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The glycosomal-membrane associated phosphoglycerate kinase isoenzyme A plays a role in sustaining the glucose flux in Trypanosoma cruzi epimastigotes
- Source :
- Molecular and Biochemical Parasitology. 200:5-8
- Publication Year :
- 2015
- Publisher :
- Elsevier BV, 2015.
-
Abstract
- 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.
- Subjects :
- Trypanosoma cruzi
Protozoan Proteins
Biology
Microbodies
Isozyme
Glycosome
chemistry.chemical_compound
Cytosol
Organelle
Humans
Chagas Disease
Glycolysis
Molecular Biology
Phosphoglycerate kinase
Biological Transport
Intracellular Membranes
biology.organism_classification
Molecular biology
Isoenzymes
Phosphoglycerate Kinase
Glucose
Digitonin
Biochemistry
chemistry
Parasitology
Subjects
Details
- ISSN :
- 01666851
- Volume :
- 200
- Database :
- OpenAIRE
- Journal :
- Molecular and Biochemical Parasitology
- Accession number :
- edsair.doi.dedup.....df2ce1816ee9337c9378e802d2ab10bb
- Full Text :
- https://doi.org/10.1016/j.molbiopara.2015.04.003