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 journalArticle

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

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Sphingomyelin Phosphodiesterase
Entamoeba histolytica
Esterases
Membranes
Subcellular Fractions
Divalent Cations
Edetic Acid
Virulence
Protein Isoforms
Proteins

All Science Journal Classification (ASJC) codes

  • Parasitology
  • Immunology
  • Infectious Diseases

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., ... 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
Vargas-Villarreal, Javier ; Palacios-Corona, Rebeca ; Hernández-Luna, Carlos ; Mata-Cárdenas, Benito David ; Torres de la Cruz, Victor M. ; Cortés-Gutiérrez, Elva I. ; González-Salazar, Francisco ; Garza-González, Jesús Norberto ; Escobedo-Guajardo, Brenda Leticia ; Said-Fernández, Salvador. / Entamoeba histolytica: Soluble and membrane-associated neutral sphingomyelinase-C and other unidentified esterase activity. In: Experimental Parasitology. 2010 ; pp. 394-399.
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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. {\circledC} 2010 Elsevier Inc.",
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Vargas-Villarreal, J, Palacios-Corona, R, Hernández-Luna, C, Mata-Cárdenas, BD, Torres de la Cruz, VM, Cortés-Gutiérrez, EI, González-Salazar, F, Garza-González, JN, Escobedo-Guajardo, BL & Said-Fernández, S 2010, 'Entamoeba histolytica: Soluble and membrane-associated neutral sphingomyelinase-C and other unidentified esterase activity', Experimental Parasitology, pp. 394-399. https://doi.org/10.1016/j.exppara.2010.03.010

Entamoeba histolytica: Soluble and membrane-associated neutral sphingomyelinase-C and other unidentified esterase activity. / Vargas-Villarreal, Javier; Palacios-Corona, Rebeca; Hernández-Luna, Carlos; Mata-Cárdenas, Benito David; Torres de la Cruz, Victor M.; Cortés-Gutiérrez, Elva I.; González-Salazar, Francisco; Garza-González, Jesús Norberto; Escobedo-Guajardo, Brenda Leticia; Said-Fernández, Salvador.

In: Experimental Parasitology, 01.08.2010, p. 394-399.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Entamoeba histolytica: Soluble and membrane-associated neutral sphingomyelinase-C and other unidentified esterase activity

AU - Vargas-Villarreal, Javier

AU - Palacios-Corona, Rebeca

AU - Hernández-Luna, Carlos

AU - Mata-Cárdenas, Benito David

AU - Torres de la Cruz, Victor M.

AU - Cortés-Gutiérrez, Elva I.

AU - González-Salazar, Francisco

AU - Garza-González, Jesús Norberto

AU - Escobedo-Guajardo, Brenda Leticia

AU - Said-Fernández, Salvador

PY - 2010/8/1

Y1 - 2010/8/1

N2 - 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.

AB - 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.

U2 - 10.1016/j.exppara.2010.03.010

DO - 10.1016/j.exppara.2010.03.010

M3 - Article

SP - 394

EP - 399

JO - Experimental Parasitology

JF - Experimental Parasitology

SN - 0014-4894

ER -

Vargas-Villarreal J, Palacios-Corona R, Hernández-Luna C, Mata-Cárdenas BD, Torres de la Cruz VM, Cortés-Gutiérrez EI et al. Entamoeba histolytica: Soluble and membrane-associated neutral sphingomyelinase-C and other unidentified esterase activity. Experimental Parasitology. 2010 Aug 1;394-399. https://doi.org/10.1016/j.exppara.2010.03.010