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J Biol Chem, Vol. 275, Issue 19, 14615-14623, May 12, 2000
From the Molecular Biology Laboratory, Ludwig Institute for Cancer
Research, P. O. Box 2008, Royal Melbourne Hospital,
Victoria 3050, Australia
Src family tyrosine kinases have previously been
proposed to mediate some of the biological effects of
lipopolysaccharide on macrophages. Accordingly, we have sought to
identify substrates of Src family kinases in
lipopolysaccharide-stimulated macrophages. Stimulation of Bac1.2F5
macrophage cells with lipopolysaccharide was found to induce gradual
and persistent tyrosine phosphorylation of Cbl in an Src family
kinase-dependent manner. Immunoprecipitation experiments
revealed that Cbl associates with Hck in Bac1.2F5 cells, while
expression of an activated form of Hck in Bac1.2F5 cells induces
tyrosine phosphorylation of Cbl in the absence of lipopolysaccharide
stimulation. The Src homology 3 domain of Hck can directly bind Cbl,
and this interaction is important for phosphorylation of Cbl.
Association of the p85 subunit of phosphatidylinositol (PI) 3-kinase
with Cbl is enhanced following lipopolysaccharide stimulation of
Bac1.2F5 cells, and transient expression experiments indicate that
phosphorylation of Cbl by Hck can facilitate the association of p85
with Cbl. Lipopolysaccharide treatment also stimulates the partial
translocation of Hck to the cytoskeleton of Bac1.2F5 cells. Notably,
lipopolysaccharide enhances the adherence of Bac1.2F5 cells, an effect
that is dependent on the activity of Src family kinases and PI
3-kinase. Thus, we postulate that Hck enhances the adherence of
lipopolysaccharide-stimulated macrophages, at least in part, via Cbl
and PI 3-kinase.
Hck Enhances the Adherence of Lipopolysaccharide-stimulated
Macrophages via Cbl and Phosphatidylinositol 3-Kinase*
,
*
This work was supported in part by a grant from the National
Health and Medical Research Council (to G. S. and A. D.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.: 61-3-9341-3155;
Fax: 61-3-9341-3191; E-mail: Glen.Scholz@ludwig.edu.au.
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