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J Biol Chem, Vol. 273, Issue 34, 22151-22158, August 21, 1998
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From the The vacuolar-type proton-translocating
pyrophosphatase (V-H+-PPase) is an enzyme previously
described in detail only in plants. This paper demonstrates its
presence in the trypanosomatid Trypanosoma cruzi.
Pyrophosphate promoted organellar acidification in permeabilized amastigotes, epimastigotes, and trypomastigotes of T. cruzi. This activity was stimulated by K+ ions and
was inhibited by Na+ ions and pyrophosphate analogs, as is
the plant activity. Separation of epimastigote extracts on Percoll
gradients yielded a dense fraction that contained H+-PPase
activity measured both by proton uptake and phosphate release but
lacked markers for mitochondria, lysosomes, glycosomes, cytosol, and
plasma membrane. Antiserum raised against specific sequences of the
plant V-H+-PPase cross-reacted with a T. cruzi
protein, which was also detectable in the dense Percoll fraction. The
organelles in this fraction appeared by electron microscopy to consist
mainly of acidocalcisomes (acidic calcium storage organelles). This
identification was confirmed by x-ray microanalysis. Immunofluorescence
and immunoelectron microscopy indicated that the V-H+-PPase
was located in the plasma membrane and acidocalcisomes of the three
different forms of the parasite. Pyrophosphate was able to drive
calcium uptake in permeabilized T. cruzi. This uptake depended upon a proton gradient and was reversed by a specific V-H+-PPase inhibitor. Our results imply that the
phylogenetic distribution of V-H+-PPases is much wider than
previously perceived but that the enzyme has a unique subcellular
location in trypanosomes.
Laboratory of Molecular Parasitology,
Department of Pathobiology, University of Illinois, Urbana,
Illinois 61802 and § Instituto de Biofísica Carlos
Chagas Filho, Universidade Federal do Rio de Janeiro, 21941, Rio de Janeiro, RJ, Brazil
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