Kinectics of Na+, K+-ATPase inhibition by calcitonin and neurotensin

Autores
López Ordieres, María Graciela; Rodriguez, Georgina Emma
Año de publicación
2014
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The kinetics of interactions between the peptides calcitonin or neurotensin, and synaptosomal membrane Na+, K+-ATPase activity was characterized in this study. Calcitonin is a 32-amino acid peptide produced by the thyroid gland, whose main role is to prevent bone resorption. Calcitonin produced a non-competitive type of inhibition at varied potassium concentrations whereas in the presence of sodium and ATP, calcitonin produced an uncompetitive and competitive type of inhibition, respectively. Neurotensin is a basic tridecapeptide which also inhibits Na+, K+-ATPase activity. Therefore, in the presence of higher sodium concentrations the peptide produced a competitive interaction and it produced a non-competitive type of inhibition at varied potassium and ATP concentrations. In summary, calcitonin and neutotensin behave as enzyme inhibitors but, each one leads to a characteristic type of enzyme inhibition at varied substrate concentrations due to differences in peptide structure and functionality that could be influencing the kinetics of substrate interactions.
Fil: López Ordieres, María Graciela. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Biología Celular y Neurociencia "Prof. Eduardo de Robertis". Universidad de Buenos Aires. Facultad de Medicina. Instituto de Biología Celular y Neurociencia; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Farmacología. Cátedra de Farmacología; Argentina
Fil: Rodriguez, Georgina Emma. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Biología Celular y Neurociencia "Prof. Eduardo de Robertis". Universidad de Buenos Aires. Facultad de Medicina. Instituto de Biología Celular y Neurociencia; Argentina
Materia
Calcitonin
Neurotensin
Atpase
Inhibition
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:11336/17157
Acceder
id CONICETDig_c6119e437ad5a44df091c9572d30831a
oai_identifier_str oai:ri.conicet.gov.ar:11336/17157
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Kinectics of Na+, K+-ATPase inhibition by calcitonin and neurotensinLópez Ordieres, María GracielaRodriguez, Georgina EmmaCalcitoninNeurotensinAtpaseInhibitionhttps://purl.org/becyt/ford/3.1https://purl.org/becyt/ford/3The kinetics of interactions between the peptides calcitonin or neurotensin, and synaptosomal membrane Na+, K+-ATPase activity was characterized in this study. Calcitonin is a 32-amino acid peptide produced by the thyroid gland, whose main role is to prevent bone resorption. Calcitonin produced a non-competitive type of inhibition at varied potassium concentrations whereas in the presence of sodium and ATP, calcitonin produced an uncompetitive and competitive type of inhibition, respectively. Neurotensin is a basic tridecapeptide which also inhibits Na+, K+-ATPase activity. Therefore, in the presence of higher sodium concentrations the peptide produced a competitive interaction and it produced a non-competitive type of inhibition at varied potassium and ATP concentrations. In summary, calcitonin and neutotensin behave as enzyme inhibitors but, each one leads to a characteristic type of enzyme inhibition at varied substrate concentrations due to differences in peptide structure and functionality that could be influencing the kinetics of substrate interactions.Fil: López Ordieres, María Graciela. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Biología Celular y Neurociencia "Prof. Eduardo de Robertis". Universidad de Buenos Aires. Facultad de Medicina. Instituto de Biología Celular y Neurociencia; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Farmacología. Cátedra de Farmacología; ArgentinaFil: Rodriguez, Georgina Emma. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Biología Celular y Neurociencia "Prof. Eduardo de Robertis". Universidad de Buenos Aires. Facultad de Medicina. Instituto de Biología Celular y Neurociencia; ArgentinaResearch Trends2014-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/vnd.openxmlformats-officedocument.wordprocessingml.documentapplication/pdfhttp://hdl.handle.net/11336/17157López Ordieres, María Graciela; Rodriguez, Georgina Emma; Kinectics of Na+, K+-ATPase inhibition by calcitonin and neurotensin; Research Trends; Current Topics in Peptide & Protein Research; 15; 1-2014; 63-700972-4524enginfo:eu-repo/semantics/altIdentifier/url/http://www.researchtrends.net/tia/abstract.asp?in=0&vn=15&tid=26&aid=5651&pub=2014&type=3info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:45:38Zoai:ri.conicet.gov.ar:11336/17157instacron: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:34982025-09-29 09:45:39.194CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Kinectics of Na+, K+-ATPase inhibition by calcitonin and neurotensin
