Characterization of the plasma-membrane calcium pump from Trypanosoma cruzi

Despite previous reports [McLaughlin (1985) Mol. Biochem. Parasitol. 15, 189-201; Ghosh, Ray, Sarkar and Bhaduri (1990) J. Biol. Chem. 265, 11345-11351; Mazumder, Mukherjee, Ghosh. Ray and Bhaduri (1992) J. Biol. Chem. 267, 18440-18446] suggesting that the plasma-membrane Ca2+-ATPases of different t...

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Bibliographic Details
Published in:Biochemical journal 1995-02, Vol.306 (1), p.299-303
Main Authors: Benaim, G, Moreno, S.N.J, Hutchinson, G, Cervino, V, Hermoso, T, Romero, P.J, Ruiz, F, Souza, W. de, Docampo, R
Format: Article
Language:English
Subjects:
adenosinetriphosphatase
Animals
Antibodies, Monoclonal - immunology
calcium
Calcium-Transporting ATPases - immunology
Calcium-Transporting ATPases - isolation & purification
Calcium-Transporting ATPases - metabolism
calmodulin
Calmodulin - pharmacology
Cattle
Cell Membrane - enzymology
chromatography
Chromatography, Affinity
Epitopes - immunology
Erythrocytes - enzymology
Humans
inorganic ions
Microscopy, Electron
plasma membrane
purification
Swine
Trypanosoma cruzi
Trypanosoma cruzi - enzymology
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Summary:Despite previous reports [McLaughlin (1985) Mol. Biochem. Parasitol. 15, 189-201; Ghosh, Ray, Sarkar and Bhaduri (1990) J. Biol. Chem. 265, 11345-11351; Mazumder, Mukherjee, Ghosh. Ray and Bhaduri (1992) J. Biol. Chem. 267, 18440-18446] suggesting that the plasma-membrane Ca2+-ATPases of different trypanosomatids differ from the Ca2+ pumps present in mammalian cells, Trypanosoma cruzi plasma-membrane Ca2+-ATPase shares several characteristics with the Ca2+ pumps present in other systems. This enzyme could be partially purified from epimastigote plasma-membrane vesicles using calmodulin agarose affinity chromatography. The activity of the partially purified enzyme was stimulated by T. cruzi or bovine brain calmodulin. In addition, the enzyme cross-reacted with antiserum and monoclonal antibody 5F10 raised against human red-bloodcell Ca2t-ATPase, has a molecular mass of 140 kDa and forms Ca2+-dependent hydroxylamine-sensitive phosphorylated intermediates. These results, together with its high sensitivity to vanadate, indicate that this enzyme belongs to the P-type class of ionic pumps.
ISSN:0264-6021
1470-8728
DOI:10.1042/bj3060299