Regulation of glycogen metabolism in cultured human muscles by the glycogen phosphorylase inhibitor CP-91149

dPharmacological inhibition of liver GP (glycogen phosphorylase), which is currently being studied as a treatment for Type II (noninsulin -dependent) diabetes, may affect muscle glycogen metabolism. In the present study, we analysed the effects of the GP inhibitor CP-91149 on non-engineered or GP-ov...

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Detalhes bibliográficos
Autores: Lerin C, Montell E, Nolasco T, García-Rocha M, Guinovart JJ, Gómez-Foix AM
Formato: artículo
Estado:Versión publicada
Fecha de publicación:2004
País:España
Recursos:Fundació Sant Joan de Déu
Repositorio:r-FSJD. Repositorio Institucional de Producción Científica de la Fundació Sant Joan de Déu
OAI Identifier:oai:fsjd.fundanetsuite.com:p6878
Acesso em linha:https://fsjd.fundanetsuite.com/Publicaciones/ProdCientif/PublicacionFrw.aspx?id=6878
Access Level:acceso abierto
Palavra-chave:glycogenolysis
glycogen phosphorylase
glycogen resynthesis
protein phosphatase 1
skeletal muscle
Descrição
Resumo:dPharmacological inhibition of liver GP (glycogen phosphorylase), which is currently being studied as a treatment for Type II (noninsulin -dependent) diabetes, may affect muscle glycogen metabolism. In the present study, we analysed the effects of the GP inhibitor CP-91149 on non-engineered or GP-overexpressing cultured human muscle cells. We found that CP-91149 treatment decreased muscle GP activity by (1) converting the phosphorylated AMP-independent a form into the dephosphorylated AMP-dependent b fonn and (2) inhibiting GP a activity and AMP-mediated GP b activation. Dephosphorylation of GP was exerted, irrespective of incubation of the cells with glucose, whereas inhibition of its activity was synergic with glucose. As expected, CP-91149 impaired the glycogenolysis induced by glucose deprivation. CP-91149 also promoted the dephosphorylation and activation of GS (glycogen synthase) in non-engineered or GP-overexpressing cultured human muscle cells, but exclusively in glucose-deprived cells. However, this inhibitor did not activate GS in glucose-deprived but glycogen-replete cells overexpressing PTG (protein targeting to glycogen), thus suggesting that glycogen inhibits the CP-91149-mediated activation of GS. Consistently, CP-91149 promoted glycogen resynthesis, but not its overaccumulation. Hence, treatment with CP-91149 impairs muscle glycogen breakdown, but enhances its recovery, which may be useful for the treatment of Type 11 (insulin-dependent) diabetes.