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

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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 Mg2+, Mn2+, or Co2+, and inhibited by Zn2+, Hg2+, Ca2+, 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. © 2010 Elsevier Inc.
Original languageEnglish
Pages (from-to)394-399
Number of pages6
JournalExperimental Parasitology
DOIs
Publication statusPublished - 1 Aug 2010
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Parasitology
  • Immunology
  • Infectious Diseases

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  • Cite this

    Vargas-Villarreal, J., Palacios-Corona, R., Hernández-Luna, C., Mata-Cárdenas, B. D., Torres de la Cruz, V. M., Cortés-Gutiérrez, E. I., González-Salazar, F., Garza-González, J. N., Escobedo-Guajardo, B. L., & Said-Fernández, S. (2010). Entamoeba histolytica: Soluble and membrane-associated neutral sphingomyelinase-C and other unidentified esterase activity. Experimental Parasitology, 394-399. https://doi.org/10.1016/j.exppara.2010.03.010