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BioMed Research International
Volume 2013, Article ID 679365, 8 pages
Research Article

Sphingomyelinase Activity of Trichomonas vaginalis Extract and Subfractions

1División de Biología Celular y Molecular, Centro de Investigación Biomédica del Noreste, Instituto Mexicano del Seguro Social, Administración de Correo No. 4, 2 de abril 501 Colonia Independencia, 64720 Monterrey, NL, Mexico
2Departamento de Ciencias Básicas, División de Ciencias de la Salud, Universidad de Monterrey, Avenida Morones Prieto 4500 Pte, 66238 San Pedro Garza García, NL, Mexico
3Departamento de Biología Celular y Genética, Facultad de Ciencias Biológicas, Universidad Autónoma de Nuevo León, 66451 San Nicolás de los Garza, NL, Mexico
4Laboratorio de Enzimología, Facultad de Ciencias Biológicas, UANL, San Nicolás de los Garza, NL, Mexico
5Facultad de Ciencias Químicas, Universidad Autónoma de Nuevo León, Avenida Manuel L Barragán S/N, San Nicolás de los Garza, NL, Mexico

Received 29 April 2013; Accepted 10 July 2013

Academic Editor: Rana Chattopadhyay

Copyright © 2013 Francisco González-Salazar et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Trichomoniasis is one of the most common acute sexually transmitted curable diseases, and it is disseminated worldwide generating more than 170 million cases annually. Trichomonas vaginalis is the parasite that causes trichomoniasis and has the ability to destroy cell monolayers of the vaginal mucosa in vitro. Sphingomyelinases (SMase) are enzymes that catalyze the hydrolysis of sphingomyelin into ceramide and phosphorylcholine. Ceramide appears to be a second messenger lipid in programmed apoptosis, cell differentiation, and cell proliferation. Sphingomyelinase is probably a major source of ceramide in cells. Signal transduction mediated by ceramide leads cells to produce cytokine induced apoptosis during several inflammatory responses. SMase are also relevant toxins in several microorganisms. The main objective of this research is to identify SMase activity of T. vaginalis in the total extract (TE), P30, and S30 subfractions from brooked trophozoites. It was found that these fractions of T. vaginalis have SMase activity, which comes principally from P30 subfraction and was mainly type C. Enzymatic activity of SMase increased linearly with time and is pH dependent with two peaks by pH 5.5 and pH 7.5. The addition of manganese to the reaction mixture increased the SMase activity by 1.97.