학술논문

Proteomic analysis of glycosomes from Trypanosoma cruzi epimastigotes.
Document Type
Article
Source
Molecular & Biochemical Parasitology. Apr2019, Vol. 229, p62-74. 13p.
Subject
*TRYPANOSOMA cruzi
*MEMBRANE proteins
*CHAGAS' disease
*SHOCK therapy
*PEROXISOMES
*GLYCOLYSIS
Language
ISSN
0166-6851
Abstract
Graphical abstract Highlights • New metabolic routes and membrane proteins were identified in the organelles. • Exponential and stationary growth-phase cells vary little in glycosomal proteins. • A variety of proteins bearing a typical PTS1 but with unknown function were found. Abstract In Trypanosoma cruzi , the causal agent of Chagas disease, the first seven steps of glycolysis are compartmentalized in glycosomes, which are authentic but specialized peroxisomes. Besides glycolysis, activity of enzymes of other metabolic processes have been reported to be present in glycosomes, such as β-oxidation of fatty acids, purine salvage, pentose-phosphate pathway, gluconeogenesis and biosynthesis of ether-lipids, isoprenoids, sterols and pyrimidines. In this study, we have purified glycosomes from T. cruzi epimastigotes, collected the soluble and membrane fractions of these organelles, and separated peripheral and integral membrane proteins by Na 2 CO 3 treatment and osmotic shock. Proteomic analysis was performed on each of these fractions, allowing us to confirm the presence of enzymes involved in various metabolic pathways as well as identify new components of this parasite's glycosomes. [ABSTRACT FROM AUTHOR]