Entamoeba histolytica:: ADP-ribosylation of secreted glyceraldehyde-3-phosphate dehydrogenase

被引：16

作者：

Alvarez, A. H.

Martinez-Cadena, G.

Silva, M. E.

Saavedra, E.

Avila, E. E. ^{[1
]}

机构：

[1] Univ Guanajuato, Fac Quim, IIBE, Guanajuato, Mexico

[2] Inst Nacl Cardiol, Dept Bioquim, Mexico City, DF, Mexico

来源：

EXPERIMENTAL PARASITOLOGY | 2007年 / 117卷 / 04期

关键词：

ameba; cysteine synthase A; extracellular GAPDH; glyceraldehyde-3-phosphate dehydrogenase phosphorylating; (EC 1.2.1.12); human parasite; mono-ADP-ribosylation; protozoa; NAD(+); DTT; dithiothreitol; E-64; trans-Epoxysuccinyl-L-leucylamido(4-guanidino)-butane; GAPDH; glyceraldehyde-3-phosphate dehydrogenase (phosphorylating); EhGAPDH; GAPDH from Entamoeba histolytica; MALDI-TOF; matrix-assisted laser desorption/ionization time-of-flight mass spectrometry; nicotinamide adenine dinucleotide; pI; isoelectric point; SDS; sodium dodecyl sulfate; SD; standard deviation; TYI-S-33; complete culture medium for Entamoeba; TYI; medium without serum and vitamins;

D O I：

10.1016/j.exppara.2007.04.016

中图分类号：

R38 [医学寄生虫学]; Q [生物科学];

学科分类号：

07 ; 0710 ; 09 ; 100103 ;

摘要：

In addition to its classic glycolytic role, glyceraldehyde-3-phosphate dehydrogenase (GAPDH) has been implicated in many activities unrelated to glycolysis, such as membrane fusion, binding to host proteins and signal transduction. GAPDH can be the target of several modifications that allow incorporation to membranes and possible regulation of its activity; among these modifications is mono-ADP-ribosylation. This post-translational modification is important for the regulation of many cellular processes and is the mechanism of action of several bacterial toxins. In a previous study, we observed the extracellular ADP-ribosylation of a 37-kDa ameba protein. We report here that GAPDH and cysteine synthase A are the main ADP-ribosylated proteins in Entamoeba histolytica extracellular medium, GAPDH is secreted from ameba at 37 degrees C in a time-dependent manner, and its enzymatic activity is not inhibited by ADP-ribosylation. Extracellular GAPDH from ameba may play an important role in the survival of this human pathogen or in interaction with host molecules, as occurs in other organisms. (C) 2007 Elsevier Inc. All rights reserved.

引用

页码：349 / 356

页数：8

共 41 条

[1] PLASMA-MEMBRANE OF ENTAMOEBA-HISTOLYTICA [J].