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: | 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. |
id |
UNSP_c3ebc14e050b557bb5fc4933f084d394 |
---|---|
oai_identifier_str |
oai:repositorio.unesp.br:11449/227849 |
network_acronym_str |
UNSP |
network_name_str |
Repositório Institucional da UNESP |
repository_id_str |
2946 |
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 |
|
_version_ |
1808128155477606400 |