| Autor: |
Rodríguez MA; Departamento de Infectómica y Patogénesis Molecular, Centro de Investigación y de Estudios Avanzados del IPN, Mexico City, Mexico., Martínez-Higuera A; Departamento de Física, Universidad de Sonora, Hermosillo, Sonora, Mexico., Valle-Solis MI; Departamento de Infectómica y Patogénesis Molecular, Centro de Investigación y de Estudios Avanzados del IPN, Mexico City, Mexico., Hernandes-Alejandro M; Departamento de Bioingeniería, Unidad Profesional Interdisciplinaria de Biotecnología del Instituto Politécnico Nacional (UPIBI-IPN), Mexico City, Mexico., Chávez-Munguía B; Departamento de Infectómica y Patogénesis Molecular, Centro de Investigación y de Estudios Avanzados del IPN, Mexico City, Mexico., Figueroa-Gutiérrez AH; Instituto de Ciencias de la Salud, Área Académica de Gerontología, Universidad Autónoma del Estado de Hidalgo, Ex Hacienda la Concepción, s/n; Carretera Actopan-Tilcuautla, San Agustín Tlaxiaca, Hidalgo, Mexico., Salas-Casas A; Instituto de Ciencias de la Salud, Área Académica de Gerontología, Universidad Autónoma del Estado de Hidalgo, Ex Hacienda la Concepción, s/n; Carretera Actopan-Tilcuautla, San Agustín Tlaxiaca, Hidalgo, Mexico. andres_salas15@yahoo.com.mx. |
| Abstrakt: |
Calcium regulates many cellular processes in protozoa, including growth, differentiation, programmed cell death, exocytosis, endocytosis, phagocytosis, fusion of the endosomes of distinct stages with phagosomes, fusion of phagosomes with lysosomes, and recycling the membrane. In Entamoeba histolytica, the protozoa responsible for human amoebiasis, calcium ions are essential for signaling pathways that lead to growth and development. In addition, calcium is crucial in the modulation of gene expression in this microorganism. However, there is scant information about the proteins responsible for regulating calcium levels in this parasite. In this work, we characterized a protein of E. histolytica that shows a close phylogenetic relationship with Ca 2+ pumps that belong to the family of secretory pathway calcium ATPases (SPCA), which for several organisms are located in the Golgi apparatus. The amoeba protein analyzed herein has several amino acid residues that are characteristic of SPCA members. By an immunofluorescent technique using specific antibodies and immunoelectron microscopy, the protein was detected on the membrane of some cytoplasmic vacuoles. Moreover, this putative calcium-ATPase was located in vacuoles stained with NBD C6-ceramide, a Golgi marker. Overall, the current findings support the hypothesis that the presently analyzed protein corresponds to the SPCA of E. histolytica. |
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