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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

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)

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Leone, Francisco A. [1] ; Lucena, Malson N. [2] ; Fabri, Leonardo M. [1] ; Garcon, Daniela P. [3] ; Fontes, Carlos F. L. [4] ; Faleiros, Rogerio O. [5] ; Moraes, Cintya M. [1] ; McNamara, John C. [6, 7]
Total Authors: 8
[1] Univ Sao Paulo, Fac Filosofia Ciencias & Letras Ribeirao Preto, Dept Quim, Ave Bandeirantes 3900, BR-14040901 Ribeirao Preto, SP - Brazil
[2] Univ Fed Mato Grosso do Sul, Inst Biociencias, Campo Grande, MS - Brazil
[3] Univ Fed Triangulo Mineiro, Iturama, MG - Brazil
[4] Univ Fed Rio de Janeiro, Inst Bioquim Med, Rio De Janeiro, RJ - Brazil
[5] Univ Fed Espirito Santo, Dept Ciencias Agr & Biol, Sao Mateus, ES - Brazil
[6] Univ Sao Paulo, Fac Filosofia Ciencias & Letras Ribeirao Preto, Dept Biol, Ribeirao Preto, SP - Brazil
[7] Univ Sao Paulo, Ctr Biol Marinha, Sao Sebastiao, SP - Brazil
Total Affiliations: 7
Document type: Journal article
Web of Science Citations: 0

We analyzed the modulation by exogenous FXYD2 peptide and by endogenous protein kinases A and C, and Ca2+-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-+,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 Ca2+/calmodulin-dependent kinase inhibits activity. Stimulation by FXYD2 and inhibition by protein kinase C and Ca2+/calmodulin-dependent kinase are salinity-dependent. This is the first demonstration of inhibitory phosphorylation of a crustacean (Na+, K+)-ATPase by Ca2+/calmodulin-dependent kinase. At low salinities, the (Na+, K+)ATPase exhibited a single, low affinity ATP-binding site that showed Michaelis-Menten behavior. Above 18%S, a second, cooperative, high affinity ATP-binding site appeared, corresponding to 10-20% of total (Na+, K+)ATPase activity. Hemolymph osmolality was strongly hyper-/hypo-regulated in crabs acclimated at 2 to 35 parts per thousand S. Cl- was well hyper-/hypo-regulated although Na+ much less so, becoming isonatremic at elevated salinity. (Na+, K+)-ATPase activity was greatest in isosmotic crabs (26 parts per thousand S), decreasing notably at 35 parts per thousand S and also diminishing progressively from 18to 2 parts per thousand S. Hyper-osmoregulation in U. cordatus showed little dependence on gill (Na+, K+)-ATPase activity, suggesting a role for other ion transporters. These findings reveal that the salinity acclimation response in U. cordatus consists of a suite of enzymatic and osmoregulatory adjustments that maintain its osmotic homeostasis in a challenging, mangrove forest environment. (AU)

FAPESP's process: 13/24252-9 - The (Na+,K+)-ATPase in osmoregulatory capacity in crab Ucides cordatus: biochemical and molecular view
Grantee:Malson Neilson de Lucena
Support type: Scholarships in Brazil - Post-Doctorate
FAPESP's process: 16/25336-0 - Comparative biochemical study of gill (Na+, K +)- ATPase of Macrobrachium amazonicum (Heller, 1862) inhabitant of coastal and continental regions
Grantee:Francisco de Assis Leone
Support type: Regular Research Grants