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Multiplicity of expression of Na+,K+-ATPase {alpha}-subunit isoforms in the gill of Atlantic salmon (Salmo salar): cellular localisation and absolute quantification in response to salinity change.
J Exp Biol. 2009 Jan; 212(Pt 1):78-88.JE

Abstract

The ability to reverse the net direction of gill ion transport in response to a salinity change is critical for euryhaline teleosts and involves a complex cellular and molecular remodelling of the gill epithelium. The present study aimed to clarify the cellular localisation and exact quantitative inter-relationship of Na(+),K(+)-ATPase alpha- and beta-subunit transcripts in Atlantic salmon gill during salinity change. The combined expression level of all alpha-isoforms in the gill increased by 100% after freshwater (FW) to seawater (SW) transfer. The alpha(1a) and alpha(1b) isoforms were both in the range 1-6 amol 20 ng(-1) total RNA; alpha(1a) decreased and alpha(1b) increased after SW-transfer, their ratio changing from 5:1 in FW to 0.26:1 in SW. The alpha(1c) and alpha(3) levels were 10- and 100-fold lower, respectively. The beta(1)-subunit mRNA level was 0.1-0.3 amol 20 ng(-1) total RNA, thus much lower than the sum of alpha-subunits. Even though increasing 3-fold after SW-transfer, beta-subunit availability may still limit functional pump synthesis. The mRNAs of the predominant alpha(1a) and alpha(1b) isoforms were localised by in situ hybridisation in specific gill cells of both FW and SW salmon. Labelling occurred mainly in presumed chloride cells and cells deep in the filament but occasionally also on lamellae. Overall, the salinity-induced variation in labelling pattern and intensity matched the quantification data. In conclusion, the predominant switching of Na(+),K(+)-ATPase alpha-subunit isoform mRNA during salinity acclimation reflects a marked remodelling of mitochondrion-rich cells (MRCs) in the gill and probably tuning of the pump performance to accomplish a net reversal of gill ion transport in hypo- and hypertonic environments.

Authors+Show Affiliations

Institute of Biology, University of Southern Denmark, 5230 Odense M, Denmark. steffen@biology.sdu.dkNo affiliation info availableNo affiliation info available

Pub Type(s)

Comparative Study
Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

19088213

Citation

Madsen, Steffen S., et al. "Multiplicity of Expression of Na+,K+-ATPase {alpha}-subunit Isoforms in the Gill of Atlantic Salmon (Salmo Salar): Cellular Localisation and Absolute Quantification in Response to Salinity Change." The Journal of Experimental Biology, vol. 212, no. Pt 1, 2009, pp. 78-88.
Madsen SS, Kiilerich P, Tipsmark CK. Multiplicity of expression of Na+,K+-ATPase {alpha}-subunit isoforms in the gill of Atlantic salmon (Salmo salar): cellular localisation and absolute quantification in response to salinity change. J Exp Biol. 2009;212(Pt 1):78-88.
Madsen, S. S., Kiilerich, P., & Tipsmark, C. K. (2009). Multiplicity of expression of Na+,K+-ATPase {alpha}-subunit isoforms in the gill of Atlantic salmon (Salmo salar): cellular localisation and absolute quantification in response to salinity change. The Journal of Experimental Biology, 212(Pt 1), 78-88. https://doi.org/10.1242/jeb.024612
Madsen SS, Kiilerich P, Tipsmark CK. Multiplicity of Expression of Na+,K+-ATPase {alpha}-subunit Isoforms in the Gill of Atlantic Salmon (Salmo Salar): Cellular Localisation and Absolute Quantification in Response to Salinity Change. J Exp Biol. 2009;212(Pt 1):78-88. PubMed PMID: 19088213.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Multiplicity of expression of Na+,K+-ATPase {alpha}-subunit isoforms in the gill of Atlantic salmon (Salmo salar): cellular localisation and absolute quantification in response to salinity change. AU - Madsen,Steffen S, AU - Kiilerich,Pia, AU - Tipsmark,Christian K, PY - 2008/12/18/entrez PY - 2008/12/18/pubmed PY - 2009/3/27/medline SP - 78 EP - 88 JF - The Journal of experimental biology JO - J. Exp. Biol. VL - 212 IS - Pt 1 N2 - The ability to reverse the net direction of gill ion transport in response to a salinity change is critical for euryhaline teleosts and involves a complex cellular and molecular remodelling of the gill epithelium. The present study aimed to clarify the cellular localisation and exact quantitative inter-relationship of Na(+),K(+)-ATPase alpha- and beta-subunit transcripts in Atlantic salmon gill during salinity change. The combined expression level of all alpha-isoforms in the gill increased by 100% after freshwater (FW) to seawater (SW) transfer. The alpha(1a) and alpha(1b) isoforms were both in the range 1-6 amol 20 ng(-1) total RNA; alpha(1a) decreased and alpha(1b) increased after SW-transfer, their ratio changing from 5:1 in FW to 0.26:1 in SW. The alpha(1c) and alpha(3) levels were 10- and 100-fold lower, respectively. The beta(1)-subunit mRNA level was 0.1-0.3 amol 20 ng(-1) total RNA, thus much lower than the sum of alpha-subunits. Even though increasing 3-fold after SW-transfer, beta-subunit availability may still limit functional pump synthesis. The mRNAs of the predominant alpha(1a) and alpha(1b) isoforms were localised by in situ hybridisation in specific gill cells of both FW and SW salmon. Labelling occurred mainly in presumed chloride cells and cells deep in the filament but occasionally also on lamellae. Overall, the salinity-induced variation in labelling pattern and intensity matched the quantification data. In conclusion, the predominant switching of Na(+),K(+)-ATPase alpha-subunit isoform mRNA during salinity acclimation reflects a marked remodelling of mitochondrion-rich cells (MRCs) in the gill and probably tuning of the pump performance to accomplish a net reversal of gill ion transport in hypo- and hypertonic environments. SN - 0022-0949 UR - https://www.unboundmedicine.com/medline/citation/19088213/Multiplicity_of_expression_of_Na+K+_ATPase_{alpha}_subunit_isoforms_in_the_gill_of_Atlantic_salmon__Salmo_salar_:_cellular_localisation_and_absolute_quantification_in_response_to_salinity_change_ L2 - http://jeb.biologists.org/cgi/pmidlookup?view=long&pmid=19088213 DB - PRIME DP - Unbound Medicine ER -