A kinetic study of the gill (Na+, K+)-ATPase, and its role in ammonia excretion in the intertidal hermit crab, Clibanarius vittatus

Gonçalves, Rúbia R.; Masui, Douglas Chodi; McNamara, John Campbell; Mantelatto, Fernando L.; Garçon, Daniela P.; Furriel, Rosa dos Prazeres Melo; Leone, Francisco de Assis

doi:10.1016/j.cbpa.2006.07.007

Cited by 42 publications

(69 citation statements)

References 56 publications

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“…O peso da isoforma foi muito parecida com a encontrada em diversas espécies, como Callinectes ornatos recém-capturado ou aclimatado a diferentes salinidades (GARÇON et. al., 2007;GARÇON et al, 2009); Callinectes danae (MASUI et al, 2002); Macrobrachium amazonicum (SANTOS et al, 2007) e Clibanarius simmetrycus recém-capturado ou aclimatado a elevada salinidade (GONÇALVES et. al., 2006;LUCENA et al, 2012).…”

Section: -Estudo Da Fração Microsomal De C Guanhumiunclassified

“…Os sítios de ligação de alta afinidade, muitas vezes observados para a hidrólise de ATP pela (Na + ,K + )-ATPase de crustáceos (MASUI et al, 2002;GONÇALVES et al, 2006;SANTOS et al, 2007;LUCENA et al, 2012), não foram revelados para a hidrólise de pnitrofenilfosfato, sugerindo que eles não estão disponíveis na forma E 2 da enzima de C.…”

Section: -Atividade Pnffase Da Fração Microsomal Do Tecido Branquial unclassified

“…vittatus (GONÇALVES et al, 2006) e para outras (Na + ,K + )-ATPases já estudadas (LUCU & TOWLE, 2003.…”

Section: -Efeito De Metais Divalentes Na Atividadeunclassified

“…Na ausência de íons magnésio a enzima não é capaz de hidrolisar o ATP, pois o complexo Mg-ATP é o verdadeiro substrado da (Na + ,K + )-ATPase (GLYNN, 1985;FURRIEL et al, 2000;KARLISH, 2003;GARÇON et al, 2007). Porém excesso de ATP ou Mg 2+ livre, inibem a atividade ATPase, como observado nesse estudo bem como para a enzima isolada de diversas fontes (ROBINSON, 1981;ROBINSON e PRATAP, 1991;TENTES e STRATAKIS, 1991;FURRIEL et al, 2000;MASUI et al, 2002;GONÇALVES et al, 2006;GARÇON et al, 2007;SANTOS et al, 2007). A afinidade da enzima de tecido branquial de C. guanhumi, recém-capturado e aclimatado à 22‰ S, pelos íons magnésio é muito similar aos valores relatados para a enzima de vertebrados (GLYNN, 1985;ROBINSON e PRATAP, 1991), membrana axonal de caranguejo (GACHE et al, 1976;ROSSI et al, 1978) e tecido branquial de M. olfersii (FURRIEL et al, 2000), C. danae (MASUI et al, 2002), C. vittatus (GONÇALVES et al, 2006) e X. kroyeri .…”

Section: -Efeito De Metais Divalentes Na Atividadeunclassified

“…olfersi , M. rosenbergii (FRANÇA et al, 2013), Clibanarius vittatus (GONÇALVES et al, 2006;LUCENA et al, 2012), Callinectes ornatus (GARÇON et al, 2007; (FURRIEL et al, 2001). …”

Section: Figura 3 Esquema Da Estrutura Das Subunidades Da (Na + K +mentioning

confidence: 99%

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Caracterização cinética e molecular da (Na+,K+)-ATPase do tecido branquial do caranguejo Cardisoma guanhumi (Latreille,1825).

Farı́as¹

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Section: -Estudo Da Fração Microsomal De C Guanhumiunclassified

Section: -Atividade Pnffase Da Fração Microsomal Do Tecido Branquial unclassified

“…vittatus (GONÇALVES et al, 2006) e para outras (Na + ,K + )-ATPases já estudadas (LUCU & TOWLE, 2003.…”

Section: -Efeito De Metais Divalentes Na Atividadeunclassified

“…olfersi , M. rosenbergii (FRANÇA et al, 2013), Clibanarius vittatus (GONÇALVES et al, 2006;LUCENA et al, 2012), Callinectes ornatus (GARÇON et al, 2007; (FURRIEL et al, 2001). …”

Section: Figura 3 Esquema Da Estrutura Das Subunidades Da (Na + K +mentioning

confidence: 99%

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Caracterização cinética e molecular da (Na+,K+)-ATPase do tecido branquial do caranguejo Cardisoma guanhumi (Latreille,1825).

Farı́as¹

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Low salinity‐induced alterations in epithelial ultrastructure, Na⁺/K⁺‐ATPase immunolocalization and enzyme kinetic characteristics in the gills of the thinstripe hermit crab, Clibanarius vittatus (Anomura, Diogenidae)

