Skip Navigation

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by NAKAMURA, T.
Right arrow Articles by ICHIHARA, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by NAKAMURA, T.
Right arrow Articles by ICHIHARA, A.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

J. Biochem, 1984, Vol. 95, No. 6 1691-1696
© 1984 Japanese Biochemical Society


research-article

Glucagon and Glucose as Major Regulators of Glycogen Metabolism in Primary Cultured Rat Hepatocytes1

Toshikazu NAKAMURA, Satoshi KATO2 and Akira ICHIHARA

Institute for Enzyme Research, School of Medicine, University of Tokushima Tokushima, Tokushima 770

The short-term controls of glycogen synthase [EC 2.4.1.11 [EC] ] and glycogen phosphorylase [EC 2.4.1.1 [EC] ] by major regulators, such as insulin, glucose, catecholamine, and glucagon, were compared in a simple, yet organized experimental system, i.e., adult rat hepatocytes in primary culture. Glycogen synthase was activated by glucose markedly and dose-dependently (5–40 mM), but insulin alone (1 x 10–8 M) activated this enzyme only two-fold. Therefore, activation of the enzyme by the two regulators together was mostly due to activation by glucose. Glucagon at a concentration of 5 x 10–10 M suppressed this activation almost completely. Glucagon at this concentration activated phosphorylase considerably and this activation was slightly inhibited by insulin. Phenylephrine also activated phosphorylase, and this activation was inhibited by phenoxybenzamine or prazosin, suggesting that activation by catecholamine is through the {alpha}1-adrenergic receptor. Similarly a high concentration of glucose diminished the effects of glucagon and phenylephrine. These results suggest that in rat liver, glycogen metabolism is controlled mainly by glucagon, catecholamine, and glucose; the former two activate phosphorylase and inactivate synthase, while glucose activates synthase strongly and inactivates phosphorylase partially. Insulin plays a minor role in both reactions. Thus, the liver is primarily an organ for glucose production, which is regulated by hormones, not for glycogen storage, which is increased only by a high glucose concentration in the portal blood.

1This work was supported by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan.

2Present address: Research Laboratories, Otsuka Pharmaceutical Co., Ltd., Kawauchi, Tokushima, Tokushima 771-01.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?




Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.