Effects of insulin and actin on phosphofructokinase activity and cellular distribution in skeletal muscle

Anais da Academia Brasileira de Ciências

Ana Paula P. Silva²  Gutemberg G. Alves²  Alexandre H.b. Araújo¹  Mauro Sola-penna² 

[1] ,Universidade Federal do Rio de Janeiro Faculdade de Farmácia Departamento de FármacosRio de Janeiro,Brasil

关键词: phosphofructokinase;    hormone;    rabbit;    actin;    metabolism;    glycolysis;    fosfofrutocinase;    hormônio;    coelho;    actina;    metabolismo;    glicólise;   

DOI  :  10.1590/S0001-37652004000300008

来源: SciELO

【 摘 要 】

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.

【 授权许可】

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