An ACTH-activated protein tyrosine phosphatase (PTP) is modulated by PKA-mediated phosphorylation.
Endocr Res
; 26(4): 609-14, 2000 Nov.
Article
em En
| MEDLINE
| ID: mdl-11196437
ABSTRACT
In adrenal cortex, ACTH regulation of steroidogenesis depends on PKA-dependent serine/threonine phosphorylation and also on the activity of protein tyrosine phosphatases (PTPs). In addition, ACTH increases total PTPs involving at least three soluble PTPs (50, 82 and 115 kDa). Serine/threonine phosphorylation of these enzymes themselves could be a regulatory mechanism of their activity since the increase of total PTP activity is dependent on PKA-activation. In this report we analyzed the effect of in vitro phospho-dephosphorylation processes on the activity displayed by the ACTH-activated PTP of 115 kDa. Using an in-gel PTP assay we demonstrate that dephosphorylation catalyzed by potato acid phosphatase (PAP) reduces the activity of the 115 kDa PTP present in ZF from ACTH-treated animals and PKA-mediated phosphorylation reverses this effect.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas Tirosina Fosfatases
/
Proteínas Quinases Dependentes de AMP Cíclico
/
Hormônio Adrenocorticotrópico
Limite:
Animals
Idioma:
En
Revista:
Endocr Res
Assunto da revista:
ENDOCRINOLOGIA
Ano de publicação:
2000
Tipo de documento:
Article
País de afiliação:
Argentina
País de publicação:
ENGLAND
/
ESCOCIA
/
GB
/
GREAT BRITAIN
/
INGLATERRA
/
REINO UNIDO
/
SCOTLAND
/
UK
/
UNITED KINGDOM