Presence of an isoform of H + -pyrophosphatase located in the alveolar sacs of a scuticociliate parasite of turbot: physiological consequences
SUMMARY 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 var...
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Cambridge University Press (CUP)
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crcambridgeupr:10.1017/s0031182015001997 2024-03-03T08:49:16+00:00 Presence of an isoform of H + -pyrophosphatase located in the alveolar sacs of a scuticociliate parasite of turbot: physiological consequences MALLO, NATALIA LAMAS, JESÚS DEFELIPE, ANA-PAULA DECASTRO, MARIA-EUGENIA SUEIRO, ROSA-ANA LEIRO, JOSÉ-MANUEL 2016 http://dx.doi.org/10.1017/s0031182015001997 https://www.cambridge.org/core/services/aop-cambridge-core/content/view/S0031182015001997 en eng Cambridge University Press (CUP) https://www.cambridge.org/core/terms Parasitology volume 143, issue 5, page 576-587 ISSN 0031-1820 1469-8161 Infectious Diseases Animal Science and Zoology Parasitology journal-article 2016 crcambridgeupr https://doi.org/10.1017/s0031182015001997 2024-02-08T08:29:31Z SUMMARY 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 PAB HK . 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 Cambridge University Press Parasitology 143 5 576 587 |
institution |
Open Polar |
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Cambridge University Press |
op_collection_id |
crcambridgeupr |
language |
English |
topic |
Infectious Diseases Animal Science and Zoology Parasitology |
spellingShingle |
Infectious Diseases Animal Science and Zoology Parasitology MALLO, NATALIA LAMAS, JESÚS DEFELIPE, ANA-PAULA DECASTRO, MARIA-EUGENIA SUEIRO, ROSA-ANA LEIRO, JOSÉ-MANUEL Presence of an isoform of H + -pyrophosphatase located in the alveolar sacs of a scuticociliate parasite of turbot: physiological consequences |
topic_facet |
Infectious Diseases Animal Science and Zoology Parasitology |
description |
SUMMARY 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 PAB HK . 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, JESÚS DEFELIPE, ANA-PAULA DECASTRO, MARIA-EUGENIA SUEIRO, ROSA-ANA LEIRO, JOSÉ-MANUEL |
author_facet |
MALLO, NATALIA LAMAS, JESÚS DEFELIPE, ANA-PAULA DECASTRO, MARIA-EUGENIA SUEIRO, ROSA-ANA LEIRO, JOSÉ-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 (CUP) |
publishDate |
2016 |
url |
http://dx.doi.org/10.1017/s0031182015001997 https://www.cambridge.org/core/services/aop-cambridge-core/content/view/S0031182015001997 |
genre |
Turbot |
genre_facet |
Turbot |
op_source |
Parasitology volume 143, issue 5, page 576-587 ISSN 0031-1820 1469-8161 |
op_rights |
https://www.cambridge.org/core/terms |
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 |
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1792506453094825984 |