|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
3
|
|
pubmed:dateCreated |
1994-10-19
|
|
pubmed:abstractText |
5-Lipoxygenase-activating protein is required for cellular leukotriene synthesis and is the target of the leukotriene biosynthesis inhibitors MK-886 (3-[1-(p-chlorophenyl)-5-isopropyl-3-tert-butylthio-1H- indol-2-yl]-2,2-dimethylpropanoic acid) and MK-591 (3-[1-(4-chlorobenzyl)-3-(t-butylthio)-5-(quinolin-2-ylmethoxy)-indol-2-yl] - 2,2-dimethylpropanoic acid). Recent studies demonstrate that 5-lipoxygenase-activating protein binds arachidonic acid and stimulates the utilization of this substrate by 5-lipoxygenase. The present study utilizes a radioligand binding assay to assess the affinity of 5-lipoxygenase-activating protein for arachidonic acid and the specificity of the fatty acid binding site on 5-lipoxygenase-activating protein. Our findings demonstrate that the presence of a free carboxyl group on fatty acids or leukotriene biosynthesis inhibitors which interact with 5-lipoxygenase-activating protein is not required for specific binding to the protein. However, the degree of saturation significantly affects the affinity of fatty acids for 5-lipoxygenase-activating protein.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/12-Hydroxy-5,8,10,14-eicosatetraenoi...,
http://linkedlifedata.com/resource/pubmed/chemical/15-hydroxy-5,8,11,13-eicosatetraenoi...,
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/Arachidonic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Hydroxyeicosatetraenoic Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Indoles,
http://linkedlifedata.com/resource/pubmed/chemical/L 663536,
http://linkedlifedata.com/resource/pubmed/chemical/L 691831,
http://linkedlifedata.com/resource/pubmed/chemical/Leukotrienes,
http://linkedlifedata.com/resource/pubmed/chemical/MK 0591,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Quinolines
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
May
|
|
pubmed:issn |
0014-2999
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
17
|
|
pubmed:volume |
267
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
275-80
|
|
pubmed:dateRevised |
2010-11-18
|
|
pubmed:meshHeading |
pubmed-meshheading:8088366-12-Hydroxy-5,8,10,14-eicosatetraenoic Acid,
pubmed-meshheading:8088366-5-Lipoxygenase-Activating Proteins,
pubmed-meshheading:8088366-Arachidonic Acid,
pubmed-meshheading:8088366-Binding Sites,
pubmed-meshheading:8088366-Carrier Proteins,
pubmed-meshheading:8088366-Humans,
pubmed-meshheading:8088366-Hydroxyeicosatetraenoic Acids,
pubmed-meshheading:8088366-Indoles,
pubmed-meshheading:8088366-Leukocytes,
pubmed-meshheading:8088366-Leukotrienes,
pubmed-meshheading:8088366-Membrane Proteins,
pubmed-meshheading:8088366-Quinolines,
pubmed-meshheading:8088366-Radioligand Assay
|
|
pubmed:year |
1994
|
|
pubmed:articleTitle |
Structural requirements for the binding of fatty acids to 5-lipoxygenase-activating protein.
|
|
pubmed:affiliation |
Department of Biochemistry, Merck Frosst Centre For Therapeutic Research, Pointe Claire-Dorval, Quebec, Canada.
|
|
pubmed:publicationType |
Journal Article
|
