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5-Lipoxygenase

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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