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

All Science Journal Classification (ASJC) codes

Parasitology
Immunology
Infectious Diseases

Access to Document

10.1016/j.exppara.2010.03.010

https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=77953023899&origin=inward

Fingerprint Dive into the research topics of 'Entamoeba histolytica: Soluble and membrane-associated neutral sphingomyelinase-C and other unidentified esterase activity'. Together they form a unique fingerprint.

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

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.

@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 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. {\textcopyright} 2010 Elsevier Inc.",

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",

year = "2010",

month = aug,

day = "1",

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

language = "English",

pages = "394--399",

journal = "Experimental Parasitology",

issn = "0014-4894",

publisher = "Academic Press Inc.",

}

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 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

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 -