Presence of an isoform of H+-pyrophosphatase located in the alveolar sacs of a scuticociliate parasite of turbot: physiological consequences
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 o...
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Cambridge University Press
2016
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ftuglasgow:oai:eprints.gla.ac.uk:149300 2023-05-15T18:41:14+02:00 Presence of an isoform of H+-pyrophosphatase located in the alveolar sacs of a scuticociliate parasite of turbot: physiological consequences Mallo, Natalia Lamas, Jesus Defilipe, Ana-Paula Decastro, Maria-Eugenia Sueiro, Rosa-Ana Leiro, Jose-Manuel 2016-04 http://eprints.gla.ac.uk/149300/ unknown Cambridge University Press Mallo, N. <http://eprints.gla.ac.uk/view/author/36521.html>, Lamas, J., Defilipe, A.-P., Decastro, M.-E., Sueiro, R.-A. and Leiro, J.-M. (2016) Presence of an isoform of H+-pyrophosphatase located in the alveolar sacs of a scuticociliate parasite of turbot: physiological consequences. Parasitology <http://eprints.gla.ac.uk/view/journal_volume/Parasitology.html>, 143(5), pp. 576-587. (doi:10.1017/S0031182015001997 <http://dx.doi.org/10.1017/S0031182015001997>) (PMID:26932195) Articles PeerReviewed 2016 ftuglasgow https://doi.org/10.1017/S0031182015001997 2020-01-10T01:30:01Z 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. Article in Journal/Newspaper Turbot University of Glasgow: Enlighten - Publications Parasitology 143 5 576 587 |
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Open Polar |
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University of Glasgow: Enlighten - Publications |
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ftuglasgow |
language |
unknown |
description |
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. |
format |
Article in Journal/Newspaper |
author |
Mallo, Natalia Lamas, Jesus Defilipe, Ana-Paula Decastro, Maria-Eugenia Sueiro, Rosa-Ana Leiro, Jose-Manuel |
spellingShingle |
Mallo, Natalia Lamas, Jesus Defilipe, Ana-Paula Decastro, Maria-Eugenia Sueiro, Rosa-Ana Leiro, Jose-Manuel Presence of an isoform of H+-pyrophosphatase located in the alveolar sacs of a scuticociliate parasite of turbot: physiological consequences |
author_facet |
Mallo, Natalia Lamas, Jesus Defilipe, Ana-Paula Decastro, Maria-Eugenia Sueiro, Rosa-Ana Leiro, Jose-Manuel |
author_sort |
Mallo, Natalia |
title |
Presence of an isoform of H+-pyrophosphatase located in the alveolar sacs of a scuticociliate parasite of turbot: physiological consequences |
title_short |
Presence of an isoform of H+-pyrophosphatase located in the alveolar sacs of a scuticociliate parasite of turbot: physiological consequences |
title_full |
Presence of an isoform of H+-pyrophosphatase located in the alveolar sacs of a scuticociliate parasite of turbot: physiological consequences |
title_fullStr |
Presence of an isoform of H+-pyrophosphatase located in the alveolar sacs of a scuticociliate parasite of turbot: physiological consequences |
title_full_unstemmed |
Presence of an isoform of H+-pyrophosphatase located in the alveolar sacs of a scuticociliate parasite of turbot: physiological consequences |
title_sort |
presence of an isoform of h+-pyrophosphatase located in the alveolar sacs of a scuticociliate parasite of turbot: physiological consequences |
publisher |
Cambridge University Press |
publishDate |
2016 |
url |
http://eprints.gla.ac.uk/149300/ |
genre |
Turbot |
genre_facet |
Turbot |
op_relation |
Mallo, N. <http://eprints.gla.ac.uk/view/author/36521.html>, Lamas, J., Defilipe, A.-P., Decastro, M.-E., Sueiro, R.-A. and Leiro, J.-M. (2016) Presence of an isoform of H+-pyrophosphatase located in the alveolar sacs of a scuticociliate parasite of turbot: physiological consequences. Parasitology <http://eprints.gla.ac.uk/view/journal_volume/Parasitology.html>, 143(5), pp. 576-587. (doi:10.1017/S0031182015001997 <http://dx.doi.org/10.1017/S0031182015001997>) (PMID:26932195) |
op_doi |
https://doi.org/10.1017/S0031182015001997 |
container_title |
Parasitology |
container_volume |
143 |
container_issue |
5 |
container_start_page |
576 |
op_container_end_page |
587 |
_version_ |
1766230733721960448 |