ArticlePloS one2014
Modulation by K+ Plus NH4+ of microsomal (Na+, K+)-ATPase activity in selected ontogenetic stages of the diadromous river shrimp Macrobrachium amazonicum (Decapoda, Palaemonidae).
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 29 citations in OpenAlex.
- Molecular and physiological adaptations to low-salinity stress in penaeid shrimp: a focus on Litopenaeus vannamei and Penaeus monodon.Stress biology · 2026Review
- Integrated Transcriptomic and Metabolomic Analyses Reveal the Adaptive Mechanisms of a Low-Salinity Selected Population of Pacific White Shrimp (Litopenaeus vannamei).Marine biotechnology (New York, N.Y.) · 2025Article
- Mechanisms of NaFrontiers in physiology · 2022Review
- Biochemical Characterization and Allosteric Modulation by Magnesium of (NaThe Journal of membrane biology · 2020Article
- A Kinetic Characterization of the Gill (NaThe Journal of membrane biology · 2017Article
- Polyamines regulate phosphorylation-dephosphorylation kinetics in a crustacean gill (NaMolecular and cellular biochemistry · 2017Article
- Perfused Gills Reveal Fundamental Principles of pH Regulation and Ammonia Homeostasis in the CephalopodFrontiers in physiology · 2017Article
- A kinetic characterization of (Na+, K+)-ATPase activity in the gills of the pelagic seabob shrimp Xiphopenaeus kroyeri (Decapoda, Penaeidae).The Journal of membrane biology · 2015Article
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We investigate the synergistic stimulation by K(+) plus NH4 (+) of (Na(+), K(+))-ATPase activity in microsomal preparations of whole zoea I and decapodid III, and in juvenile and adult river shrimp gills. Modulation of (Na(+), K(+))-ATPase activity is ontogenetic stage-specific, and particularly distinct between juveniles and adults. Although both gill enzymes exhibit two different sites for K(+) and NH4 (+) binding, in the juvenile enzyme, these two sites are equivalent: binding by both ions results in slightly stimulated activity compared to that of a single ionic species. In the adult enzyme, the sites are not equivalent: when one ion occupies its specific binding site, (Na(+), K(+))-ATPase activity is stimulated synergistically by ≈ 50% on binding of the complementary ion. Immunolocalization reveals the enzyme to be distributed predominantly throughout the intralamellar septum in the gill lamellae of juveniles and adults. Western blot analyses demonstrate a single immunoreactive band, suggesting a single (Na(+), K(+))-ATPase α-subunit isoform that is distributed into different density membrane fractions, independently of ontogenetic stage. We propose a model for the modulation by K(+) and NH4 (+) of gill (Na(+), K(+))-ATPase activity. These findings suggest that the gill enzyme may be regulated by NH4 (+) during ontogenetic development in M. amazonicum.
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