The malate dehydrogenase isoforms from Trypanosoma brucei: Subcellular localization and differential expression in bloodstream and procyclic forms

Aranda, Alejandro; Maugeri, Dante; Uttaro, Antonio D.; Opperdoes, Frederik; Cazzulo, Juán José; Nowicki, Cristina

doi:10.1016/j.ijpara.2005.09.013

Cited by 25 publications

(19 citation statements)

References 36 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…brucei encodes three separate isoforms of malate dehydrogenase (MDH), localized to the mitochondrion, glycosomes and the cytosol, respectively [55]. The glycosomal isoform is reportedly absent from the BSF, while the cytosolic isoform is present at higher levels in BSF than procyclics [55]. Additionally a small amount of the mitochondrial isoform is reportedly present [55–57].…”

Section: Resultsmentioning

confidence: 99%

“…The glycosomal isoform is reportedly absent from the BSF, while the cytosolic isoform is present at higher levels in BSF than procyclics [55]. Additionally a small amount of the mitochondrial isoform is reportedly present [55–57]. The succinate fermentation pathway therefore might involve oxaloacetate produced in the glycosome via PEPCK which might re-enter the cytosol and possibly the mitochondrion for further metabolism.…”

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Probing the Metabolic Network in Bloodstream-Form Trypanosoma brucei Using Untargeted Metabolomics with Stable Isotope Labelled Glucose

et al. 2015

View full text Add to dashboard Cite

Metabolomics coupled with heavy-atom isotope-labelled glucose has been used to probe the metabolic pathways active in cultured bloodstream form trypomastigotes of Trypanosoma brucei, a parasite responsible for human African trypanosomiasis. Glucose enters many branches of metabolism beyond glycolysis, which has been widely held to be the sole route of glucose metabolism. Whilst pyruvate is the major end-product of glucose catabolism, its transamination product, alanine, is also produced in significant quantities. The oxidative branch of the pentose phosphate pathway is operative, although the non-oxidative branch is not. Ribose 5-phosphate generated through this pathway distributes widely into nucleotide synthesis and other branches of metabolism. Acetate, derived from glucose, is found associated with a range of acetylated amino acids and, to a lesser extent, fatty acids; while labelled glycerol is found in many glycerophospholipids. Glucose also enters inositol and several sugar nucleotides that serve as precursors to macromolecule biosynthesis. Although a Krebs cycle is not operative, malate, fumarate and succinate, primarily labelled in three carbons, were present, indicating an origin from phosphoenolpyruvate via oxaloacetate. Interestingly, the enzyme responsible for conversion of phosphoenolpyruvate to oxaloacetate, phosphoenolpyruvate carboxykinase, was shown to be essential to the bloodstream form trypanosomes, as demonstrated by the lethal phenotype induced by RNAi-mediated downregulation of its expression. In addition, glucose derivatives enter pyrimidine biosynthesis via oxaloacetate as a precursor to aspartate and orotate.

show abstract

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Probing the Metabolic Network in Bloodstream-Form Trypanosoma brucei Using Untargeted Metabolomics with Stable Isotope Labelled Glucose

et al. 2015

View full text Add to dashboard Cite

show abstract

“…538 Confocal fluorescence microscopy of immuno-labeled malate dehydrogenase confirmed that malate dehydrogenases were localized in the cytosolic, glycosomal or mitochondrial regions. In the cytosol, this enzyme was responsible for reducing oxaloacetate to malate in the glycolysis pathway.…”

Section: Organelle Functionmentioning

confidence: 88%

Bioanalysis of Eukaryotic Organelles

et al. 2013

View full text Add to dashboard Cite

“…Nearly 80% of the total activity in procyclic crude extracts corresponds to the former isozyme which also catalyzes, although less efficiently, the reduction of p-hydroxyphenyl-pyruvate. Importantly these studies helped to distinguish Trypanosoma brucei from Trypanosoma cruzi, since in the latter parasite a cytosolic malate dehydrogenase is not present and mitochondrial malate dehydrogenase specifically reduces oxaloacetate which can be very useful in diagnosis (ARANDA et al, 2006).…”

Section: Developmental Aspects Of Mdh Action and Functionsmentioning

confidence: 99%

HORMONE-DEPENDENT AND HORMONE-INDEPENDENT CONTROL OF METABOLIC AND DEVELOPMENTAL FUNCTIONS OF MALATE DEHYDROGENASE – Review

Danis

Farkas

2009

endo

View full text Add to dashboard Cite

The malate dehydrogenase isoforms from Trypanosoma brucei: Subcellular localization and differential expression in bloodstream and procyclic forms

Cited by 25 publications

References 36 publications

Probing the Metabolic Network in Bloodstream-Form Trypanosoma brucei Using Untargeted Metabolomics with Stable Isotope Labelled Glucose

Probing the Metabolic Network in Bloodstream-Form Trypanosoma brucei Using Untargeted Metabolomics with Stable Isotope Labelled Glucose

Bioanalysis of Eukaryotic Organelles

HORMONE-DEPENDENT AND HORMONE-INDEPENDENT CONTROL OF METABOLIC AND DEVELOPMENTAL FUNCTIONS OF MALATE DEHYDROGENASE – Review

Contact Info

Product

Resources

About

The malate dehydrogenase isoforms from Trypanosoma brucei: Subcellular localization and differential expression in bloodstream and procyclic forms

Cited by 25 publications

References 36 publications

Probing the Metabolic Network in Bloodstream-Form Trypanosoma brucei Using Untargeted Metabolomics with Stable Isotope Labelled Glucose

Probing the Metabolic Network in Bloodstream-Form Trypanosoma brucei Using Untargeted Metabolomics with Stable Isotope Labelled Glucose

Bioanalysis of Eukaryotic Organelles

HORMONE-DEPENDENT AND HORMONE-INDEPENDENT CONTROL OF METABOLIC AND DE­VEL­OP­MEN­TAL FUNCTIONS OF MALATE DEHYDROGENASE – Review

Contact Info

Product

Resources

About

HORMONE-DEPENDENT AND HORMONE-INDEPENDENT CONTROL OF METABOLIC AND DEVELOPMENTAL FUNCTIONS OF MALATE DEHYDROGENASE – Review