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Substrain-related dependence of Cu(I)-ATPase activity among prion protein-null mice.
Adão-Novaes, J; Valverde, R H F; Landemberger, M C; Silveira, M S; Simões-Pires, E N; Lowe, J; Linden, R.
Afiliação
  • Adão-Novaes J; Instituto de Biofísica Carlos Chagas Filho, UFRJ, Rio de Janeiro, Brazil.
  • Valverde RHF; Instituto de Biofísica Carlos Chagas Filho, UFRJ, Rio de Janeiro, Brazil.
  • Landemberger MC; Centro Internacional de Pesquisa A.C. Camargo Cancer Center, São Paulo, SP, Brazil.
  • Silveira MS; Instituto de Biofísica Carlos Chagas Filho, UFRJ, Rio de Janeiro, Brazil.
  • Simões-Pires EN; Instituto de Biofísica Carlos Chagas Filho, UFRJ, Rio de Janeiro, Brazil.
  • Lowe J; Instituto de Biofísica Carlos Chagas Filho, UFRJ, Rio de Janeiro, Brazil.
  • Linden R; Instituto de Biofísica Carlos Chagas Filho, UFRJ, Rio de Janeiro, Brazil. Electronic address: rlinden@biof.ufrj.br.
Brain Res ; 1727: 146550, 2020 01 15.
Article em En | MEDLINE | ID: mdl-31726043
The prion protein (PrPC) binds copper and affects copper metabolism, albeit among a poorly understood functional landscape. Much of the data on physiological roles of PrPC were obtained in mice of mixed genetic background deficient of the PrPC-coding gene Prnp. This strategy is currently under scrutiny due to the flanking gene problem, in particular related with a polymorphism, typical of both the 129Sv and 129Ola mouse substrains, in the Sirpa gene located in the vicinity of Prnp. Here we report an investigation of biochemical properties of Cu(I)-ATPases as a function of genotype in two strains of PrPC-deficient mice. We found that both the brain and liver of Prnp-null mice of mixed B6;129Sv background had diminished activity, accompanied by increased catalytic phosphorylation of Cu(I)-ATPase, as compared with the respective wild-type animals. However, no such differences were found between Prnp-null and wild-type mice of a B10;129Ola background. Activity of Cu(I)-ATPase was strongly reduced in brain tissue from mice of 129Sv strain, when compared with wild-type either of B6;129Sv, and especially of mice of the B6 strain. No differences between wild-type and Prnp-null brain tissue were noted in the expression of either Atp7a or b genes, and RFLP analysis indicated that the Sirpa129 polymorphism was present in both the B6;129Sv and B10;129Ola Prnp-null mouse colonies used in this study. The results suggest a novel substrain-dependent effect of 129Sv, but not 129Ola, genotype upon the regulation of the Cu(I)-ATPase catalytic cycle in Prnp-null mice, rather than either a Prnp-dependent, or a 129 strain-dependent effect.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Encéfalo / Proteínas Priônicas / ATPases Transportadoras de Cobre Limite: Animals Idioma: En Revista: Brain Res Ano de publicação: 2020 Tipo de documento: Article País de afiliação: Brasil País de publicação: Holanda
Texto completo
Adicionar na Minha BVS
Imprimir
XML
PubMed Links
Buscar no Google

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Encéfalo / Proteínas Priônicas / ATPases Transportadoras de Cobre Limite: Animals Idioma: En Revista: Brain Res Ano de publicação: 2020 Tipo de documento: Article País de afiliação: Brasil País de publicação: Holanda