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J Biol Chem, Vol. 273, Issue 18, 11144-11149, May 1, 1998
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From the Integrin-mediated interaction with the
extracellular matrix plays a critical role in the function of
osteoclasts, the bone-resorbing cells. This study examines the role of
p130Cas (Crk-associated
substrate (Cas)) in actin organization in osteoclasts. Multinucleated osteoclast-like cells (OCLs) were obtained in a co-culture of murine bone marrow cells and primary osteoblasts. After
plating on culture dishes, OCLs formed a ringlike structure consisting
of F-actin dots at cell periphery (actin ring). The percentage of OCLs
with actin rings and its diameter increased with time and cell
spreading. Tyrosine phosphorylation of a protein (p130) increased with
actin ring formation. Treatment with cytochalasin D disrupted actin
rings and reduced tyrosine phosphorylation of p130. Using specific
antibodies, p130 was identified as Cas. By immunocytochemistry, Cas was
localized to the peripheral regions of OCLs and its distribution
overlapped that of F-actin. In OCLs derived from Src( Departments of Biochemistry and Oral
Anatomy, School of Dentistry, Showa University, 1-5-8 Hatanodai,
Shinagawa-ku, Tokyo 142, Japan and the § Department of Bone
Biology, Merck Research Laboratories,
West Point, Pennsylvania 19486
/) mice, in
which osteoclast activity is severely compromised, tyrosine
phosphorylation of Cas was markedly reduced. Moreover, Cas was
diffusely distributed in the cytoplasm and actin ring formation is not
observed. These findings suggest that Src-dependent tyrosine phosphorylation of Cas is involved in the adhesion-induced actin organization associated with osteoclast activation.
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