Entamoeba histolytica: an ecto-phosphatase activity regulated by oxidation-reduction reactions.

Abstract:

:In this work, an ecto-phosphatase activity of Entamoeba histolytica was characterized using intact cells. This activity presented the following biochemical characteristics: (i) it hydrolyzes p-NPP with V(max) of 8.00+/-0.22 nmol p-NP x h(-1) x 10(-5) cells and K(m) of 2.68+/-0.25 mM; (ii) it is inhibited by acid phosphatase inhibitors, such as sodium molybdate (K(i)=1.70+/-0.24 microM) and sodium fluoride (K(i)=0.25+/-0.02 mM); (iii) it also showed high sensitivity to phosphotyrosine phosphatase inhibitors, such as sodium orthovanadate (K(i)=1.07+/-0.14 microM), bpV-PHEN (K(i)=0.38+/-0.02 microM) and mpV-PIC (K(i)=0.39+/-0.04 microM). Zn(2+), an oxidizing agent, decreased the enzymatic activity in 50%. DTT and GSH, two reducing agents, enhanced the activity twofold. The non-invasive E. histolytica and free-living E. moshkovskii were less efficient in hydrolyzing p-NPP than the pathogenic E. histolytica suggesting that this enzyme could represent a virulence marker for this cell.

journal_name

Exp Parasitol

authors

de Sá Pinheiro AA,Amazonas JN,de Souza Barros F,De Menezes LF,Batista EJ,Silva EF,De Souza W,Meyer-Fernandes JR

doi

10.1016/j.exppara.2006.09.019

subject

Has Abstract

pub_date

2007-04-01 00:00:00

pages

352-8

issue

4

eissn

0014-4894

issn

1090-2449

pii

S0014-4894(06)00238-4

journal_volume

115

pub_type

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