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J. Biol. Chem., Vol. 277, Issue 10, 8146-8153, March 8, 2002
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From the Laboratory of Molecular Parasitology, Department of
Pathobiology, University of Illinois at Urbana-Champaign,
Urbana, Illinois 61802
The mass-dense granules of Dictyostelium
discoideum were shown to contain large amounts of phosphorus,
magnesium, and calcium, as determined by x-ray microanalysis, either
in situ or when purified using iodixanol gradient
centrifugation. The high phosphorus content was due to the
presence of pyrophosphate and polyphosphate, which were also
present in the contractile vacuoles. Both organelles also possessed a
vacuolar H+-ATPase, an
H+-pyrophosphatase, and a Ca2+-ATPase, as
determined by biochemical methods or by immunofluorescence microscopy.
The H+-pyrophosphatase activity of isolated mass-dense
granules was stimulated by potassium ions and inhibited by the
pyrophosphate analogs aminomethylenediphosphonate and
imidodiphosphate and by KF and N-ethylmaleimide in a
dose-dependent manner. The mass-dense granules and the
contractile vacuole appeared to contact each other when the cells were
submitted to hyposmotic stress. Acetazolamide inhibited the carbonic
anhydrase activity of the contractile vacuoles and prolonged their
contraction cycle in a dose-dependent manner. Similar
effects were observed with the anion exchanger inhibitor 4,4'-diisothiocyanatodihydrostilbene-2, 2'-disulfonic acid and the vacuolar H+-ATPase inhibitor bafilomycin
A1. Together, these results suggest that the mass-dense
granules of D. discoideum are homologous to the
acidocalcisomes described in protozoan parasites and are linked to the
function of the contractile vacuole.
Acidocalcisomes Are Functionally Linked to the Contractile
Vacuole of Dictyostelium discoideum*
,,
*
This work was supported in part by National Institutes of
Health Grant AI-23259 (to R. 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.
Both authors contributed equally to this work.
§
To whom correspondence should be addressed: Lab. of Molecular
Parasitology, Dept. of Pathobiology, College of Veterinary Medicine, University of Illinois at Urbana-Champaign, 2001 South Lincoln Ave.,
Urbana, IL 61802. Tel.: 217-333-3845; Fax: 217-244-7421; E-mail:
rodoc@uiuc.edu.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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