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- W2034160242 abstract "Primary macrophages isolated from hck−/−fgr−/− mice display altered morphology and F-actin cytoskeletal structures and reduced migration. The ability of phorbol myristyl acetate (PMA), a protein kinase C activator that has been reported to increase macrophage spreading and carcinoma cell motility, to rescue these hck−/−fgr−/− defects was tested. Although PMA-treated wild-type and hck−/−fgr−/− macrophages exhibited a similar flattened, spread phenotype, PMA did not rescue the hck−/−fgr−/− macrophage migration defect. Instead, both PMA-treated wild type and hck−/−fgr−/− macrophages were defective in spontaneous and chemotactic migration and tyrosine phosphorylation of the Cbl protooncoprotein was decreased in both. Moreover, c-cbl−/− macrophages displayed the same impairment of motility as hck−/−fgr−/− macrophages and a similar morphology with less polarization and more dorsal ruffling than wild-type macrophages. As Hck and Fgr expression and activity were not decreased in c-cbl−/− macrophages, these results suggest that Cbl is likely to be an important downstream mediator of the Src family kinase-regulated macrophage motility pathway. © 2003 Wiley-Liss, Inc." @default.
- W2034160242 created "2016-06-24" @default.
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- W2034160242 date "2003-03-18" @default.
- W2034160242 modified "2023-10-10" @default.
- W2034160242 title "Expression and tyrosine phosphorylation of Cbl regulates macrophage chemokinetic and chemotactic movement" @default.
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- W2034160242 doi "https://doi.org/10.1002/jcp.10236" @default.
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