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Journal of Biomedicine and Biotechnology
Volume 2010 (2010), Article ID 747121, 11 pages
http://dx.doi.org/10.1155/2010/747121
Research Article

A New MAP Kinase Protein Involved in Estradiol-Stimulated Reproduction of the Helminth Parasite Taenia crassiceps

1Departamento de Medicina Experimental, Facultad de Medicina, UNAM, Hospital General de México, México D.F. 06726, Mexico
2Departamento de Biología, Facultad de Química, UNAM, AP 70228, México D.F. 04510, Mexico
3Departamento de Inmunología, Instituto de Investigaciones Biomédicas, UNAM., AP 70228, México D.F. 04510, Mexico
4Departamento de Genética y Biología Molecular, Cinvestav, IPN, Av. Instituto Politécnico Nacional 2508 Col. San Pedro Zacatenco, México D.F. 07360, Mexico
5Subdirección de Investigación Clínica, Instituto Nacional de Perinatología, México D.F. 11000, Mexico
6Facultad de Farmacia, Universidad Autónoma del Estado de Morelos, Morelos 62209, Mexico

Received 30 July 2009; Accepted 12 October 2009

Academic Editor: Luis I. Terrazas

Copyright © 2010 Galileo Escobedo 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.

Abstract

MAP kinases (MAPK) are involved in the regulation of cellular processes such as reproduction and growth. In parasites, the role of MAPK has been scarcely studied. Here, we describe the participation of an ERK-like protein in estrogen-dependent reproduction of the helminth parasite Taenia crassiceps. Our results show that 17β-estradiol induces a concentration-dependent increase in the bud number of in vitro cultured cysticerci. If parasites are also incubated in presence of an ERK-inhibitor, the stimulatory effect of estrogen is blocked. The expression of ERK-like mRNA and its corresponding protein was detected in the parasite. The ERK-like protein was over-expressed by all treatments. Nevertheless, a strong induction of phosphorylation of this protein was observed only in response to 17β-estradiol. Cross-contamination by host cells was discarded by flow cytometry analysis. Parasite cells expressing the ERK-like protein were exclusively located at the subtegument tissue by confocal microscopy. Finally, the ERK-like protein was separated by bidimensional electrophoresis and then sequenced, showing the conserved TEY activation motif, typical of all known ERK 1/2 proteins. Our results show that an ERK-like protein is involved in the molecular signalling during the interaction between the host and T. crassiceps, and may be considered as target for anti-helminth drugs design.