An ACTH-activated protein tyrosine phosphatase (PTP) is modulated by PKA-mediated phosphorylation

Autores
Paz, Cristina del Valle; Cornejo Maciel, Maria Fabiana; Poderoso, Cecilia; Gorostizaga, Alejandra Beatriz; Podesta, Ernesto Jorge
Año de publicación
2000
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
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.
Fil: Paz, Cristina del Valle. Universidad de Buenos Aires. Facultad de Medicina. Departamento de Bioquímica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Cornejo Maciel, Maria Fabiana. Universidad de Buenos Aires. Facultad de Medicina. Departamento de Bioquímica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Poderoso, Cecilia. Universidad de Buenos Aires. Facultad de Medicina. Departamento de Bioquímica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Gorostizaga, Alejandra Beatriz. Universidad de Buenos Aires. Facultad de Medicina. Departamento de Bioquímica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Podesta, Ernesto Jorge. Universidad de Buenos Aires. Facultad de Medicina. Departamento de Bioquímica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Materia
Acth
Tyrosine Phosphatase
Pka
Phosphorylation
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/39236
Acceder
id CONICETDig_0e3bb95cc08f2b289fe1b1f56c0d8403
oai_identifier_str oai:ri.conicet.gov.ar:11336/39236
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling An ACTH-activated protein tyrosine phosphatase (PTP) is modulated by PKA-mediated phosphorylationPaz, Cristina del ValleCornejo Maciel, Maria FabianaPoderoso, CeciliaGorostizaga, Alejandra BeatrizPodesta, Ernesto JorgeActhTyrosine PhosphatasePkaPhosphorylationhttps://purl.org/becyt/ford/3.1https://purl.org/becyt/ford/3In 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.Fil: Paz, Cristina del Valle. Universidad de Buenos Aires. Facultad de Medicina. Departamento de Bioquímica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Cornejo Maciel, Maria Fabiana. Universidad de Buenos Aires. Facultad de Medicina. Departamento de Bioquímica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Poderoso, Cecilia. Universidad de Buenos Aires. Facultad de Medicina. Departamento de Bioquímica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Gorostizaga, Alejandra Beatriz. Universidad de Buenos Aires. Facultad de Medicina. Departamento de Bioquímica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Podesta, Ernesto Jorge. Universidad de Buenos Aires. Facultad de Medicina. Departamento de Bioquímica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaTaylor2000-11info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/39236Paz, 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; 609-6140743-5800CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.3109/07435800009048579info:eu-repo/semantics/altIdentifier/url/https://www.tandfonline.com/doi/abs/10.3109/07435800009048579info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:53:01Zoai:ri.conicet.gov.ar:11336/39236instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-03 09:53:02.192CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv An ACTH-activated protein tyrosine phosphatase (PTP) is modulated by PKA-mediated phosphorylation
title An ACTH-activated protein tyrosine phosphatase (PTP) is modulated by PKA-mediated phosphorylation
spellingShingle An ACTH-activated protein tyrosine phosphatase (PTP) is modulated by PKA-mediated phosphorylation
Paz, Cristina del Valle
Acth
Tyrosine Phosphatase
Pka
Phosphorylation
title_short An ACTH-activated protein tyrosine phosphatase (PTP) is modulated by PKA-mediated phosphorylation
title_full An ACTH-activated protein tyrosine phosphatase (PTP) is modulated by PKA-mediated phosphorylation
title_fullStr An ACTH-activated protein tyrosine phosphatase (PTP) is modulated by PKA-mediated phosphorylation
title_full_unstemmed An ACTH-activated protein tyrosine phosphatase (PTP) is modulated by PKA-mediated phosphorylation
title_sort An ACTH-activated protein tyrosine phosphatase (PTP) is modulated by PKA-mediated phosphorylation
dc.creator.none.fl_str_mv Paz, Cristina del Valle
Cornejo Maciel, Maria Fabiana
Poderoso, Cecilia
Gorostizaga, Alejandra Beatriz
Podesta, Ernesto Jorge
author Paz, Cristina del Valle
author_facet Paz, Cristina del Valle
Cornejo Maciel, Maria Fabiana
Poderoso, Cecilia
Gorostizaga, Alejandra Beatriz
Podesta, Ernesto Jorge
author_role author
author2 Cornejo Maciel, Maria Fabiana
Poderoso, Cecilia
Gorostizaga, Alejandra Beatriz
Podesta, Ernesto Jorge
author2_role author
author
author
author
dc.subject.none.fl_str_mv Acth
Tyrosine Phosphatase
Pka
Phosphorylation
topic Acth
Tyrosine Phosphatase
Pka
Phosphorylation
purl_subject.fl_str_mv https://purl.org/becyt/ford/3.1
https://purl.org/becyt/ford/3
dc.description.none.fl_txt_mv 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.
Fil: Paz, Cristina del Valle. Universidad de Buenos Aires. Facultad de Medicina. Departamento de Bioquímica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Cornejo Maciel, Maria Fabiana. Universidad de Buenos Aires. Facultad de Medicina. Departamento de Bioquímica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Poderoso, Cecilia. Universidad de Buenos Aires. Facultad de Medicina. Departamento de Bioquímica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Gorostizaga, Alejandra Beatriz. Universidad de Buenos Aires. Facultad de Medicina. Departamento de Bioquímica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Podesta, Ernesto Jorge. Universidad de Buenos Aires. Facultad de Medicina. Departamento de Bioquímica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
description 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.
publishDate 2000
dc.date.none.fl_str_mv 2000-11
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/39236
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
url http://hdl.handle.net/11336/39236
identifier_str_mv 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
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.3109/07435800009048579
info:eu-repo/semantics/altIdentifier/url/https://www.tandfonline.com/doi/abs/10.3109/07435800009048579
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Taylor
publisher.none.fl_str_mv Taylor
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
_version_ 1842269196277252096
score 13.13397

Publicaciones similares