Platelet-activating factor modulates a secreted phosphatase activity of the trypanosomatid parasite Herpetomonas muscarum muscarum

In the present work we characterized the secreted phosphatase activity of the trypanosomatid parasite Herpetomonas muscarum muscarum. This housefly parasite hydrolyzed p-nitrophenylphosphate at a rate of 10.26 nmol Pi/mg protein/min. Classical inhibitors of acid phosphatases, such as sodium orthovan...

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Bibliographic Details
Published in:Current microbiology 2001-10, Vol.43 (4), p.288-292
Main Authors: DUTRA, Patricia M. L, DIAS, Felipe A, RODRIGUES, Claudia O, ROMEIRO, Alexandre, ATTIAS, Marcia, DE SOUZA, Wanderley, LOPES, Angela H. C. S, MEYER-FERNANDES, José Roberto
Format: Article
Language:English
Subjects:
Acid phosphatase
Acid Phosphatase - drug effects
Acid Phosphatase - secretion
Ammonium
ammonium molybdate(VI)
Animals
Biological and medical sciences
Culture Media
Fundamental and applied biological sciences. Psychology
Herpetomonas muscarum muscarum
Houseflies - parasitology
Insecta
Invertebrates
Kinases
Parasites
Pathology
Platelet Activating Factor - pharmacology
platelet-activating factor
Sodium
sodium fluoride
sodium orthovanadate
sodium tartrate
Trypanosomatina - enzymology
Trypanosomatina - growth & development
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Summary:In the present work we characterized the secreted phosphatase activity of the trypanosomatid parasite Herpetomonas muscarum muscarum. This housefly parasite hydrolyzed p-nitrophenylphosphate at a rate of 10.26 nmol Pi/mg protein/min. Classical inhibitors of acid phosphatases, such as sodium orthovanadate (NaVO3), sodium fluoride (NaF), and ammonium molybdate promoted a decrease in this phosphatase activity. When the parasites were assayed in the presence of sodium tartrate, an inhibitor of Leishmania spp-secreted acid phosphatases, this activity was drastically diminished. Cytochemical analysis showed the localization of this enzyme on the external surface and in the flagellar pocket of these parasites. Sodium tartrate inhibited this reaction, confirming the biochemical data. Platelet-activating factor (PAF) inhibited the phosphatase activity determined in the supernatant of living H. m. muscarum.
ISSN:0343-8651
1432-0991
DOI:10.1007/s002840010303