This site is intended for healthcare professionals

Go to /sign-in page

You can view 5 more pages before signing in

Regulation

Last reviewed dd mmm yyyy. Last edited dd mmm yyyy

Authoring team

Glycogen phosphorylase is the key enzyme in glycogenolysis as it is rate-limiting; the remaining enzymes in the pathway are near equilibrium and non-saturated. Consequently, agents which alter glycogen phosphorylase activity alter the rate of glycogenolysis.

The agents are best considered in terms of site as there is slight variation:

  • the liver, where glycogenolysis is tailored to plasma blood glucose concentration:
    • hormones:
      • glucagon and adrenaline increase glycogenolysis
      • insulin decreases glycogenolysis
    • local factors:
    • the intracellular glucose concentration feedsback to inhibit glycogen phosphorylase, so providing fine-control over glycogenolysis
      • calcium increases glycogenolysis
      • low energy state within the cell increases glycogenolysis
  • in skeletal muscle:
    • hormones: as above, but glucagon has minimal effect
    • local factors: as above, but calcium release during muscular contraction has a more significant role in rapid activation of glycogen phosphorylase

Create an account to add page annotations

Annotations allow you to add information to this page that would be handy to have on hand during a consultation. E.g. a website or number. This information will always show when you visit this page.

The content herein is provided for informational purposes and does not replace the need to apply professional clinical judgement when diagnosing or treating any medical condition. A licensed medical practitioner should be consulted for diagnosis and treatment of any and all medical conditions.

Connect

Copyright 2024 Oxbridge Solutions Limited, a subsidiary of OmniaMed Communications Limited. All rights reserved. Any distribution or duplication of the information contained herein is strictly prohibited. Oxbridge Solutions receives funding from advertising but maintains editorial independence.