et al. 2017

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Fresh caught Clibanarius vittatus [SW, 31‰ salinity (S)] were acclimated to a dilute medium (15‰ S) for 10 days, employing silver staining to locate gill ion transporting tissue, immunofluorescence to localize the Na/K-ATPase α-subunit in the lamellae, and electron microscopy to portray ultrastructural changes in the gill epithelia. Na/K-ATPase activity was characterized kinetically in a gill microsomal fraction, including synergistic stimulation by NH plus K. Silver staining revealed that all 26 phyllobranchiate arthro- and pleurobranchiae participate in ion transport. Na/K-ATPase α-subunit staining was weak in SW crabs and distributed exclusively and irregularly within the intralamellar septal cells, particularly at the septal-pillar cell body junctions, and septal cell cytoplasm facing the hemolymph space. In 15‰ S crabs, α-subunit localization was intense, occupying the entire thickened septum. Pillar cells and flanges did not stain. Mitochondria and membrane foldings increased in the pillar cell flanges and intralamellar septal cells, greatly amplifying surface area. Only a single ATP binding site (V = 130.8 ± 10.5 nmol min mg protein; K = 55.3 ± 1.7 μmol l) obeying Michaelis-Menten kinetics was disclosed. Na/K-ATPase activity was modulated by Mg, Na, and NH, exhibiting site-site interactions; K modulation showed Michaelis-Menten kinetics. K plus NH synergistically stimulated activity ≈ 1.7-fold. Ouabain inhibited total ATPase activity by ≈ 70% (K = 220-300 μmol l), revealing phosphohydrolytic activities other than the Na/K-ATPase. Despite ample phylogenetic separation, the phyllobranchiate lamellae of the Anomura and Caridea share many ultrastructural features, that is, an intralamellar septum and opposed abutting pillar cells, similar Na/K-ATPase distribution, and comparable kinetic characteristics. These findings suggest either convergent evolution at the structural and biochemical levels, or preservation of traits present in a remote common ancestor.

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Structural and biochemical correlates of Na⁺,K⁺‐ATPase driven ion uptake across the posterior gill epithelium of the true freshwater crab, Dilocarcinus pagei (Brachyura, Trichodactylidae)

et al. 2010

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To better comprehend the structural and biochemical underpinnings of ion uptake across the gills of true freshwater crabs, we performed an ultrastructural, ultracytochemical and morphometric investigation, and kinetically characterized the Na(+),K(+)-ATPase, in posterior gill lamellae of Dilocarcinus pagei. Ultrastructurally, the lamellar epithelia are markedly asymmetrical: the thick, mushroom-shaped, proximal ionocytes contain elongate mitochondria (41% cell volume) associated with numerous (≈14 µm² membrane per µm³cytoplasm), deep invaginations that house the Na(+),K(+)-ATPase, revealed ultracytochemically. Their apical surface is amplified (7.5 µm² µm⁻²)) by stubby evaginations whose bases adjoin mitochondria below the subcuticular space. The apical membrane of the thin, distal ionocytes shows few evaginations (1.6 µm² µm⁻²), each surrounding a mitochondrion, abundant in the cytoplasm below the subcuticular space; basolateral invaginations and mitochondria are few. Fine basal cytoplasmic bridges project across the hemolymph space, penetrating into the thick ionocytes, suggesting ion movement between the epithelia. Microsomal Na(+),K(+)-ATPase specific activity resembles marine crabs but is ≈5-fold less than in species from fluctuating salinities, and freshwater shrimps, suggesting ion loss compensation by strategies other than Na(+) uptake. Enzyme apparent K(+) affinity attains 14-fold that of marine crabs, emphasizing the relevance of elevated K(+) affinity to the conquest of fresh water. Western blotting and biphasic ouabain inhibition disclose two α-subunit isoforms comprising distinct functional isoenzymes. While enzyme activity is not synergistically stimulated by NH(4) (+) and K(+), each increases affinity for the other, possibly assuring appropriate intracellular K(+) concentrations. These findings reveal specific structural and biochemical adaptations that may have allowed the establishment of the Brachyura in fresh water.

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A kinetic study of the gill (Na+, K+)-ATPase, and its role in ammonia excretion in the intertidal hermit crab, Clibanarius vittatus

Cited by 42 publications

References 56 publications

Caracterização cinética e molecular da (Na+,K+)-ATPase do tecido branquial do caranguejo Cardisoma guanhumi (Latreille,1825).

Caracterização cinética e molecular da (Na+,K+)-ATPase do tecido branquial do caranguejo Cardisoma guanhumi (Latreille,1825).

Low salinity‐induced alterations in epithelial ultrastructure, Na⁺/K⁺‐ATPase immunolocalization and enzyme kinetic characteristics in the gills of the thinstripe hermit crab, Clibanarius vittatus (Anomura, Diogenidae)

Structural and biochemical correlates of Na⁺,K⁺‐ATPase driven ion uptake across the posterior gill epithelium of the true freshwater crab, Dilocarcinus pagei (Brachyura, Trichodactylidae)

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A kinetic study of the gill (Na+, K+)-ATPase, and its role in ammonia excretion in the intertidal hermit crab, Clibanarius vittatus

Cited by 42 publications

References 56 publications

Caracterização cinética e molecular da (Na+,K+)-ATPase do tecido branquial do caranguejo Cardisoma guanhumi (Latreille,1825).

Caracterização cinética e molecular da (Na+,K+)-ATPase do tecido branquial do caranguejo Cardisoma guanhumi (Latreille,1825).

Low salinity‐induced alterations in epithelial ultrastructure, Na+/K+‐ATPase immunolocalization and enzyme kinetic characteristics in the gills of the thinstripe hermit crab, Clibanarius vittatus (Anomura, Diogenidae)

Structural and biochemical correlates of Na+,K+‐ATPase driven ion uptake across the posterior gill epithelium of the true freshwater crab, Dilocarcinus pagei (Brachyura, Trichodactylidae)

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Low salinity‐induced alterations in epithelial ultrastructure, Na⁺/K⁺‐ATPase immunolocalization and enzyme kinetic characteristics in the gills of the thinstripe hermit crab, Clibanarius vittatus (Anomura, Diogenidae)

Structural and biochemical correlates of Na⁺,K⁺‐ATPase driven ion uptake across the posterior gill epithelium of the true freshwater crab, Dilocarcinus pagei (Brachyura, Trichodactylidae)