Obesity does not Lead to Imbalance Between Myocardial Phospholamban Phosphorylation and Dephosphorylation
Autor(a) principal: | |
---|---|
Data de Publicação: | 2014 |
Outros Autores: | , , , , , , , |
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. |
id |
SBC-1_f52af23ae0af1b2ef4595316a922d0b5 |
---|---|
oai_identifier_str |
oai:scielo:S0066-782X2014001900007 |
network_acronym_str |
SBC-1 |
network_name_str |
Arquivos Brasileiros de Cardiologia (Online) |
repository_id_str |
|
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 |
_version_ |
1752126564409016320 |