Presence of an isoform of H+-pyrophosphatase located in the alveolar sacs of a scuticociliate parasite of turbot: physiological consequences
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Title: | Presence of an isoform of H+-pyrophosphatase located in the alveolar sacs of a scuticociliate parasite of turbot: physiological consequences |
Author: | Mallo Seijas, Natalia Lamas Fernández, Jesús Felipe González, Ana Paula de Castro de Antonio, María Eugenia de Sueiro Benavides, Rosa Ana Leiro Vidal, José Manuel |
Affiliation: | Universidade de Santiago de Compostela. Departamento de Bioloxía Funcional Universidade de Santiago de Compostela. Departamento de Microbioloxía e Parasitoloxía Universidade de Santiago de Compostela. Instituto de Acuicultura Universidade de Santiago de Compostela. Instituto de Investigación e Análises Alimentarias |
Subject: | H+-PPase | Philasterides dicentrarchi | Alveolar sacs | Osmoregulation | |
Date of Issue: | 2016-04 |
Publisher: | Cambridge University Press |
Citation: | Mallo N, Lamas J, Defelipe AP, Decastro ME, Sueiro RA, Leiro JM. (2016).Presence of an isoform of H+-pyrophosphatase located in the alveolar sacs of a scuticociliate parasite of turbot: physiological consequences. Parasitology143: 576-87. doi: 10.1017/S0031182015001997 |
Abstract: | H+-pyrophosphatases (H+-PPases) are integral membrane proteins that couple pyrophosphate energy to an electrochemical gradient across biological membranes and promote the acidification of cellular compartments. Eukaryotic organisms, essentially plants and protozoan parasites, contain various types of H+-PPases associated with vacuoles, plasma membrane and acidic Ca+2 storage organelles called acidocalcisomes. We used Lysotracker Red DND-99 staining to identify two acidic cellular compartments in trophozoites of the marine scuticociliate parasite Philasterides dicentrarchi: the phagocytic vacuoles and the alveolar sacs. The membranes of these compartments also contain H+-PPase, which may promote acidification of these cell structures. We also demonstrated for the first time that the P. dicentrarchi H+-PPase has two isoforms: H+-PPase 1 and 2. Isoform 2, which is probably generated by splicing, is located in the membranes of the alveolar sacs and has an amino acid motif recognized by the H+-PPase-specific antibody PABHK. The amino acid sequences of different isolates of this ciliate are highly conserved. Gene and protein expression in this isoform are significantly regulated by variations in salinity, indicating a possible physiological role of this enzyme and the alveolar sacs in osmoregulation and salt tolerance in P. dicentrarchi |
Description: | This article has been published in a revised form in Parasitology
[http://doi.org/10.1017/ S0031182015001997]. This version is free to view
and download for private research and study only. Not for re-distribution,
re-sale or use in derivative works. © 2017 Cambridge University Press |
Publisher version: | https://doi.org/10.1017/S0031182015001997 |
URI: | http://hdl.handle.net/10347/18171 |
DOI: | 10.1017/S0031182015001997 |
ISSN: | 0031-1820 |
E-ISSN: | 1469-8161 |
Rights: | © 2017 Cambridge University Press. This version is free to view and download for private research and study only. Not for re-distribution, re-sale or use in derivative works |
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