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Cited by 133Trypanosoma species research and implicationsCellular transport and secretionResearch on Leishmaniasis Studies

Endocytosis of gold-labeled proteins and LDL byTrypanosoma cruzi

José Soares, Maurílio, de Souza, Wanderley·1991·Parasitology Research
DOI 10.1007/bf00928410
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Abstract

Endocytosis was studied at the ultrastructural level in different developmental forms of Trypanosoma cruzi after incubation of the parasites in the presence of gold-labeled proteins (albumin-Au, peroxidase-Au and transferrin-Au) and low-density lipoprotein (LDL-Au). Epimastigote (culture) forms actively ingested LDL and proteins. Initially, gold particles were seen adhering only to the cytostome and inside the flagellar pocket. In parasites incubated at 4 degrees C with transferrin-Au or peroxidase-Au, labeling was found only at these two sites, showing that receptor-mediated endocytosis occurs in both regions. In the cytoplasm, gold particles were seen only inside two different compartments: membrane-bound vesicles and reservosomes. Incubation of epimastigotes with acridine orange followed by fluorescence microscopy revealed intense orange staining, indicating that the reservosomes have an acidic pH. This staining was abolished after incubation of the parasites in the presence of ammonium chloride. These data confirm that this compartment is the site of accumulation of ingested lipids and proteins. Little intracellular labeling with transferrin-Au was found in in vitro-derived amastigotes and trypomastigotes (both lack reservosomes). However, although in amastigotes very few gold particles were seen bound to the cells, in trypomastigotes they were observed bound to the membrane that encloses the cell body, the flagellar pocket, and the flagellum, suggesting that the receptors are more abundant in this form.

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  • The T. brucei genome contains only one IRP-related gene.

    “The T. brucei genome contains only one IRP-related gene, which suggests that a different mechanism, a different type of transacting factor, is responsible for Fe sensing and regulation of transferrin receptor mRNA in this protozoan [91, 92].”

    From Strategies of intracellular pathogens for obtaining iron from the environment (2015) · cites this paper as [92]

  • A different mechanism, a different type of transacting factor, is responsible for Fe sensing and regulation of transferrin receptor mRNA in T. brucei.

    “The T. brucei genome contains only one IRP-related gene, which suggests that a different mechanism, a different type of transacting factor, is responsible for Fe sensing and regulation of transferrin receptor mRNA in this protozoan [91, 92].”

    From Strategies of intracellular pathogens for obtaining iron from the environment (2015) · cites this paper as [92]

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Authors
José Soares, M., & de Souza, W.
Venue
Parasitology Research
Publisher
Springer Science and Business Media LLC
Published
1991-06
Volume
77
Issue
6
Pages
461-468
ISSN
  • 0044-3255 (ISSN-L)
  • 0932-0113
  • 1432-1955
DOI
10.1007/bf00928410
OpenAlex
W1998626269
Cited by
133
References
38
Citations by year
2025: 6 · 2024: 4 · 2023: 3 · 2022: 3 · 2021: 8 · 2020: 8 · 2019: 1 · 2018: 5 · 2017: 7 · 2016: 2 · 2015: 5 · 2014: 6 · 2013: 3 · 2012: 3
FWCI
2.22
Type
journal article
Language
en
Open access
closed
Licence
www.springer.com/tdm (tdm)
Locations
  • Parasitology Research (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Health Sciences › Medicine › Epidemiology › Trypanosoma species research and implications
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
  • Health Sciences › Medicine › Public Health, Environmental and Occupational Health › Research on Leishmaniasis Studies
Keywords
Trypanosoma cruzi, endocytosis, receptor-mediated endocytosis, low-density lipoprotein uptake, reservosomes, flagellar pocket, epimastigotes, amastigotes, trypomastigotes, intracellular pH, membrane vesicles, developmental forms
MeSH terms
Albumins, Animals, Endocytosis, Gold, Lipoproteins, LDL, Microscopy, Electron, Microscopy, Fluorescence, Peroxidase, Proteins, Transferrin, Trypanosoma cruzi

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