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.
UR - http://www.scopus.com/inward/record.url?scp=77953023899&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=77953023899&partnerID=8YFLogxK
UR - https://www.mendeley.com/catalogue/80710c55-9807-3228-96c0-82b2a1e95382/
U2 - 10.1016/j.exppara.2010.03.010
DO - 10.1016/j.exppara.2010.03.010
M3 - Article
VL - 125
SP - 394
EP - 399
JO - Experimental Parasitology
JF - Experimental Parasitology
SN - 0014-4894
IS - 4
ER -
