A. Lukic

B. Samuelsson

Brungs

D. Basavarajappa

D. Steinhilber

Esser

Evans

Ferguson

Gilbert

Haeggstro  m

Kulkarni

Levy

M. Wan

O. Radmark

Provost

Radmark

Werz

Significance
          
            5-Lipoxygenase (5LO) is a key enzyme in biosynthesis of leukotrienes (LTs), lipid mediators of inflammation. To study the roles of the 5LO accessory proteins coactosin-like protein (CLP) and 5LO-activating protein (FLAP), we knocked down these proteins in human monocytic cells. Our results show that expression of CLP was required for full cellular 5LO activity when cells were activated with Ca
            2+
            ionophore, as well as with a physiological stimulus (lipopolysaccharide followed by N-formylmethionyl-leucyl-phenylalanine). During LT biosynthesis in stimulated cells, 5LO typically translocates to the nuclear membrane. This redistribution, from cytosolic to perinuclear, was clearly compromised in both CLP- and FLAP-deficient cells. Our results suggest that the CLP–5LO interaction may be a target for reduced LT production.
          </jats:p

Devaraj Basavarajappa

Min Wan

Ana Lukic

Dieter Steinhilber

Bengt Samuelsson

Olof Rådmark

Crossref

Proceedings of the National Academy of Sciences

Roles of coactosin-like protein (CLP) and 5-lipoxygenase-activating protein (FLAP) in cellular leukotriene biosynthesis

Roles of coactosin-like protein (CLP) and 5-lipoxygenase-activating protein (FLAP) in cellular leukotriene biosynthesis

Abstract

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