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Galvagni, F., Pennacchini, S., Salameh, A., Rocchigiani, M., Neri, F., Orlandini, M. et al.(2010) Endothelial cell adhesion to the extracellular matrix induces c-Src-dependent VEGFR-3 phosphorylation without the activation of the receptor intrinsic kinase activity. Circulation Research, 106, 1839-1848. doi:10.1161/CIRCRESAHA.109.206326

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• TITLE: The role of Src family kinases in mediating M-CSF receptor signaling and monocytic cell survival

  AUTHORS: Yijie Wang, Melissa G. Piper, Clay B. Marsh

  KEYWORDS: Monocyte/Macrophage; M-CSF Receptor; Src Family Kinases; Cell Survival

  JOURNAL NAME: Advances in Bioscience and Biotechnology, Vol.3 No.5, September 21, 2012

  ABSTRACT: Previously, we reported that M-CSF induced monocyte survival through the activation of Akt, p38MAPK and Erk1/2 kinases. Here, we found that Src family kinases were upstream of these kinases and played a central role in regulating M-CSF-induced monocyte survival. We observed that M-CSF promoted c-Src activation in monocytes and MDMs in a time-dependent manner. Src inhibitors reduced M-CSF-mediated phosphorylation of the M-CSF receptor (M-CSFR), Akt, Erk1/2, and p38 MAPK. We also observed that Src directly phosphorylated the M-CSFR. Notably, the inhibitors blocked phosphorylation of specific tyrosine residues within the M-CSFR. We further demonstrated that the Src inhibitor, PP2, attenuated M-CSF-induced NF-κB activation and M-CSF-induced monocyte survival. These findings indicated that Src family kinases mediate monocyte survival through the regulation of receptor phosphorylation and modulation of downstream signaling events. Thus, we predict that targeting Src family kinases may have therapeutic implication in inflammatory diseases.