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Mangrove ecosystems are tidal wetlands with anaerobic, salt-saturated soils that support diverse fauna. Despite intensive studies on the osmoregulatory mechanisms of decapods inhabiting distinct osmotic niches, there is little information on the kinetic characteristics of the gill (Na, K)-ATPase of decapod crustaceans inhabiting mangroves. Here, we provide a comprehensive kinetic characterization of the K-phosphatase activity of the gill (Na, K)-ATPase in two semi-terrestrial brachyuran crabs, Goniopsis cruentata and Cardisoma guanhumi, which respectively inhabit intermittently flooded lower zones and drier upper zones along the vertical gradient of mangrove environments. This study revealed distinct kinetic profiles between the two species. Goniopsis cruentata shows twice as much K-phosphatase activity and a 3-fold greater affinity for p-nitrophenyl phosphate than Cardisoma guanhumi. Substrate hydrolysis by the Goniopsis cruentata enzyme follows cooperative kinetics, whereas Cardisoma guanhumi displays typical Michaelis-Menten behavior. In both species, stimulation by K ions shows cooperative kinetics. Notably, Cardisoma guanhumi also exhibits 25% higher K-phosphatase activity when both K and NH₄ are present. However, whether these differences arise from phylogenetic divergence or reflect physiological adaptation to different mangrove microhabitats remains unresolved. Given the paucity of kinetic studies on (Na, K)-ATPase in semi-/terrestrial crabs, our data contribute novel insights into the enzymatic basis of ion transport in decapods inhabiting variable salinity environments.
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http://dx.doi.org/10.1016/j.cbpb.2025.111129 | DOI Listing |
Comp Biochem Physiol B Biochem Mol Biol
September 2025
Universidade Federal do Triângulo Mineiro, Campus Universitário de Iturama, Iturama, MG, Brazil.
Mangrove ecosystems are tidal wetlands with anaerobic, salt-saturated soils that support diverse fauna. Despite intensive studies on the osmoregulatory mechanisms of decapods inhabiting distinct osmotic niches, there is little information on the kinetic characteristics of the gill (Na, K)-ATPase of decapod crustaceans inhabiting mangroves. Here, we provide a comprehensive kinetic characterization of the K-phosphatase activity of the gill (Na, K)-ATPase in two semi-terrestrial brachyuran crabs, Goniopsis cruentata and Cardisoma guanhumi, which respectively inhabit intermittently flooded lower zones and drier upper zones along the vertical gradient of mangrove environments.
View Article and Find Full Text PDFComp Biochem Physiol C Toxicol Pharmacol
December 2023
Departamento de Biologia, Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto, Universidade de São Paulo, Ribeirão Preto, Brazil; Centro de Biologia Marinha, Universidade de São Paulo, São Sebastião, Brazil. Electronic address:
We used the gill (Na, K)-ATPase as a molecular marker to provide a comprehensive kinetic analysis of the effects of Coin vitro on the modulation of K-phosphatase activity in the Blue crab Callinectes danae. Co can stimulate or inhibit K-phosphatase activity. With Mg, K-phosphatase activity is almost completely inhibited by Co.
View Article and Find Full Text PDFEcotoxicol Environ Saf
September 2017
Marine Biology and Fisheries, Rosenstiel School of Marine and Atmospheric Science, University of Miami, Marine Biology and Fisheries, Miami, Florida.
The effects of exposure to copper (Cu) on tissue Cu accumulation, on hemolymph osmotic, Na and Cl regulation, and on gill Na/K-ATPase (NKA) and carbonic anhydrase (CA) activities were evaluated in the fiddler crab Minuca rapax. Waterborne copper was delivered to the crabs at one of three salinities (seawater at 25‰ salinity [S] = isosmotic control; distilled water [<0.1‰ S] = hypo-osmotic medium; or 60‰ S = hyper-osmotic seawater) either for 5 days in a 0.
View Article and Find Full Text PDFArch Biochem Biophys
February 2013
Departamento de Biologia Molecular, Centro de Ciências Exatas e da Natureza, Universidade Federal da Paraíba, Brazil.
We provide an extensive characterization of the modulation by p-nitrophenylphosphate, Mg²⁺, Na⁺, K(+), Rb⁺, NH(4)(+) and pH of gill microsomal K⁺-phosphatase activity in the posterior gills of Callinectes ornatus acclimated to low salinity (21‰). The synergistic stimulation by K⁺ and NH(4)(+) of the K⁺-phosphatase activity is a novel finding, and may constitute a species-specific feature of K(+)/NH(4)(+) interplay that regulates crustacean gill (Na⁺, K⁺)-ATPase activity. p-Nitrophenylphosphate was hydrolyzed at a maximum rate (V) of 69.
View Article and Find Full Text PDFCell Mol Biol (Noisy-le-grand)
July 2011
INSERM U927, School of Medicine, CHU/University Hospital, University of Poitiers, Poitiers, France.
In skeletal muscle the relationship between Na+,K+-ATPase activity and isoform content remains controversial (9,6). It could be due to the fiber-type content, membrane isolation and analytical methods. We investigated the distribution of subunit α1 and α2 Na+,K+-ATPase catalytic isoforms and the Na+,K+-ATPase activity in isolated membranes from white ( type I and glycolitic fibers) and red (type II and oxidative fibers) skeletal muscles.
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