[The phosphorylation and tyrosine kinase activity of an internalized complex of epidermal growth factor and its receptor]. / Fosforilirovanie i tirozinkinaznaia aktivnost' internalizovannogo kompleksa épidermal'nogo faktora rosta i ego retseptora.
Tsitologiia
; 32(2): 140-7, 1990.
Article
em Ru
| MEDLINE
| ID: mdl-2368159
ABSTRACT
A study was made of the functional state of the epidermal growth factor (EGF)--receptor complexes in A-431 cells. Conditions of surface bound EGF extraction were selected which allow to consider the intracellular EGF--receptor complexes only. A procedure of high efficient and specific immunoprecipitation of tyrosyl-phosphorylated EGF receptors was developed. It is shown that the dissociation of EGF--receptor complexes leads to receptor dephosphorylation due to a rapid and reversible inactivation of EGF receptor tyrosine kinase. The internalized receptor is found to be tyrosyl-phosphorylated and to retain tyrosine kinase for at least an hour after the internalization. The dynamics of dissociation, degradation and dephosphorylation of EGF--receptor complexes has been estimated. The rates of these processes prove to be almost negligible for the first 2.5 hours after internalization.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas Tirosina Quinases
/
Fator de Crescimento Epidérmico
/
Receptores ErbB
Limite:
Humans
Idioma:
Ru
Revista:
Tsitologiia
Ano de publicação:
1990
Tipo de documento:
Article