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Immunocytochemical localization of V-H+-ATPase, Na+/K+-ATPase, and carbonic anhydrase in gill lamellae of adult freshwater euryhaline shrimp Macrobrachium acanthurus (Decapoda, Palaemonidae)

ABSTRACT Physiological (organismal), biochemical, and molecular biological contributions to the knowledge of the osmoregulatory plasticity of palaemonid freshwater shrimps has provided a fairly complete model of transporter localization in their branchial epithelium. Direct immunological demonstrati...

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Published in:Journal of experimental zoology. Part A, Ecological and integrative physiology Ecological and integrative physiology, 2015-08, Vol.323 (7), p.414-421
Main Authors: Maraschi, Anieli Cristina, Freire, Carolina Arruda, Prodocimo, Viviane
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cited_by cdi_FETCH-LOGICAL-c3874-596c39a6a81c8975ec9655d7a759bac82bda115f03e875b2cf34966876650d2d3
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Prodocimo, Viviane
description ABSTRACT Physiological (organismal), biochemical, and molecular biological contributions to the knowledge of the osmoregulatory plasticity of palaemonid freshwater shrimps has provided a fairly complete model of transporter localization in their branchial epithelium. Direct immunological demonstration of the main enzymes in the gill epithelia of adult palaemonids is, however, still incipient. The diadromous freshwater shrimp Macrobrachium acanthurus was exposed to increased salinity (25‰ for 24 hr), and its responses at the systemic level were evaluated through the assays of hemolymph osmolality and muscle hydration, and at cellular and subcellular levels through the activity and localization of the V‐H+‐ATPase, the Na+/K+‐ATPase, and the carbonic anhydrase. Results showed an increase in hemolymph osmolality (629 ± 5.3 mOsm/kg H2O) and a decrease in muscle hydration (73.8 ± 0.5%), comparing values after 24 hr in 25‰ with control shrimps in freshwater (respectively 409.5 ± 15.8 mOsm/kg H2O and 77.5 ± 0.4%). V‐H+‐ATPase was localized in pillar cells, whereas Na+/K+‐ATPase in the septal cells. The main novelty of this study was that carbonic anhydrase was localized in the whole branchial tissue, in pillar and septal cells. Exposure to high salinity for 24 hr led to no detectable changes in their localization or in vitro activity. Immunolocalization data corroborated the literature and current models of palaemonid gill ion transport. The absence of changes reinforces the need for the constant expression of these enzymes to account for the euryhalinity of these shrimps. J. Exp. Zool. 323A: 414–421, 2015. © 2015 Wiley Periodicals, Inc.
doi_str_mv 10.1002/jez.1934
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Results showed an increase in hemolymph osmolality (629 ± 5.3 mOsm/kg H2O) and a decrease in muscle hydration (73.8 ± 0.5%), comparing values after 24 hr in 25‰ with control shrimps in freshwater (respectively 409.5 ± 15.8 mOsm/kg H2O and 77.5 ± 0.4%). V‐H+‐ATPase was localized in pillar cells, whereas Na+/K+‐ATPase in the septal cells. The main novelty of this study was that carbonic anhydrase was localized in the whole branchial tissue, in pillar and septal cells. Exposure to high salinity for 24 hr led to no detectable changes in their localization or in vitro activity. Immunolocalization data corroborated the literature and current models of palaemonid gill ion transport. The absence of changes reinforces the need for the constant expression of these enzymes to account for the euryhalinity of these shrimps. J. Exp. 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The diadromous freshwater shrimp Macrobrachium acanthurus was exposed to increased salinity (25‰ for 24 hr), and its responses at the systemic level were evaluated through the assays of hemolymph osmolality and muscle hydration, and at cellular and subcellular levels through the activity and localization of the V‐H+‐ATPase, the Na+/K+‐ATPase, and the carbonic anhydrase. Results showed an increase in hemolymph osmolality (629 ± 5.3 mOsm/kg H2O) and a decrease in muscle hydration (73.8 ± 0.5%), comparing values after 24 hr in 25‰ with control shrimps in freshwater (respectively 409.5 ± 15.8 mOsm/kg H2O and 77.5 ± 0.4%). V‐H+‐ATPase was localized in pillar cells, whereas Na+/K+‐ATPase in the septal cells. The main novelty of this study was that carbonic anhydrase was localized in the whole branchial tissue, in pillar and septal cells. Exposure to high salinity for 24 hr led to no detectable changes in their localization or in vitro activity. Immunolocalization data corroborated the literature and current models of palaemonid gill ion transport. The absence of changes reinforces the need for the constant expression of these enzymes to account for the euryhalinity of these shrimps. J. Exp. Zool. 323A: 414–421, 2015. © 2015 Wiley Periodicals, Inc.</abstract><cop>United States</cop><pub>Blackwell Publishing Ltd</pub><pmid>26036663</pmid><doi>10.1002/jez.1934</doi><tpages>8</tpages></addata></record>
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ispartof Journal of experimental zoology. Part A, Ecological and integrative physiology, 2015-08, Vol.323 (7), p.414-421
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subjects Adaptation, Physiological
Animals
Carbonic Anhydrases - metabolism
Epithelium - metabolism
Gills - metabolism
Hemolymph - chemistry
Ion Transport
Osmolar Concentration
Palaemonidae - metabolism
Salinity
Sodium-Potassium-Exchanging ATPase - metabolism
Vacuolar Proton-Translocating ATPases - metabolism
title Immunocytochemical localization of V-H+-ATPase, Na+/K+-ATPase, and carbonic anhydrase in gill lamellae of adult freshwater euryhaline shrimp Macrobrachium acanthurus (Decapoda, Palaemonidae)
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