Obesity does not Lead to Imbalance Between Myocardial Phospholamban Phosphorylation and Dephosphorylation

Detalhes bibliográficos
Autor(a) principal: Freire,Paula Paccielli
Data de Publicação: 2014
Outros Autores: Alves,Carlos Augusto Barnabe, Deus,Adriana Fernandes de, Leopoldo,Ana Paula Lima, Leopoldo,André Soares, Silva,Danielle Cristina Tomaz da, Tomasi,Loreta Casquel de, Campos,Dijon Henrique Salomé, Cicogna,Antonio Carlos
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Arquivos Brasileiros de Cardiologia (Online)
Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0066-782X2014001900007
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 DephosphorylationObesityPhosphorylationRatsLeptinAdyposity 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. Sociedade Brasileira de Cardiologia - SBC2014-07-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0066-782X2014001900007Arquivos Brasileiros de Cardiologia v.103 n.1 2014reponame:Arquivos Brasileiros de Cardiologia (Online)instname:Sociedade Brasileira de Cardiologia (SBC)instacron:SBC10.5935/abc.20140083info:eu-repo/semantics/openAccessFreire,Paula PaccielliAlves,Carlos Augusto BarnabeDeus,Adriana Fernandes deLeopoldo,Ana Paula LimaLeopoldo,André SoaresSilva,Danielle Cristina Tomaz daTomasi,Loreta Casquel deCampos,Dijon Henrique SaloméCicogna,Antonio Carloseng2014-10-10T00:00:00Zoai:scielo:S0066-782X2014001900007Revistahttp://www.arquivosonline.com.br/https://old.scielo.br/oai/scielo-oai.php||arquivos@cardiol.br1678-41700066-782Xopendoar:2014-10-10T00:00Arquivos Brasileiros de Cardiologia (Online) - Sociedade Brasileira de Cardiologia (SBC)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
Obesity
Phosphorylation
Rats
Leptin
Adyposity
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
author_facet Freire,Paula Paccielli
Alves,Carlos Augusto Barnabe
Deus,Adriana Fernandes de
Leopoldo,Ana Paula Lima
Leopoldo,André Soares
Silva,Danielle Cristina Tomaz da
Tomasi,Loreta Casquel de
Campos,Dijon Henrique Salomé
Cicogna,Antonio Carlos
author_role author
author2 Alves,Carlos Augusto Barnabe
Deus,Adriana Fernandes de
Leopoldo,Ana Paula Lima
Leopoldo,André Soares
Silva,Danielle Cristina Tomaz da
Tomasi,Loreta Casquel de
Campos,Dijon Henrique Salomé
Cicogna,Antonio Carlos
author2_role author
author
author
author
author
author
author
author
dc.contributor.author.fl_str_mv Freire,Paula Paccielli
Alves,Carlos Augusto Barnabe
Deus,Adriana Fernandes de
Leopoldo,Ana Paula Lima
Leopoldo,André Soares
Silva,Danielle Cristina Tomaz da
Tomasi,Loreta Casquel de
Campos,Dijon Henrique Salomé
Cicogna,Antonio Carlos
dc.subject.por.fl_str_mv Obesity
Phosphorylation
Rats
Leptin
Adyposity
topic Obesity
Phosphorylation
Rats
Leptin
Adyposity
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 2014-07-01
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0066-782X2014001900007
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0066-782X2014001900007
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.5935/abc.20140083
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv text/html
dc.publisher.none.fl_str_mv Sociedade Brasileira de Cardiologia - SBC
publisher.none.fl_str_mv Sociedade Brasileira de Cardiologia - SBC
dc.source.none.fl_str_mv Arquivos Brasileiros de Cardiologia v.103 n.1 2014
reponame:Arquivos Brasileiros de Cardiologia (Online)
instname:Sociedade Brasileira de Cardiologia (SBC)
instacron:SBC
instname_str Sociedade Brasileira de Cardiologia (SBC)
instacron_str SBC
institution SBC
reponame_str Arquivos Brasileiros de Cardiologia (Online)
collection Arquivos Brasileiros de Cardiologia (Online)
repository.name.fl_str_mv Arquivos Brasileiros de Cardiologia (Online) - Sociedade Brasileira de Cardiologia (SBC)
repository.mail.fl_str_mv ||arquivos@cardiol.br
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