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)

Author(s)

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]}

Affiliation

^[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

• Document type: Journal article
• Source: COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY; v. 250, DEC 2020.
• Web of Science Citations: 0

Abstract

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 Opportunities: Scholarships in Brazil - Post-Doctoral
• 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 Opportunities: Regular Research Grants