results suggest that 8S,15S-diH(P)ETE as well as 8S-H(P)ETE would contribute to the physiological function of 8-LOX and also that 8-LOX can function as a potential 15-LOX.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/ALOX15B protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Arachidonate 15-Lipoxygenase,
http://linkedlifedata.com/resource/pubmed/chemical/Hydroxyeicosatetraenoic Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoxygenase,
http://linkedlifedata.com/resource/pubmed/chemical/Oxygen,
http://linkedlifedata.com/resource/pubmed/chemical/PPAR alpha,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0006-291X
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pubmed:author |
pubmed-author:FushikiTohruT,
pubmed-author:GotoTsuyoshiT,
pubmed-author:IkedaIzumiI,
pubmed-author:IwanagaChitoseC,
pubmed-author:JisakaMitsuoM,
pubmed-author:KawadaTeruoT,
pubmed-author:NagayaTsutomuT,
pubmed-author:NishimuraKohjiK,
pubmed-author:TakahashiNobuyukiN,
pubmed-author:YamamotoTatsuyukiT,
pubmed-author:YokotaKazushigeK
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pubmed:issnType |
Print
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pubmed:day |
9
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pubmed:volume |
338
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
136-43
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:16112079-Animals,
pubmed-meshheading:16112079-Arachidonate 15-Lipoxygenase,
pubmed-meshheading:16112079-Humans,
pubmed-meshheading:16112079-Hydroxyeicosatetraenoic Acids,
pubmed-meshheading:16112079-Kinetics,
pubmed-meshheading:16112079-Lipoxygenase,
pubmed-meshheading:16112079-Mice,
pubmed-meshheading:16112079-Oxygen,
pubmed-meshheading:16112079-PPAR alpha,
pubmed-meshheading:16112079-Recombinant Proteins,
pubmed-meshheading:16112079-Substrate Specificity
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pubmed:year |
2005
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pubmed:articleTitle |
Double dioxygenation by mouse 8S-lipoxygenase: specific formation of a potent peroxisome proliferator-activated receptor alpha agonist.
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pubmed:affiliation |
Department of Life Science and Biotechnology, Shimane University, Matsue, Shimane 690-8504, Japan. jisaka@life.shimane-u.ac.jp
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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