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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.


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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