Active Transport of l-Proline in Trypanosoma cruzi

l-proline is the main energy source in insect vector stages of most trypanosomatids, including Trypanosoma cruzi epimastigotes. This is the first biochemical description of two active proline transporter systems in T. cruzi. Uptake of this amino acid occurred by a low affinity system B and a high af...

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Published inThe Journal of eukaryotic microbiology Vol. 49; no. 6; pp. 441 - 446
Main Authors SILBER, ARIEL M, TONELLI, RENATA R, MARTINELLI, MARCELA, COLLI, WALTER, ALVES, MARIA JÚLIA M
Format Journal Article
LanguageEnglish
Published Oxford, UK Blackwell Publishing Ltd 01.11.2002
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Abstract l-proline is the main energy source in insect vector stages of most trypanosomatids, including Trypanosoma cruzi epimastigotes. This is the first biochemical description of two active proline transporter systems in T. cruzi. Uptake of this amino acid occurred by a low affinity system B and a high affinity system A. System B consistently appeared more specific than System A when excess competing amino acids were used in transport inhibition assays. Furthermore, the high affinity system is 70% inhibited by l-tryptophan, but the low affinity system is not. Both systems were found to be insensitive to the intracellular proline concentration and d-proline did not inhibit l-proline uptake showing that both systems are stereospecific. Both systems were Na+ and K+ independant but dependant on energy since ATP depletion impairs l-proline uptake. The combined action of carbonyl cyanide p-trifluoromethoxyphenyl hydrazone (FCCP) and oligomycin, and the dependence of activity on pH, further differentiated between the two systems leading to the conclusion that the high affinity system is a H+ gradient-dependant transporter whereas the low affinity system depends directly on ATP.
AbstractList L-proline is the main energy source in insect vector stages of most trypanosomatids, including Trypanosoma cruzi epimastigotes. This is the first biochemical description of two active proline transporter systems in T. cruzi. Uptake of this amino acid occurred by a low affinity system B and a high affinity system A. System B consistently appeared more specific than System A when excess competing amino acids were used in transport inhibition assays. Furthermore, the high affinity system is 70% inhibited by L-tryptophan, but the low affinity system is not. Both systems were found to be insensitive to the intracellular proline concentration and D-proline did not inhibit L-proline uptake showing that both systems are stereospecific. Both systems were Na+ and K+ independant but dependant on energy since ATP depletion impairs L-proline uptake. The combined action of carbonyl cyanide p-trifluoromethoxyphenyl hydrazone (FCCP) and oligomycin, and the dependence of activity on pH, further differentiated between the two systems leading to the conclusion that the high affinity system is a H+ gradient-dependant transporter whereas the low affinity system depends directly on ATP.
L‐proline is the main energy source in insect vector stages of most trypanosomatids, including Trypanosoma cruzi epimastigotes. This is the first biochemical description of two active proline transporter systems in T. cruzi . Uptake of this amino acid occurred by a low affinity system B and a high affinity system A. System B consistently appeared more specific than System A when excess competing amino acids were used in transport inhibition assays. Furthermore, the high affinity system is 70% inhibited by L‐tryptophan, but the low affinity system is not. Both systems were found to be insensitive to the intracellular proline concentration and D‐proline did not inhibit L‐proline uptake showing that both systems are stereospecific. Both systems were Na + and K + independant but dependant on energy since ATP depletion impairs L‐proline uptake. The combined action of carbonyl cyanide p‐trifluoromethoxyphenyl hydrazone (FCCP) and oligomycin, and the dependence of activity on pH, further differentiated between the two systems leading to the conclusion that the high affinity system is a H + gradient‐dependant transporter whereas the low affinity system depends directly on ATP.
Author ALVES, MARIA JúLIA M.
TONELLI, RENATA R.
COLLI, WALTER
MARTINELLI, MARCELA
SILBER, ARIEL M.
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Issue 6
Keywords Kinetoplastida
Protozoa
Host parasite relation
Active transport
Protozoal disease
Biological transport
Parasite
Proline
Chagas disease
Parasitosis
proline permease
Trypanosoma cruzi
Infection
proline transporter
L-aminoacid
epimastigotes
Chagas' disease
Differentiation
Trypanosomiasis
parasite differentiation
Language English
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2001; 1505
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1997; 387
1976; 55B
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Snippet l-proline is the main energy source in insect vector stages of most trypanosomatids, including Trypanosoma cruzi epimastigotes. This is the first biochemical...
L‐proline is the main energy source in insect vector stages of most trypanosomatids, including Trypanosoma cruzi epimastigotes. This is the first biochemical...
L-proline is the main energy source in insect vector stages of most trypanosomatids, including Trypanosoma cruzi epimastigotes. This is the first biochemical...
L‐proline is the main energy source in insect vector stages of most trypanosomatids, including Trypanosoma cruzi epimastigotes. This is the first biochemical...
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StartPage 441
SubjectTerms Adenosine Triphosphate - metabolism
Animals
Binding, Competitive
Biological and medical sciences
Biological Transport, Active
Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone - pharmacology
Chagas' disease
epimastigotes
Fundamental and applied biological sciences. Psychology
Hydrogen-Ion Concentration
Kinetics
Life cycle. Host-agent relationship. Pathogenesis
parasite differentiation
Proline - metabolism
proline permease
proline transporter
Protozoa
Thermodynamics
Trypanosoma cruzi - growth & development
Trypanosoma cruzi - metabolism
Title Active Transport of l-Proline in Trypanosoma cruzi
URI http://www.bioone.org/doi/abs/10.1111/j.1550-7408.2002.tb00225.x
https://api.istex.fr/ark:/67375/WNG-9MMDG0L5-2/fulltext.pdf
https://onlinelibrary.wiley.com/doi/abs/10.1111%2Fj.1550-7408.2002.tb00225.x
https://www.ncbi.nlm.nih.gov/pubmed/12503677
https://search.proquest.com/docview/72794431
Volume 49
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