Entamoeba histolytica: Soluble and membrane-associated neutral sphingomyelinase-C and other unidentified esterase activity

Javier Vargas-Villarreal, Rebeca Palacios-Corona, Carlos Hernández-Luna, Benito David Mata-Cárdenas, Victor M. Torres de la Cruz, Elva I. Cortés-Gutiérrez, Francisco González-Salazar, Jesús Norberto Garza-González, Brenda Leticia Escobedo-Guajardo, Salvador Said-Fernández

Research output: Contribution to journalArticlepeer-review

3 Citations (Scopus)

Abstract

Sphingomyelinase (SMase) activity was measured in Entamoeba histolytica particulate and soluble subcellular fractions. The effects on SMase of incubation time, total protein concentration, pH, and several divalent cations were determined. SMase-C and other unidentified esterase activity were detected in soluble and particulate fractions. SMase-C was 94.5-96.0% higher than the unidentified esterase activity. Soluble and insoluble SMase-C specific activities increased with protein dose and incubation time. Soluble and insoluble SMase-C activities were maximum at pH 7.5 and were dependent on Mg 2+, Mn 2+, or Co 2+, and inhibited by Zn 2+, Hg 2+, Ca 2+, and EDTA. SMase-C was active in the pH range of 3-10 and its maximum activity was at pH 7.5. The soluble and insoluble SMases have remarkably similar physicochemical properties, strongly suggesting that E. histolytica has just one isoform of neutral SMase-C that had not been described before and might be essential for E. histolytica metabolism or virulence.

Original languageEnglish
Pages (from-to)394-399
Number of pages6
JournalExperimental Parasitology
Volume125
Issue number4
DOIs
Publication statusPublished - 1 Aug 2010
Externally publishedYes

Bibliographical note

Funding Information:
The authors thank Antonio Luna de la Rosa for the artwork. This study was supported by FIS/IMSS/PROT/509 and CONACyT/80049/FIS/IMSS/PROT/600.

Copyright:
Copyright 2010 Elsevier B.V., All rights reserved.

All Science Journal Classification (ASJC) codes

  • Parasitology
  • Immunology
  • Infectious Diseases

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