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A more recent version of this article appeared on February 1, 2004
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Submitted on July 3, 2003
Revised on September 12, 2003
Accepted on September 30, 2003
1 CIHR Group in Matrix Dynamics, University of Toronto, Toronto, Ontario, CANADA
2 Dept. of Surgery, University Health Network, University of Toronto, Toronto, Ontario, CANADA
3 Dept. of Hematology, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts, USA
* Corresponding author. E-mail address: christopher.mccculloch{at}utoronto.ca.
The role of gelsolin, a calcium-dependent actin severing protein,
in mediating collagen phagocytosis, is not defined. We examined
2
1 integrin-mediated phagocytosis in fibroblasts from
wild-type (WT) and gelsolin knock-out (Gsn-) mice. After
initial contact with collagen beads, collagen binding and
internalization were 60% lower in Gsn- than WT cells.
This deficiency was restored by transfection with gelsolin or with 1
integrin-activating antibodies. WT cells showed robust rac
activation and increased [Ca2+]i during early
contact with collagen beads but Gsn- cells showed very
limited responses. Transfected gelsolin in Gsn- cells
restored rac activation after collagen binding. Transfection of
Gsn- cells with active rac increased collagen binding to
WT levels. Chelation of intracellular calcium inhibited collagen
binding and rac activation while calcium ionophore induced rac
activation in WT and Gsn- cells. We conclude that the
ability of gelsolin to remodel actin filaments is important for
collagen-induced calcium entry; calcium in turn is required for rac
activation which subsequently enhances collagen binding to unoccupied
21 integrins.
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