Obesity does not lead to imbalance between myocardial phospholamban phosphorylation and dephosphorylation

Detalhes bibliográficos
Autor(a) principal: Freire, Paula Paccielli [UNESP]
Data de Publicação: 2014
Outros Autores: Alves, Carlos Augusto Barnabe [UNESP], de Deus, Adriana Fernandes [UNESP], Leopoldo, Ana Paula Lima, Leopoldo, André Soares, da Silva, Danielle Cristina Tomaz [UNESP], de Tomasi, Loreta Casquel [UNESP], Campos, Dijon Henrique Salomé [UNESP], Cicogna, Antonio Carlos [UNESP]
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://dx.doi.org/10.5935/abc.20140083
http://hdl.handle.net/11449/227849
Resumo: Background: The activation of the beta-adrenergic system promotes G protein stimulation that, via cyclic adenosine monophosphate (cAMP), alters the structure of protein kinase A (PKA) and leads to phospholamban (PLB) phosphorylation. This protein participates in the system that controls intracellular calcium in muscle cells, and it is the primary regulator of sarcoplasmic reticulum calcium pump activity. In obesity, the beta-adrenergic system is activated by the influence of increased leptin, therefore, resulting in higher myocardial phospholamban phosphorylation via cAMP-PKA. Objective: To investigate the involvement of proteins which regulate the degree of PLB phosphorylation due to beta-adrenergic activation in obesity. In the present study, we hypothesized that there is an imbalance between phospholamban phosphorylation and dephosphorylation, with prevalence of protein phosphorylation. Methods: Male Wistar rats were randomly distributed into two groups: control (n = 14), fed with normocaloric diet; and obese (n = 13), fed with a cycle of four unsaturated high-fat diets. Obesity was determined by the adiposity index, and protein expressions of phosphatase 1 (PP-1), PKA, PLB, phosphorylated phospholamban at serine16 (PPLB-Ser16) were assessed by Western blot. Results: Obesity caused glucose intolerance, hyperinsulinemia, hypertriglyceridemia, hyperleptinemia and did not alter the protein expression of PKA, PP-1, PLB, PPLB-Ser16. Conclusion: Obesity does not promote an imbalance between myocardial PLB phosphorylation and dephosphorylation via beta-adrenergic system.
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spelling Obesity does not lead to imbalance between myocardial phospholamban phosphorylation and dephosphorylationAdyposityLeptinObesityPhosphorylationRatsBackground: The activation of the beta-adrenergic system promotes G protein stimulation that, via cyclic adenosine monophosphate (cAMP), alters the structure of protein kinase A (PKA) and leads to phospholamban (PLB) phosphorylation. This protein participates in the system that controls intracellular calcium in muscle cells, and it is the primary regulator of sarcoplasmic reticulum calcium pump activity. In obesity, the beta-adrenergic system is activated by the influence of increased leptin, therefore, resulting in higher myocardial phospholamban phosphorylation via cAMP-PKA. Objective: To investigate the involvement of proteins which regulate the degree of PLB phosphorylation due to beta-adrenergic activation in obesity. In the present study, we hypothesized that there is an imbalance between phospholamban phosphorylation and dephosphorylation, with prevalence of protein phosphorylation. Methods: Male Wistar rats were randomly distributed into two groups: control (n = 14), fed with normocaloric diet; and obese (n = 13), fed with a cycle of four unsaturated high-fat diets. Obesity was determined by the adiposity index, and protein expressions of phosphatase 1 (PP-1), PKA, PLB, phosphorylated phospholamban at serine16 (PPLB-Ser16) were assessed by Western blot. Results: Obesity caused glucose intolerance, hyperinsulinemia, hypertriglyceridemia, hyperleptinemia and did not alter the protein expression of PKA, PP-1, PLB, PPLB-Ser16. Conclusion: Obesity does not promote an imbalance between myocardial PLB phosphorylation and dephosphorylation via beta-adrenergic system.Departamento de Clínica Médica, Universidade Estadual Paulista, Botucatu, SP Vitória, ESCentro de Educação Física e Desportos, Universidade Federal do Espírito Santo, Vitória, ESDepartamento de Clínica Médica, Universidade Estadual Paulista, Botucatu, SP Vitória, ESUniversidade Estadual Paulista (UNESP)Universidade Federal do Espírito Santo (UFES)Freire, Paula Paccielli [UNESP]Alves, Carlos Augusto Barnabe [UNESP]de Deus, Adriana Fernandes [UNESP]Leopoldo, Ana Paula LimaLeopoldo, André Soaresda Silva, Danielle Cristina Tomaz [UNESP]de Tomasi, Loreta Casquel [UNESP]Campos, Dijon Henrique Salomé [UNESP]Cicogna, Antonio Carlos [UNESP]2022-04-29T07:20:26Z2022-04-29T07:20:26Z2014-01-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article41-50http://dx.doi.org/10.5935/abc.20140083Arquivos Brasileiros de Cardiologia, v. 103, n. 1, p. 41-50, 2014.1678-41700066-782Xhttp://hdl.handle.net/11449/22784910.5935/abc.201400832-s2.0-84906057991Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengArquivos Brasileiros de Cardiologiainfo:eu-repo/semantics/openAccess2024-08-14T17:23:20Zoai:repositorio.unesp.br:11449/227849Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-14T17:23:20Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Obesity does not lead to imbalance between myocardial phospholamban phosphorylation and dephosphorylation
