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

doi:10.1016/j.exppara.2010.03.010

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 journal › Article › peer-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 language	English
Pages (from-to)	394-399
Number of pages	6
Journal	Experimental Parasitology
Volume	125
Issue number	4
DOIs	https://doi.org/10.1016/j.exppara.2010.03.010
Publication status	Published - 1 Aug 2010
Externally published	Yes

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

UN SDGs

This output contributes to the following Sustainable Development Goal(s)

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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, 125(4), 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 ; Vol. 125, No. 4. pp. 394-399.

@article{81f147eaabd54e11ba2a9d3026f0e4f2,

title = "Entamoeba histolytica: Soluble and membrane-associated neutral sphingomyelinase-C and other unidentified esterase activity",

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.",

author = "Javier Vargas-Villarreal and Rebeca Palacios-Corona and Carlos Hern{\'a}ndez-Luna and Mata-C{\'a}rdenas, {Benito David} and {Torres de la Cruz}, {Victor M.} and Cort{\'e}s-Guti{\'e}rrez, {Elva I.} and Francisco Gonz{\'a}lez-Salazar and Garza-Gonz{\'a}lez, {Jes{\'u}s Norberto} and Escobedo-Guajardo, {Brenda Leticia} and Salvador Said-Fern{\'a}ndez",

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.",

year = "2010",

month = aug,

day = "1",

doi = "10.1016/j.exppara.2010.03.010",

language = "English",

volume = "125",

pages = "394--399",

journal = "Experimental Parasitology",

issn = "0014-4894",

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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, vol. 125, no. 4, 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, Vol. 125, No. 4, 01.08.2010, p. 394-399.

Research output: Contribution to journal › Article › peer-review

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

N1 - 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.

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 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.

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 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.

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M3 - Article

VL - 125

SP - 394

EP - 399

JO - Experimental Parasitology

JF - Experimental Parasitology

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ER -

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

Abstract

Bibliographical note

All Science Journal Classification (ASJC) codes

UN SDGs

Access to Document

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