Effects of insulin and actin on phosphofructokinase activity and cellular distribution in skeletal muscle
Autor(a) principal: | |
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Data de Publicação: | 2004 |
Outros Autores: | , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Anais da Academia Brasileira de Ciências (Online) |
Texto Completo: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652004000300008 |
Resumo: | In this work, we report evidences that the association of phosphofructokinase and F-actin can be affected by insulin stimulation in rabbit skeletal muscle homogenates and that this association can be a mechanism of phos-phofructokinase regulation. Through co-sedimentation techniques, we observed that on insulin-stimulated tissues, approximately 70% of phosphofructokinase activity is co-located in an actin-enriched fraction, against 28% in control. This phenomenon is accompanied by a 100% increase in specific phosphofructokinase activity in stimulated homogenates. Purified F-actin causes an increase of 230% in phosphofructokinase activity and alters its kinetic parameters. The presence of F-actin increases the affinity of phosphofructokinase for fructose 6-phosphate nevertheless, with no changes in maximum velocity (Vmax). Here we propose that the modulation of cellular distribution of phosphofructokinase may be one of the mechanisms of control of glycolytic flux in mammalian muscle by insulin. |
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Anais da Academia Brasileira de Ciências (Online) |
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Effects of insulin and actin on phosphofructokinase activity and cellular distribution in skeletal musclephosphofructokinasehormonerabbitactinmetabolismglycolysisIn this work, we report evidences that the association of phosphofructokinase and F-actin can be affected by insulin stimulation in rabbit skeletal muscle homogenates and that this association can be a mechanism of phos-phofructokinase regulation. Through co-sedimentation techniques, we observed that on insulin-stimulated tissues, approximately 70% of phosphofructokinase activity is co-located in an actin-enriched fraction, against 28% in control. This phenomenon is accompanied by a 100% increase in specific phosphofructokinase activity in stimulated homogenates. Purified F-actin causes an increase of 230% in phosphofructokinase activity and alters its kinetic parameters. The presence of F-actin increases the affinity of phosphofructokinase for fructose 6-phosphate nevertheless, with no changes in maximum velocity (Vmax). Here we propose that the modulation of cellular distribution of phosphofructokinase may be one of the mechanisms of control of glycolytic flux in mammalian muscle by insulin.Academia Brasileira de Ciências2004-09-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652004000300008Anais da Academia Brasileira de Ciências v.76 n.3 2004reponame:Anais da Academia Brasileira de Ciências (Online)instname:Academia Brasileira de Ciências (ABC)instacron:ABC10.1590/S0001-37652004000300008info:eu-repo/semantics/openAccessSilva,Ana Paula P.Alves,Gutemberg G.Araújo,Alexandre H.B.Sola-Penna,Mauroeng2004-08-20T00:00:00Zoai:scielo:S0001-37652004000300008Revistahttp://www.scielo.br/aabchttps://old.scielo.br/oai/scielo-oai.php||aabc@abc.org.br1678-26900001-3765opendoar:2004-08-20T00:00Anais da Academia Brasileira de Ciências (Online) - Academia Brasileira de Ciências (ABC)false |
dc.title.none.fl_str_mv |
Effects of insulin and actin on phosphofructokinase activity and cellular distribution in skeletal muscle |
title |
Effects of insulin and actin on phosphofructokinase activity and cellular distribution in skeletal muscle |
spellingShingle |
Effects of insulin and actin on phosphofructokinase activity and cellular distribution in skeletal muscle Silva,Ana Paula P. phosphofructokinase hormone rabbit actin metabolism glycolysis |
title_short |
Effects of insulin and actin on phosphofructokinase activity and cellular distribution in skeletal muscle |
title_full |
Effects of insulin and actin on phosphofructokinase activity and cellular distribution in skeletal muscle |
title_fullStr |
Effects of insulin and actin on phosphofructokinase activity and cellular distribution in skeletal muscle |
title_full_unstemmed |
Effects of insulin and actin on phosphofructokinase activity and cellular distribution in skeletal muscle |
title_sort |
Effects of insulin and actin on phosphofructokinase activity and cellular distribution in skeletal muscle |
author |
Silva,Ana Paula P. |
author_facet |
Silva,Ana Paula P. Alves,Gutemberg G. Araújo,Alexandre H.B. Sola-Penna,Mauro |
author_role |
author |
author2 |
Alves,Gutemberg G. Araújo,Alexandre H.B. Sola-Penna,Mauro |
author2_role |
author author author |
dc.contributor.author.fl_str_mv |
Silva,Ana Paula P. Alves,Gutemberg G. Araújo,Alexandre H.B. Sola-Penna,Mauro |
dc.subject.por.fl_str_mv |
phosphofructokinase hormone rabbit actin metabolism glycolysis |
topic |
phosphofructokinase hormone rabbit actin metabolism glycolysis |
description |
In this work, we report evidences that the association of phosphofructokinase and F-actin can be affected by insulin stimulation in rabbit skeletal muscle homogenates and that this association can be a mechanism of phos-phofructokinase regulation. Through co-sedimentation techniques, we observed that on insulin-stimulated tissues, approximately 70% of phosphofructokinase activity is co-located in an actin-enriched fraction, against 28% in control. This phenomenon is accompanied by a 100% increase in specific phosphofructokinase activity in stimulated homogenates. Purified F-actin causes an increase of 230% in phosphofructokinase activity and alters its kinetic parameters. The presence of F-actin increases the affinity of phosphofructokinase for fructose 6-phosphate nevertheless, with no changes in maximum velocity (Vmax). Here we propose that the modulation of cellular distribution of phosphofructokinase may be one of the mechanisms of control of glycolytic flux in mammalian muscle by insulin. |
publishDate |
2004 |
dc.date.none.fl_str_mv |
2004-09-01 |
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=S0001-37652004000300008 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652004000300008 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/S0001-37652004000300008 |
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 |
Academia Brasileira de Ciências |
publisher.none.fl_str_mv |
Academia Brasileira de Ciências |
dc.source.none.fl_str_mv |
Anais da Academia Brasileira de Ciências v.76 n.3 2004 reponame:Anais da Academia Brasileira de Ciências (Online) instname:Academia Brasileira de Ciências (ABC) instacron:ABC |
instname_str |
Academia Brasileira de Ciências (ABC) |
instacron_str |
ABC |
institution |
ABC |
reponame_str |
Anais da Academia Brasileira de Ciências (Online) |
collection |
Anais da Academia Brasileira de Ciências (Online) |
repository.name.fl_str_mv |
Anais da Academia Brasileira de Ciências (Online) - Academia Brasileira de Ciências (ABC) |
repository.mail.fl_str_mv |
||aabc@abc.org.br |
_version_ |
1754302856155889664 |