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J Biol Chem, Vol. 273, Issue 29, 18122-18129, July 17, 1998
From the Aerolysin is a pore-forming toxin that plays a
key role in the pathogenesis of Aeromonas hydrophila
infections. In this study, we have analyzed the effect of aerolysin on
human granulocytes (HL-60 cells). Proaerolysin could bind to these
cells, was processed into active aerolysin, and led to membrane
depolarization, indicating that granulocytes are potential targets for
this toxin. Fura-2 measurements were used to analyze the effect of
aerolysin on cytosolic [Ca2+] homeostasis. As expected
for a pore-forming toxin, aerolysin addition led to Ca2+
influx across the plasma membrane. In addition, the toxin triggered Ca2+ release from agonist and thapsigargin-sensitive
intracellular Ca2+ stores. This Ca2+ release
was independent of the aerolysin-induced Ca2+ influx and
occurred in two kinetically distinct phases: an initial rapid and
transient phase and a second, more sustained, phase. The first, but not
the second phase was sensitive to pertussis toxin. Activation of
pertussis toxin-sensitive G-proteins appeared to be a consequence of
pore formation, rather than receptor activation through
aerolysin-binding, as it: (i) was not observed with a binding
competent, insertion-incompetent aerolysin mutant, (ii) had a marked
lag time, and (iii) was also observed in response to other bacterial
pore-forming toxins (staphylococcal
Aerolysin Induces G-protein Activation and Ca2+
Release from Intracellular Stores in Human Granulocytes
,, and Infectious Diseases Division, University
Hospital, 1211 Geneva 14, Switzerland and the § Department
of Biochemistry, University of Geneva, 30 quai E. Ansermet,
1211 Geneva 4, Switzerland
-toxin, streptolysin O) which
are thought to bind to different receptors. G-protein activation
through pore-forming toxins stimulated cellular functions, as evidenced
by pertussis toxin-sensitive chemotaxis. Our results demonstrate that
granulocytes are potential target cells for aerolysin and that in these
cells, Ca2+ signaling in response to a pore-forming toxin
involves G-protein-dependent cell activation and
Ca2+ release from intracellular stores.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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