| Author | Cortes, Vanessa Faria | |
| Author | Lopes, Fabio Eduardo Veiga | |
| Author | Barrabin, Hector | |
| Author | Ferreira, Marcelo Alves | |
| Author | Fontes, Carlos Frederico Leite | |
| Access date | 2020-01-03T14:46:25Z | |
| Available date | 2020-01-03T14:46:25Z | |
| Document date | 2006 | |
| Citation | CORTES, Vanessa Faria et al. The γ subunit of Na⁺, K⁺-ATPase: role on ATPase activity and regulatory phosphorylation by PKA. The International Journal of Biochemistry and Cell Biology, v. 38, n. 11, p. 1901-1913, 17 May 2006. | |
| ISSN | 1357-2725 | |
| URI | https://www.arca.fiocruz.br/handle/icict/38967 | |
| Language | eng | en_US |
| Publisher | Elsevier | |
| Rights | restricted access | |
| Title | The γ subunit of Na⁺, K⁺-ATPase: role on ATPase activity and regulatory phosphorylation by PKA | en_US |
| Type | Article | |
| DOI | 10.1016/j.biocel.2006.05.002 | |
| Abstract | In kidney, Na⁺, K⁺-ATPase is an oligomer (αβγ) with equimolar amounts of essential α and β subunits and one small hydrophobic FXYD protein (γ subunit). This report describes γ subunit as an activator of pig kidney outer medulla Na⁺, K⁺-ATPase in aqueous medium. The effects of γ subunit on Na⁺, K⁺-ATPase were dose-dependent and preincubation-dependent. Changes in αβ/γ stoichiometry did not alter Kₘ₁ for ATP, and slightly increased Kₘ₂, but Vₘₐₓ was increased at both catalytic and regulatory sites. Hydroxylamine treatment of enzyme phosphorylated by ATP (E-P), in the presence of additional γ subunit, revealed that 52% of the E-P accumulation was not via acyl-phosphate formation. The γ subunit was phosphorylated by endogenous kinases and by commercial catalytic subunit of protein kinase A (PKA). Additionally, we demonstrated that PKA phosphorylation of γ subunit increased its capacity to stimulate ATP hydrolysis. These results suggest that γ subunit can act as an intrinsic Na⁺, K⁺-ATPase regulator in kidney. | en_US |
| Affilliation | Universidade Federal do Rio de Janeiro. Centro de Ciências da Saúde. Instituto de Bioquímica Médica Leopoldo de Meis. Laboratório de Estrutura e Regulação de Proteínas e ATPases. Programa de Biologia Estrutural. Rio de Janeiro, RJ, Brasil. | |
| Affilliation | Universidade Federal do Rio de Janeiro. Centro de Ciências da Saúde. Instituto de Bioquímica Médica Leopoldo de Meis. Laboratório de Estrutura e Regulação de Proteínas e ATPases. Programa de Biologia Estrutural. Rio de Janeiro, RJ, Brasil. | |
| Affilliation | Universidade Federal do Rio de Janeiro. Centro de Ciências da Saúde. Instituto de Bioquímica Médica Leopoldo de Meis. Laboratório de Estrutura e Regulação de Proteínas e ATPases. Programa de Biologia Estrutural. Rio de Janeiro, RJ, Brasil. | |
| Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Departamento de Bioquímica e Biologia Molecular. Rio de Janeiro, RJ, Brasil. | |
| Affilliation | Universidade Federal do Rio de Janeiro. Centro de Ciências da Saúde. Instituto de Bioquímica Médica Leopoldo de Meis. Laboratório de Estrutura e Regulação de Proteínas e ATPases. Programa de Biologia Estrutural. Rio de Janeiro, RJ, Brasil. | |
| Subject | Na⁺ | en_US |
| Subject | K⁺-ATPase | en_US |
| Subject | Pig kidney | en_US |
| Subject | γ subunit | en_US |
| Subject | Phosphorylation | en_US |
| Subject | PKA | en_US |
| e-ISSN | 1878-5875 | |
| Embargo date | 2025-01-01 | |
| xmlui.metadata.dc.subject.ods | 03 Saúde e Bem-Estar | |
