ArticleThe Journal of membrane biology2008
Importance for absorption of Na+ from freshwater of lysine, valine and serine substitutions in the alpha1a-isoform of Na,K-ATPase in the gills of rainbow trout (Oncorhynchus mykiss) and Atlantic salmon (Salmo salar).
Article in The Journal of membrane biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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12 citing papers in PubMed, 48 citations in OpenAlex.
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- Molecular characterization and expression of NaFish physiology and biochemistry · 2016Article
- Does Japanese medaka (Oryzias latipes) exhibit a gill Na(+)/K(+)-ATPase isoform switch during salinity change?Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2016Article
- Comparisons of two types of teleostean pseudobranchs, silver moony (Monodactylus argenteus) and tilapia (Oreochromis mossambicus), with salinity-dependent morphology and ion transporter expression.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2015Article
- Differential expression of Na+, K(+)-ATPase α-1 isoforms during seawater acclimation in the amphidromous galaxiid fish Galaxias maculatus.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2013Article
- Characterization of Na(+) uptake in the endangered desert pupfish, Cyprinodon macularius (Baird and Girard).Conservation physiology · 2013Article
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1 author at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
In the gills of rainbow trout and Atlantic salmon, the alpha1a- and alpha1b-isoforms of Na,K-ATPase are expressed reciprocally during salt acclimation. The alpha1a-isoform is important for Na(+) uptake in freshwater, but the molecular basis for the functional differences between the two isoforms is not known. Here, three amino acid substitutions are identified in transmembrane segment 5 (TM5), TM8 and TM9 of the alpha1a-isoform compared to the alpha1b-isoform, and the functional consequences are examined by mutagenesis and molecular modeling on the crystal structures of Ca-ATPase or porcine kidney Na,K-ATPase. In TM5 of the alpha1a-isoform, a lysine substitution, Asn783 --> Lys, inserts the epsilon-amino group in cation site 1 in the E(1) form to reduce the Na(+)/ATP ratio. In the E(2) form the epsilon-amino group approaches cation site 2 to force ejection of Na(+) to the blood phase and to interfere with binding of K(+). In TM8, a Asp933 --> Val substitution further reduces K(+) binding, while a Glu961 --> Ser substitution in TM9 can prevent interaction of FXYD peptides with TM9 and alter Na(+) or K(+) affinities. Together, the three substitutions in the alpha1a-isoform of Na,K-ATPase act to promote binding of Na(+) over K(+) from the cytoplasm, to reduce the Na(+)/ATP ratio and the work done in one Na,K pump cycle of active Na(+) transport against the steep gradient from freshwater (10-100 microM: Na(+)) to blood (160 mM: Na(+)) and to inhibit binding of K(+) to allow Na(+)/H(+) rather than Na(+)/K(+) exchange.
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