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PMID: 8920013 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Enhanced acquisition of purine nucleosides and nucleobases by purine-starved Crithidia luciliae.

Molecular and biochemical parasitology ·Vol. 76 ·No. 1-2 ·1996-00-00 ·Pages 279-87

Alleman MM, Gottlieb M

Abstract

The effects of purine starvation on the ability of the trypanosomatid Crithidia luciliae to accumulate purines were determined. Kinetic studies showed that the uptake of the nucleoside adenosine by purine-starved organisms was approximately 7-fold faster than by nutrient-replete cells. Further, these studies demonstrated that purine-starved organisms accumulated the nucleobases hypoxanthine and adenine at a rate > 100-fold faster than organisms cultivated under replete conditions. Activities of several intracellular purine-salvage enzymes were measured in organisms from both culture conditions. Of those measured, the activities of adenine deaminase and hypoxanthine phosphoribosyltransferase were elevated approximately 4-fold and approximately 11-fold, respectively, in purine-starved organisms. Competitive substrate specificity studies suggested that these elevated enzyme activities were not responsible for the increased rates of uptake by purine-starved cells. The results are consistent with the induction of novel surface membrane purine transporters expressed in response to purine starvation. These studies using C. luciliae may provide insights into the mechanisms of trypanosomatid adaptation to altered environments encountered during the course of the life cycle.

MeSH Terms
ATP-Binding Cassette Transporters/biosynthesis Adenine/metabolism Adenosine/metabolism Aminohydrolases/biosynthesis Animals Crithidia/metabolism Hypoxanthine Phosphoribosyltransferase/biosynthesis Hypoxanthines/metabolism Kinetics
Chemicals
ATP-Binding Cassette Transporters Hypoxanthines Hypoxanthine Phosphoribosyltransferase Aminohydrolases adenine deaminase Adenine Adenosine
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Alleman M M
Department of Molecular Microbiology and Immunology, Johns Hopkins University School of Hygiene and Public Health, Baltimore, MD 21205, USA.
Gottlieb M
Article Info
Journal
Molecular and biochemical parasitology
Abbr.
Mol Biochem Parasitol
ISSN
0166-6851
Published
1996-00-00
Pages
279-87
Language
English
Region
Netherlands
NLM ID
8006324
Subset
IM
Grants
NIAID NIH HHS · R01 AI16530 · United States
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