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5-Lipoxygenase
(5LO) (Provost et
al, 2001) an
enzyme pivotally involved in the production of leukotrienes from arachidonic
acid. 5LO is itself an actin-binding protein (Lepley
& Fitzpatrick, 1994;
Provost et al,
2001). A
17 kDa actin-binding protein coactosin,
originally
isolated from Dictyostelium (de
Hostos et al, 1993)
has
since found in humans where it has been discovered to be a binding partner for 5LO.
The
human version of coactosin is named CLP (Coactosin-Like Protein). Another
lipoxygenase, 12/15-lipoxygenase (12/15LO) has been implicated in actin
polymerization in macrophages (Miller
et al, 2001),
this enzyme catalyses the peroxylation of double bonds of fatty acids.
References:-
de Hostas, E. L., B. Bradtke, et al.
(1993). “Coactosin, a 17 kDa F-actin binding protein from Dictyostelium
discoideum.” Cell
Mot.Cytoskeleton 26, 181-191.
Lepley, R.A. &
Fitzpatrick, F.A. (1994). J.Biol.Chem. 269, 24163-24168
Miller, Y. I., Cang, M.-K., Funk, C. D.,
Feramisco, J. R. & Witztum, J. L. (2001) 12/15-lipoxygenase translocation
enhances site-specific actin polymerization in marcophages phagocytosing
apoptotic cells., J.Biol.Chem. 276, 194310-19439.
Provost, P., Doucet, J., Hammarberg, T.,
Gerisch, G., Samuelsson, B. & Radmark, O. (2001) 5-Lipoxygenase interacts
with coactosin-like protein., J. Biol.Chem. 276, 16520-16527.
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