Redox-linked ligand-independent cell surface triggering for extensive protein tyrosine phosphorylation.
FEBS Lett
; 317(1-2): 35-8, 1993 Feb 08.
Article
em En
| MEDLINE
| ID: mdl-8381367
ABSTRACT
Exposure of lymphocytes to 0.2-2 mM HgCl2, a thiol-reactive heavy metal, induced extensive tyrosine phosphorylation of multiple cellular proteins. The phosphorylation started as quickly as 5 s after exposure to HgCl2, and was irreversible. Another 3 thiol-reactive chemicals also displayed similar, though less marked, actions, whereas dithiothreitol, a reducing agent, antagonized the HgCl2 action. The demonstrated new action of HgCl2 indispensably required membrane-intact cells as a target. Whereas exposure of lymphocytes to > 0.2 mM HgCl2 caused rapid cell death, 0.01-0.1 mM HgCl2 affected the cells so as to accelerate their c-fos transcription. These results suggest a novel redox-linked mechanism of cell surface triggering of intracellular protein kinase activity, which is independent of receptor-ligand interactions.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Tirosina
/
Linfócitos
/
Proteínas
/
Compostos de Ouro
Limite:
Animals
Idioma:
En
Ano de publicação:
1993
Tipo de documento:
Article