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Cloning and partial characterization of Entamoeba histolytica PTPases.

Abstract：

:Reversible protein tyrosine phosphorylation is an essential signal transduction mechanism that regulates cell growth, differentiation, mobility, metabolism, and survival. Two genes coding for protein tyrosine phophatases, designed EhPTPA and EhPTPB, were cloned from Entamoeba histolytica. EhPTPA and EhPTPB proteins showed amino acid sequence identity of 37%, both EhPTPases showed similarity with Dictyostelium discoideum and vertebrate trasmembranal PTPases. mRNA levels of EhPTPA gene are up-regulated in trophozoites recovered after 96h of liver abscess development in the hamster model. EhPTPA protein expressed as a glutathione S-transferase fusion protein (GST::EhPTPA) showed enzymatic activity with p-nitrophenylphosphate as a substrate and was inhibited by PTPase inhibitors vanadate and molybdate. GST::EhPTPA protein selectively dephosphorylates a 130kDa phosphotyrosine-containing protein in trophozoite cell lysates. EhPTPA gene codifies for a 43kDa native protein. Up-regulation of EhPTPA expression suggests that EhPTPA may play an important role in the adaptive response of trophozoites during amoebic liver abscess development.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Herrera-Rodríguez SE,Baylón-Pacheco L,Talamás-Rohana P,Rosales-Encina JL

doi

10.1016/j.bbrc.2006.02.055

subject

Has Abstract

pub_date

2006-04-21 00:00:00

pages

1014-21

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(06)00350-0

journal_volume

342

pub_type

杂志文章

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