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(Received for publication, December 7, 1994) Vacuolar membrane vesicles were isolated from Candida
albicans protoplasts, and marker enzyme assays were employed to
identify the membranes as vacuolar in origin. The mechanisms of
Ca
Volume 270,
Number 13,
Issue of March 31, 1995 pp. 7272-7280
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
Mobilization Pathways at the Vacuolar Membrane of Candida
albicans
uptake and Ca
release at the
vacuolar membrane were investigated. Ca
accumulation
by vacuolar membrane vesicles can be generated via
H
/Ca
antiport. The inside-acid pH is
in turn generated by a vacuolar-type H
-ATPase, as
demonstrated by the sensitivity of Ca
uptake to
ionophores and the vacuolar H
-ATPase inhibitor
bafilomycin A
. Vacuolar membrane vesicles exhibit two
Ca
release pathways: one induced by inositol
1,4,5-trisphosphate (InsP
) and the other by inside-positive
voltage. These two pathways are distinct with respect to the amount of
Ca
released, the nature of response to successive
stimuli, and their respective pharmacological profiles. The
InsP
-gated pathway exhibits a K
for
InsP
of 2.4 µM but is not activated by
inositol 4,5-bisphosphate or inositol 1,3,4,5-tetrakisphosphate at
concentrations up to 50 µM. Ca
release
by InsP
is blocked partially by low molecular weight
heparin. Ca
released by the voltage-sensitive pathway
occurs at membrane potentials estimated to be over a physiological
range from 0 to 80 mV. The voltage-sensitive Ca
release pathway can be blocked by lanthanide ions and organic
channel blockers such as ruthenium red and verapamil. Furthermore, the
voltage-sensitive Ca
release pathway exhibits
Ca
-induced Ca
release. These
findings are discussed in relation to the mechanism of
Ca
-mediated cellular signaling in C. albicans and other fungi.
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