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Vol. 12, Issue 7, 2061-2073, July 2001
*Department of Ultrastructures, Istituto Superiore di Sanità,
00161, Rome, Italy; Macropinocytosis, a ruffling-driven process that allows the capture
of large material, is an essential aspect of normal cell function. It
can be either constitutive, as in professional phagocytes where it ends
with the digestion of captured material, or induced, as in epithelial
cells stimulated by growth factors. In this case, the internalized
material recycles back to the cell surface. We herein show that
activation of Rho GTPases by a bacterial protein toxin, the
Escherichia coli cytotoxic necrotizing factor 1 (CNF1), allowed epithelial cells to engulf and digest apoptotic cells in a
manner similar to that of professional phagocytes. In particular, we
have demonstrated that 1) the activation of all Rho, Rac, and Cdc42 by
CNF1 was essential for the capture and internalization of apoptotic
cells; and 2) such activation allowed the discharge of macropinosomal
content into Rab7 and lysosomal associated membrane protein-1 acidic
lysosomal vesicles where the ingested particles underwent degradation.
Taken together, these findings indicate that CNF1-induced "switching
on" of Rho GTPases may induce in epithelial cells a scavenging
activity, comparable to that exerted by professional phagocytes. The
activation of such activity in epithelial cells may be relevant, in
mucosal tissues, in supporting or integrating the scavenging activity
of resident macrophages.
Department of Immunology, Istituto
Superiore di Sanità, 00161, Rome, Italy; and
§Institut National de la Santé et de la Recerche
Médicale U452, Faculté de Médecine, 06107, Nice Cedex 2, France
Corresponding author. E-mail address:
carla.fiorentini{at}iss.it.
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