| Texto completo | |
| Autor(es): |
Adamis, Paula D. B.
[1]
;
Mannarino, Sergio C.
[1]
;
Riger, Cristiano J.
[1]
;
Duarte, Giselle
[1]
;
Cruz, Ana
[1]
;
Pereira, Marcos D.
[1]
;
Eleutherio, Elis C. A.
[1]
Número total de Autores: 7
|
| Afiliação do(s) autor(es): | [1] UFRJ, IQ, Dept Bioquim, BR-21941909 Rio De Janeiro - Brazil
Número total de Afiliações: 1
|
| Tipo de documento: | Artigo Científico |
| Fonte: | BIOMETALS; v. 22, n. 2, p. 243-249, APR 2009. |
| Citações Web of Science: | 8 |
| Resumo | |
In Saccharomyces cerevisiae, accumulation of cadmium-glutathione complex in cytoplasm inhibits cadmium absorption, glutathione transferase 2 is required for the formation of the complex and the vacuolar gamma-glutamyl transferase participates of the first step of glutathione degradation. Here, we proposed that Lap4, a vacuolar amino peptidase, is involved in glutathione catabolism under cadmium stress. Saccharomyces cerevisiae cells deficient in Lap4 absorbed almost 3-fold as much cadmium as the wild-type strain (wt), probably due to the lower rate of cadmium-glutathione complex synthesis in the cytoplasm. In wt, but not in lap4 strain, the oxidized/reduced GSH ratio and the Gtt activity increased in response to cadmium, confirming that the mutant is deficient in the synthesis of the complex probably because the degradation of vacuolar glutathione is impaired. Thus, under cadmium stress, Lap4 and gamma-glutamyl transferase seem to work together to assure an efficient glutathione turnover stored in the vacuole. (AU) | |
| Processo FAPESP: | 04/10067-6 - Estresse, transporte e metabolismo de alfa-glicosídios em Saccharomyces cerevisiae |
| Beneficiário: | Pedro Soares de Araujo |
| Modalidade de apoio: | Auxílio à Pesquisa - Temático |