TY - JOUR
T1 - A putative calcium-ATPase of the secretory pathway family may regulate calcium/manganese levels in the Golgi apparatus of Entamoeba histolytica
AU - Rodríguez, Mario A.
AU - Martínez-Higuera, Aarón
AU - Valle-Solis, Martha I.
AU - Hernandes-Alejandro, Mario
AU - Chávez-Munguía, Bibiana
AU - Figueroa-Gutiérrez, Ana H.
AU - Salas-Casas, Andrés
N1 - Publisher Copyright:
© 2018, Springer-Verlag GmbH Germany, part of Springer Nature.
PY - 2018/11/1
Y1 - 2018/11/1
N2 - 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 Ca2+ 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.
AB - 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 Ca2+ 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.
KW - Calcium-ATPases
KW - Entamoeba histolytica
KW - Golgi apparatus
KW - SPCA
UR - http://www.scopus.com/inward/record.url?scp=85051747038&partnerID=8YFLogxK
U2 - 10.1007/s00436-018-6030-4
DO - 10.1007/s00436-018-6030-4
M3 - Artículo
C2 - 30084034
AN - SCOPUS:85051747038
SN - 0932-0113
VL - 117
SP - 3381
EP - 3389
JO - Parasitology Research
JF - Parasitology Research
IS - 11
ER -
