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Oxidized LDL/CD36 interaction induces loss of cell polarity and inhibits macrophage locomotion

Title
Oxidized LDL/CD36 interaction induces loss of cell polarity and inhibits macrophage locomotion
Authors
Park Y.M.Drazba J.A.Vasanji A.Egelhoff T.Febbraio M.Silverstein R.L.
Ewha Authors
박영미
SCOPUS Author ID
박영미scopus
Issue Date
2012
Journal Title
Molecular Biology of the Cell
ISSN
1059-1524JCR Link
Citation
vol. 23, no. 16, pp. 3057 - 3068
Indexed
SCI; SCIE; SCOPUS scopus
Abstract
Cell polarization is essential for migration and the exploratory function of leukocytes. However, the mechanism by which cells maintain polarity or how cells revert to the immobilized state by gaining cellular symmetry is not clear. Previously we showed that interaction between oxidized low-density lipoprotein (oxLDL) and CD36 inhibits macrophage migration; in the current study we tested the hypothesis that oxLDL/CD36-induced inhibition of migration is the result of intracellular signals that regulate cell polarity. Live cell imaging of macrophages showed that oxLDL actuated retraction of macrophage front end lamellipodia and induced loss of cell polarity. Cd36 null and macrophages null for Vav, a guanine nucleotide exchange factor (GEF), did not show this effect. These findings were caused by Rac-mediated inhibition of nonmuscle myosin II, a cell polarity determinant. OxLDL induced dephosphorylation of myosin regulatory light chain (MRLC) by increasing the activity of Rac. Six-thioguanine triphosphate (6-thio-GTP), which inhibits Vav-mediated activation of Rac, abrogated the effect of oxLDL. Activation of the Vav-Rac-myosin II pathway by oxidant stress may induce trapping of macrophages at sites of chronic inflammation such as atherosclerotic plaque. © 2012 Park et al.
DOI
10.1091/mbc.E11-12-1051
Appears in Collections:
의학전문대학원 > 의학과 > Journal papers
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