The glycosomal-membrane associated phosphoglycerate kinase isoenzyme A plays a role in sustaining the glucose flux in Trypanosoma cruzi epimastigotes

•In T. cruzi epimastigotes, PGKA is associated to the glycosomal membrane.•At least part of the 80 amino-acids insertion in PGKA is exposed to the cytosol.•The PGKA isoenzyme contributes to sustaining glycolysis through T. cruzi glycosomes. In Trypanosoma cruzi three isoenzymes of phosphoglycerate k...

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Bibliographic Details
Published in:Molecular and biochemical parasitology 2015-03, Vol.200 (1-2), p.5-8
Main Authors: Barros-Álvarez, Ximena, Cáceres, Ana J., Ruiz, Maria T., Michels, Paul A.M., Concepción, Juan Luis, Quiñones, Wilfredo
Format: Article
Language:English
Subjects:
Biological Transport
Carbohydrate metabolism regulation
Chagas Disease - parasitology
Cytosol - enzymology
Digitonin
Glucose - metabolism
Glycolysis
Humans
Intracellular Membranes - enzymology
Intracellular Membranes - metabolism
Isoenzymes - genetics
Isoenzymes - metabolism
Microbodies - enzymology
Osmotic shock
Phosphoglycerate kinase
Phosphoglycerate Kinase - genetics
Phosphoglycerate Kinase - metabolism
Protozoan Proteins - genetics
Protozoan Proteins - metabolism
Trypanosoma cruzi
Trypanosoma cruzi - enzymology
Trypanosoma cruzi - genetics
Trypanosoma cruzi - growth & development
Trypanosoma cruzi - metabolism
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Summary:•In T. cruzi epimastigotes, PGKA is associated to the glycosomal membrane.•At least part of the 80 amino-acids insertion in PGKA is exposed to the cytosol.•The PGKA isoenzyme contributes to sustaining glycolysis through T. cruzi glycosomes. In Trypanosoma cruzi three isoenzymes of phosphoglycerate kinase (PGK) are found which are simultaneously expressed: the cytosolic isoenzyme PGKB as well as two glycosomal enzymes, PGKA and PGKC. In this paper, we show that PGKA in T. cruzi epimastigotes is associated to the glycosomal membrane; it is responsible for about 23% of the glycosomal PGK activity, the fraction that remains in the pellet after osmotic shock treatment of purified organelles, in contrast to the 77% soluble activity that is mainly attributed to PGKC. Antibodies against the unique 80 amino-acid insertion of PGKA blocked almost completely the glucose consumption by epimastigotes that were partially permeabilized with digitonin. These results indicate that PGKA is the predominant isoenzyme for sustaining glycolysis through the glycosomes of these parasites.
ISSN:0166-6851
1872-9428
DOI:10.1016/j.molbiopara.2015.04.003