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Requirement of a 5-lipoxygenase-activating protein for leukotriene synthesis.

Authors: Dixon, RA  Diehl, RE  Opas, E  Rands, E  Vickers, PJ  Evans, JF  Gillard, JW  Miller, DK 
Citation: Dixon RA, etal., Nature 1990 Jan 18;343(6255):282-4.
Pubmed: (View Article at PubMed) PMID:2300173
DOI: Full-text: DOI:10.1038/343282a0

Leukotrienes, the biologically active metabolites of arachidonic acid, have been implicated in a variety of inflammatory responses, including asthma, arthritis and psoriasis. Recently a compound, MK-886, has been described that blocks the synthesis of leukotrienes in intact activated leukocytes, but has little or no effect on enzymes involved in leukotriene synthesis, including 5-lipoxygenase, in cell-free systems. A membrane protein with a high affinity for MK-886 and possibly representing the cellular target for MK-886 has been isolated from rat and human leukocytes. Here, we report the isolation of a complementary DNA clone encoding the MK-886-binding protein. We also demonstrate that the expression of both the MK-886-binding protein and 5-lipoxygenase is necessary for leukotriene synthesis in intact cells. Because the MK-886-binding protein seems to play a part in activating this enzyme in cells, it is termed the five-lipoxygenase activating protein (FLAP).


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CRRD Object Information
CRRD ID: 69749
Created: 2002-01-08
Species: All species
Last Modified: 2002-01-08
Status: ACTIVE


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