Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1993-3-30
pubmed:abstractText
5-Lipoxygenase-activating protein (FLAP) is an 18-kDa integral membrane protein which is essential for cellular leukotriene (LT) synthesis, and is the target of LT biosynthesis inhibitors. However, the mechanism by which FLAP activates 5-LO has not been determined. We have expressed high levels of human FLAP in Spodoptera frugiperda (Sf9) insect cells infected with recombinant baculovirus, and used this system to demonstrate that FLAP specifically binds [125I]L-739,059, a novel photoaffinity analog of arachidonic acid. This binding is inhibited by both arachidonic acid and MK-886, an LT biosynthesis inhibitor which specifically interacts with FLAP. These studies suggest that FLAP may activate 5-LO by specifically binding arachidonic acid and transferring this substrate to the enzyme.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/5-Lipoxygenase-Activating Proteins, http://linkedlifedata.com/resource/pubmed/chemical/ALOX5AP protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Affinity Labels, http://linkedlifedata.com/resource/pubmed/chemical/Arachidonate 5-Lipoxygenase, http://linkedlifedata.com/resource/pubmed/chemical/Arachidonic Acids, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Indoles, http://linkedlifedata.com/resource/pubmed/chemical/Iodine Radioisotopes, http://linkedlifedata.com/resource/pubmed/chemical/L 691831, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Quinolines, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
8
pubmed:volume
318
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
277-81
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:8440384-5-Lipoxygenase-Activating Proteins, pubmed-meshheading:8440384-Affinity Labels, pubmed-meshheading:8440384-Animals, pubmed-meshheading:8440384-Arachidonate 5-Lipoxygenase, pubmed-meshheading:8440384-Arachidonic Acids, pubmed-meshheading:8440384-Baculoviridae, pubmed-meshheading:8440384-Carrier Proteins, pubmed-meshheading:8440384-Cell Line, pubmed-meshheading:8440384-Enzyme Activation, pubmed-meshheading:8440384-Gene Expression, pubmed-meshheading:8440384-Humans, pubmed-meshheading:8440384-Indoles, pubmed-meshheading:8440384-Iodine Radioisotopes, pubmed-meshheading:8440384-Membrane Proteins, pubmed-meshheading:8440384-Moths, pubmed-meshheading:8440384-Photochemistry, pubmed-meshheading:8440384-Quinolines, pubmed-meshheading:8440384-Recombinant Proteins, pubmed-meshheading:8440384-Transfection
pubmed:year
1993
pubmed:articleTitle
5-lipoxygenase-activating protein is an arachidonate binding protein.
pubmed:affiliation
Department of Pharmacology, Merck Frosst Centre for Therapeutic Research, Quebec, Canada.
pubmed:publicationType
Journal Article