info:eu-repo/semantics/article
An ACTH-activated protein tyrosine phosphatase (PTP) is modulated by PKA-mediated phosphorylation
Fecha
2000-11Registro en:
Paz, Cristina del Valle; Cornejo Maciel, Maria Fabiana; Poderoso, Cecilia; Gorostizaga, Alejandra Beatriz; Podesta, Ernesto Jorge; An ACTH-activated protein tyrosine phosphatase (PTP) is modulated by PKA-mediated phosphorylation; Taylor; Endocrine Research; 26; 4; 11-2000; 609-614
0743-5800
CONICET Digital
CONICET
Autor
Paz, Cristina del Valle
Cornejo Maciel, Maria Fabiana
Poderoso, Cecilia
Gorostizaga, Alejandra Beatriz
Podesta, Ernesto Jorge
Resumen
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.