Conversion of adrenergic mechanism from an alpha- to a beta-type during primary culture of rat hepatocytes. Accompanying decreases in the function of the inhibitory guanine nucleotide regulatory component of adenylate cyclase identified as the substrate of islet-activating protein.-Reference-Cited by-同舟云学术

Conversion of adrenergic mechanism from an alpha- to a beta-type during primary culture of rat hepatocytes. Accompanying decreases in the function of the inhibitory guanine nucleotide regulatory component of adenylate cyclase identified as the substrate of islet-activating protein.

Published:1984-12 Issue:24 Volume:259 Page:15464-15473
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Itoh H,Okajima F,Ui M

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference69 articles.

1. Characterization with [3H] dihydroergocryptine of the alpha-adrenergic receptor of the hepatic plasma membrane. Comparison with the beta-adrenergic receptor in normal and adrenalectomized rats

2. beta-Adrenergic receptors in rabbit liver plasma membranes. Predominance of beta 2-receptors and mediation of adrenergic regulation of hepatic glycogenolysis.

3. Differences between male and female rats in the regulation of hepatic glycogenolysis. The relative role of calcium and cAMP in phosphorylase activation by catecholamines.

4. Adrenergic control of glucose output and adenosine 3‘:5‘-monophosphate levels in hepatocytes from juvenile and adult rats.

5. Hormonal activation of glycogen phosphorylase in hepatocytes from hypothyroid rats.

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