Primary amino acid sequences of decapod (Na, K)-ATPase provide evolutionary insights into osmoregulatory mechanisms.

Decapod Crustacea exhibit a marine origin, but many taxa have occupied environments ranging from brackish to fresh water and terrestrial habitats, overcoming their inherent osmotic challenges. Osmotic and ionic regulation is achieved by the gill epithelia, driven by two active ATP-hydrolyzing ion transporters, the basal (Na, K)-ATPase and the apical V(H)-ATPase. The kinetic characteristic of gill (Na, K)-ATPase and the mRNA expression of its α subunit have been widely studied in various decapod species under different salinity challenges.

(Na, K)- ATPase kinetics in Macrobrachium pantanalense: highlighting intra- and interspecific variation within the Macrobrachium amazonicum complex.

The Macrobrachium amazonicum complex is composed of at least the Macrobrachium amazonicum and Macrobrachium pantanalense species, with the latter described from specimens originally identified as part of an endemic M. amazonicum population in the Brazilian Pantanal region. While there may be a reproductive barrier between these two Macrobrachium species, both are phylogenetically close, with small genetic distance.

Differential effects of cobalt ions in vitro on gill (Na, K)-ATPase kinetics in the Blue crab Callinectes danae (Decapoda, Brachyura).

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.

A kinetic characterization of the gill V(H)-ATPase from two hololimnetic populations of the Amazon River shrimp Macrobrachium amazonicum.

This investigation examines the kinetic characteristics and effect of acclimation to a brackish medium (21 ‰S) on gill V(H)-ATPase activity in two hololimnetic populations of M. amazonicum. We also investigate the cellular immunolocalization of the enzyme.

Salinity-dependent modulation by protein kinases and the FXYD2 peptide of gill (Na, K)-ATPase activity in the freshwater shrimp Macrobrachium amazonicum (Decapoda, Palaemonidae).

The geographical distribution of aquatic crustaceans is determined by ambient factors like salinity that modulate their biochemistry, physiology, behavior, reproduction, development and growth. We investigated the effects of exogenous pig FXYD2 peptide and endogenous protein kinases A and C on gill (Na, K)-ATPase activity, and characterized enzyme kinetic properties in a freshwater population of Macrobrachium amazonicum in fresh water (<0.5 ‰ salinity) or acclimated to 21 ‰S.

Effects of ammonia on gill (Na, K)-ATPase kinetics in a hololimnetic population of the Amazon River shrimp Macrobrachium amazonicum.

Water quality is essential for successful aquaculture. For freshwater shrimp farming, ammonia concentrations can increase considerably, even when culture water is renewed frequently, consequently increasing the risk of ammonia intoxication. We investigated ammonia lethality (LC-96 h) in a hololimnetic population of the Amazon River shrimp Macrobrachium amazonicum from the Paraná/Paraguay River basin, including the effects of exposure to 4.

Osmotic and ionic regulation, and modulation by protein kinases, FXYD2 peptide and ATP of gill (Na, K)-ATPase activity, in the swamp ghost crab Ucides cordatus (Brachyura, Ocypodidae).

We analyzed the modulation by exogenous FXYD2 peptide and by endogenous protein kinases A and C, and Ca-calmodulin-dependent kinase, of gill (Na, K)-ATPase activity in the semi-terrestrial mangrove crab Ucides cordatus after 10-days acclimation to different salinities. Osmotic and ionic regulatory ability and gill (Na, K)-ATPase activity also were evaluated. (Na, K)-ATPase activity is stimulated by exogenous pig kidney FXYD2 peptide, while phosphorylation by endogenous protein kinases A and C and Ca/calmodulin-dependent kinase inhibits activity.

Biochemical Characterization and Allosteric Modulation by Magnesium of (Na, K)-ATPase Activity in the Gills of the Red Mangrove Crab Goniopsis cruentata (Brachyura, Grapsidae).

We provide a kinetic characterization of (Na, K)-ATPase activity in a posterior gill microsomal fraction from the grapsid crab Goniopsis cruentata. (Na, K)-ATPase activity constitutes 95% of total ATPase activity, and sucrose density centrifugation reveals an ATPase activity peak between 25 and 35% sucrose, distributed into two, partially separated protein fractions. The (Na, K)-ATPase α-subunit is localized throughout the ionocyte cytoplasm and has an M of ≈ 10 kDa and hydrolyzes ATP obeying cooperative kinetics.

Dopamine binding directly up-regulates (Na, K)-ATPase activity in the gills of the freshwater shrimp Macrobrachium amazonicum.

We examined the effects of exogenous dopamine on gill (Na, K)-ATPase activity in vitro in microsomal preparations from juvenile or adult freshwater shrimp, Macrobrachium amazonicum. Dopamine had no effect on enzyme activity in juveniles but stimulated activity in adult shrimp gills by ≈35%. Stimulation of the gill (Na, K)-ATPase in adult shrimps by 100 mmol L dopamine was characterized kinetically by varying ATP, MgATP, and Na and K concentrations, together with inhibition by ouabain.

Kinetic characterization of the gill (Na, K)-ATPase in a hololimnetic population of the diadromous Amazon River shrimp Macrobrachium amazonicum (Decapoda, Palaemonidae).

We provide a kinetic characterization of (Na, K)-ATPase activity in a posterior gill microsomal fraction from a hololimnetic population of the diadromous Amazon River shrimp Macrobrachium amazonicum. Sucrose density gradient centrifugation reveals two distinct membrane fractions showing considerable (Na, K)ATP-ase activity, but also containing other microsomal ATPases. Only a single immune-reactive (Na, K)-ATPase with M of ≈110 kDa is present that hydrolyzes ATP with V = 130.