title Kinectics of Na+, K+-ATPase inhibition by calcitonin and neurotensin
spellingShingle Kinectics of Na+, K+-ATPase inhibition by calcitonin and neurotensin
López Ordieres, María Graciela
Calcitonin
Neurotensin
Atpase
Inhibition
title_short Kinectics of Na+, K+-ATPase inhibition by calcitonin and neurotensin
title_full Kinectics of Na+, K+-ATPase inhibition by calcitonin and neurotensin
title_fullStr Kinectics of Na+, K+-ATPase inhibition by calcitonin and neurotensin
title_full_unstemmed Kinectics of Na+, K+-ATPase inhibition by calcitonin and neurotensin
title_sort Kinectics of Na+, K+-ATPase inhibition by calcitonin and neurotensin
dc.creator.none.fl_str_mv López Ordieres, María Graciela
Rodriguez, Georgina Emma
author López Ordieres, María Graciela
author_facet López Ordieres, María Graciela
Rodriguez, Georgina Emma
author_role author
author2 Rodriguez, Georgina Emma
author2_role author
dc.subject.none.fl_str_mv Calcitonin
Neurotensin
Atpase
Inhibition
topic Calcitonin
Neurotensin
Atpase
Inhibition
purl_subject.fl_str_mv https://purl.org/becyt/ford/3.1
https://purl.org/becyt/ford/3
dc.description.none.fl_txt_mv The kinetics of interactions between the peptides calcitonin or neurotensin, and synaptosomal membrane Na+, K+-ATPase activity was characterized in this study. Calcitonin is a 32-amino acid peptide produced by the thyroid gland, whose main role is to prevent bone resorption. Calcitonin produced a non-competitive type of inhibition at varied potassium concentrations whereas in the presence of sodium and ATP, calcitonin produced an uncompetitive and competitive type of inhibition, respectively. Neurotensin is a basic tridecapeptide which also inhibits Na+, K+-ATPase activity. Therefore, in the presence of higher sodium concentrations the peptide produced a competitive interaction and it produced a non-competitive type of inhibition at varied potassium and ATP concentrations. In summary, calcitonin and neutotensin behave as enzyme inhibitors but, each one leads to a characteristic type of enzyme inhibition at varied substrate concentrations due to differences in peptide structure and functionality that could be influencing the kinetics of substrate interactions.
Fil: López Ordieres, María Graciela. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Biología Celular y Neurociencia "Prof. Eduardo de Robertis". Universidad de Buenos Aires. Facultad de Medicina. Instituto de Biología Celular y Neurociencia; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Farmacología. Cátedra de Farmacología; Argentina
Fil: Rodriguez, Georgina Emma. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Biología Celular y Neurociencia "Prof. Eduardo de Robertis". Universidad de Buenos Aires. Facultad de Medicina. Instituto de Biología Celular y Neurociencia; Argentina
description The kinetics of interactions between the peptides calcitonin or neurotensin, and synaptosomal membrane Na+, K+-ATPase activity was characterized in this study. Calcitonin is a 32-amino acid peptide produced by the thyroid gland, whose main role is to prevent bone resorption. Calcitonin produced a non-competitive type of inhibition at varied potassium concentrations whereas in the presence of sodium and ATP, calcitonin produced an uncompetitive and competitive type of inhibition, respectively. Neurotensin is a basic tridecapeptide which also inhibits Na+, K+-ATPase activity. Therefore, in the presence of higher sodium concentrations the peptide produced a competitive interaction and it produced a non-competitive type of inhibition at varied potassium and ATP concentrations. In summary, calcitonin and neutotensin behave as enzyme inhibitors but, each one leads to a characteristic type of enzyme inhibition at varied substrate concentrations due to differences in peptide structure and functionality that could be influencing the kinetics of substrate interactions.
publishDate 2014
dc.date.none.fl_str_mv 2014-01
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/11336/17157
López Ordieres, María Graciela; Rodriguez, Georgina Emma; Kinectics of Na+, K+-ATPase inhibition by calcitonin and neurotensin; Research Trends; Current Topics in Peptide & Protein Research; 15; 1-2014; 63-70
0972-4524
url http://hdl.handle.net/11336/17157
identifier_str_mv López Ordieres, María Graciela; Rodriguez, Georgina Emma; Kinectics of Na+, K+-ATPase inhibition by calcitonin and neurotensin; Research Trends; Current Topics in Peptide & Protein Research; 15; 1-2014; 63-70
0972-4524
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.researchtrends.net/tia/abstract.asp?in=0&vn=15&tid=26&aid=5651&pub=2014&type=3
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/vnd.openxmlformats-officedocument.wordprocessingml.document
application/pdf
dc.publisher.none.fl_str_mv Research Trends
publisher.none.fl_str_mv Research Trends
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_ 1844613429454700544
score 13.069144

Publicaciones similares