Project: Research project

Project Details


Glycogen metabolism is under the control of several hormones, including insulin
and catecholamines, and covalent phosphorylation of certain key enzymes is
thought to be involved in such regulation. Glycogen synthase in vitro is
subject to a particularly intricate interconversion, undergoing phosphorylation
at several distinct sites through the action of at least four different types of
protein kinase: (1) cAMP-dependent protein kinases, (2) phosphorylation kinase,
(3) PC 0.4/PC 0.5 and (4) PC 0.7. One emphasis of the proposal is the continued
characterization of this interconversion in vitro seeking to relate the action
of a given kinase with phosphorylation of specific sites. In addition, the
further purification and characterization of the PC 0.4/PC 0.5 and PC 0.7
protein kinases will be undertaken. A second emphasis will be an attempt to
evaluate how far the conversion studied in vitro is functional in intact muscle. One important question is of the role of Ca2 ion in regulating glycogen
synthase activity. Insofaras hormone action is mediated by the action of
protein kinases, knowledge of the specificities of the different kinases in
vitro should identify which kinase(s) is a candidate to mediate different
hormonal and other treatments.
Effective start/end date11/1/796/30/87


  • National Institutes of Health


  • Medicine(all)

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