The Molecular Mechanism by Which Insulin Activates Glycogen Synthase in Mammalian Skeletal Muscle View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

1985

AUTHORS

Philip Cohen , Peter J. Parker , James R. Woodgett

ABSTRACT

One of the important metabolic effects of insulin is its ability to stimulate the synthesis of glycogen in skeletal muscle within minutes; much research has been directed toward understanding the molecular basis of this effect. Almost 25 years ago, Joseph Larner and co-workers showed that glycogen synthase, the rate-limiting enzyme in this pathway, could exist in at least two forms. One possessed little activity in the absence of glucose 6-phosphate (G6P), while the other was almost fully active in the absence of G6P.(1) Incubation of rat hemidiaphragms with insulin decreased the proportion of glycogen synthase in the G6P-dependent form which paralleled the increased rate of glycogen production.(1–3) Furthermore, the conversion of glycogen synthase to a G6Pindependent form was still observed when glucose was omitted from the perfusion medium,(2,3) indicating that it was not a consequence of the increased rate of transport of glucose into muscle, which is also stimulated by insulin. Conversely, incubation of the hemidiaphragms with epinephrine increased the proportion of the G6P-dependent form and decreased the rate of glycogen synthesis.(2,3) More... »

PAGES

213-233

References to SciGraph publications

Book

TITLE

Molecular Basis of Insulin Action

ISBN

978-1-4684-4876-4
978-1-4684-4874-0

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-1-4684-4874-0_13

DOI

http://dx.doi.org/10.1007/978-1-4684-4874-0_13

DIMENSIONS

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