title Obesity does not lead to imbalance between myocardial phospholamban phosphorylation and dephosphorylation
spellingShingle Obesity does not lead to imbalance between myocardial phospholamban phosphorylation and dephosphorylation
Freire, Paula Paccielli [UNESP]
Adyposity
Leptin
Obesity
Phosphorylation
Rats
title_short Obesity does not lead to imbalance between myocardial phospholamban phosphorylation and dephosphorylation
title_full Obesity does not lead to imbalance between myocardial phospholamban phosphorylation and dephosphorylation
title_fullStr Obesity does not lead to imbalance between myocardial phospholamban phosphorylation and dephosphorylation
title_full_unstemmed Obesity does not lead to imbalance between myocardial phospholamban phosphorylation and dephosphorylation
title_sort Obesity does not lead to imbalance between myocardial phospholamban phosphorylation and dephosphorylation
author Freire, Paula Paccielli [UNESP]
author_facet Freire, Paula Paccielli [UNESP]
Alves, Carlos Augusto Barnabe [UNESP]
de Deus, Adriana Fernandes [UNESP]
Leopoldo, Ana Paula Lima
Leopoldo, André Soares
da Silva, Danielle Cristina Tomaz [UNESP]
de Tomasi, Loreta Casquel [UNESP]
Campos, Dijon Henrique Salomé [UNESP]
Cicogna, Antonio Carlos [UNESP]
author_role author
author2 Alves, Carlos Augusto Barnabe [UNESP]
de Deus, Adriana Fernandes [UNESP]
Leopoldo, Ana Paula Lima
Leopoldo, André Soares
da Silva, Danielle Cristina Tomaz [UNESP]
de Tomasi, Loreta Casquel [UNESP]
Campos, Dijon Henrique Salomé [UNESP]
Cicogna, Antonio Carlos [UNESP]
author2_role author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Universidade Estadual Paulista (UNESP)
Universidade Federal do Espírito Santo (UFES)
dc.contributor.author.fl_str_mv Freire, Paula Paccielli [UNESP]
Alves, Carlos Augusto Barnabe [UNESP]
de Deus, Adriana Fernandes [UNESP]
Leopoldo, Ana Paula Lima
Leopoldo, André Soares
da Silva, Danielle Cristina Tomaz [UNESP]
de Tomasi, Loreta Casquel [UNESP]
Campos, Dijon Henrique Salomé [UNESP]
Cicogna, Antonio Carlos [UNESP]
dc.subject.por.fl_str_mv Adyposity
Leptin
Obesity
Phosphorylation
Rats
topic Adyposity
Leptin
Obesity
Phosphorylation
Rats
description Background: The activation of the beta-adrenergic system promotes G protein stimulation that, via cyclic adenosine monophosphate (cAMP), alters the structure of protein kinase A (PKA) and leads to phospholamban (PLB) phosphorylation. This protein participates in the system that controls intracellular calcium in muscle cells, and it is the primary regulator of sarcoplasmic reticulum calcium pump activity. In obesity, the beta-adrenergic system is activated by the influence of increased leptin, therefore, resulting in higher myocardial phospholamban phosphorylation via cAMP-PKA. Objective: To investigate the involvement of proteins which regulate the degree of PLB phosphorylation due to beta-adrenergic activation in obesity. In the present study, we hypothesized that there is an imbalance between phospholamban phosphorylation and dephosphorylation, with prevalence of protein phosphorylation. Methods: Male Wistar rats were randomly distributed into two groups: control (n = 14), fed with normocaloric diet; and obese (n = 13), fed with a cycle of four unsaturated high-fat diets. Obesity was determined by the adiposity index, and protein expressions of phosphatase 1 (PP-1), PKA, PLB, phosphorylated phospholamban at serine16 (PPLB-Ser16) were assessed by Western blot. Results: Obesity caused glucose intolerance, hyperinsulinemia, hypertriglyceridemia, hyperleptinemia and did not alter the protein expression of PKA, PP-1, PLB, PPLB-Ser16. Conclusion: Obesity does not promote an imbalance between myocardial PLB phosphorylation and dephosphorylation via beta-adrenergic system.
publishDate 2014
dc.date.none.fl_str_mv 2014-01-01
2022-04-29T07:20:26Z
2022-04-29T07:20:26Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://dx.doi.org/10.5935/abc.20140083
Arquivos Brasileiros de Cardiologia, v. 103, n. 1, p. 41-50, 2014.
1678-4170
0066-782X
http://hdl.handle.net/11449/227849
10.5935/abc.20140083
2-s2.0-84906057991
url http://dx.doi.org/10.5935/abc.20140083
http://hdl.handle.net/11449/227849
identifier_str_mv Arquivos Brasileiros de Cardiologia, v. 103, n. 1, p. 41-50, 2014.
1678-4170
0066-782X
10.5935/abc.20140083
2-s2.0-84906057991
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Arquivos Brasileiros de Cardiologia
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 41-50
dc.source.none.fl_str_mv Scopus
reponame:Repositório Institucional da UNESP
instname:Universidade Estadual Paulista (UNESP)
instacron:UNESP
instname_str Universidade Estadual Paulista (UNESP)
instacron_str UNESP
institution UNESP
reponame_str Repositório Institucional da UNESP
collection Repositório Institucional da UNESP
repository.name.fl_str_mv Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)
repository.mail.fl_str_mv
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