Escobedo Galileo, Soldevila Gloria, Ortega-Pierres Guadalupe, Chávez-Ríos Jesús Ramsés, Nava Karen, Fonseca-Liñán Rocío, López-Griego Lorena, Hallal-Calleros Claudia, Ostoa-Saloma Pedro, Morales-Montor Jorge
Departamento de Medicina Experimental, Facultad de Medicina, UNAM, Hospital General de México, México D.F. 06726, Mexico.
J Biomed Biotechnol. 2010;2010:747121. doi: 10.1155/2010/747121. Epub 2010 Jan 21.
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 17beta-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 17beta-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.
丝裂原活化蛋白激酶(MAPK)参与细胞过程的调控,如繁殖和生长。在寄生虫中,MAPK的作用鲜有研究。在此,我们描述了一种类细胞外信号调节激酶(ERK)蛋白在蠕虫寄生虫克氏绦虫雌激素依赖性繁殖中的作用。我们的结果表明,17β-雌二醇可诱导体外培养的囊尾蚴芽体数量呈浓度依赖性增加。如果寄生虫同时在ERK抑制剂存在的情况下孵育,雌激素的刺激作用会被阻断。在寄生虫中检测到了类ERK mRNA及其相应蛋白的表达。所有处理均使类ERK蛋白过度表达。然而,仅在对17β-雌二醇的反应中观察到该蛋白磷酸化的强烈诱导。通过流式细胞术分析排除了宿主细胞的交叉污染。通过共聚焦显微镜观察,表达类ERK蛋白的寄生虫细胞仅位于皮层下组织。最后,通过二维电泳分离类ERK蛋白,然后进行测序,显示出所有已知ERK 1/2蛋白典型的保守TEY激活基序。我们的结果表明,一种类ERK蛋白参与宿主与克氏绦虫相互作用过程中的分子信号传导,并且可被视为抗蠕虫药物设计的靶点。