EurekaMag.com logo
+ Site Statistics
References:
53,869,633
Abstracts:
29,686,251
+ Search Articles
+ Subscribe to Site Feeds
EurekaMag Most Shared ContentMost Shared
EurekaMag PDF Full Text ContentPDF Full Text
+ PDF Full Text
Request PDF Full TextRequest PDF Full Text
+ Follow Us
Follow on FacebookFollow on Facebook
Follow on TwitterFollow on Twitter
Follow on LinkedInFollow on LinkedIn

+ Translate

Conversion of adrenergic mechanism from an alpha type 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



Conversion of adrenergic mechanism from an alpha type 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



Journal of Biological Chemistry 259(24): 15464-15473



Adrenergic mechanism for phosphorylase activation was gradually converted from an .alpha.1- to a .beta.2-type during primary culture of rat hepatocytes. .beta.2-Receptor-mediated cAMP generation was also much greater in 8-h cultured cells than in fresh cells. Incubation of hepatocyte membranes with [.alpha.-32P]NAD and the preactivated A-protomer (an active component) of islet-activating protein (IAP), pertussis toxin, resulted in the ADP-ribosylation of a specific IAP substrate protein (MW = 41,000). This ADP-ribosylation diminished progressively when the membrane-donor hepatocytes was cultured. The early diminution was interfered with by the addition of nicotinamide or isonicotinamide, a potent inhibitor of ADP ribosyltransferase, to the culture medium. The decrease of the IAP substrate was well correlated with the potentiation of .beta.-adrenergic functions under various conditions of culture. .beta.-Receptor-mediated activation of GTP-dependent membrane adenylate cyclase was, but glucagon-induced activation was not enhanced by either prior culture of hepatocytes or prior exposure of membranes to the A-protomer of IAP. There was no further enhancement, however, when membranes from cultured cells were exposed to the active toxin. The IAP-susceptible inhibitory guanine nucleotide-regulatory protein is coupled to .beta.-adrenergic receptors in such a manner as to reduce the degree of activation of cyclase, and the decrease in this IAP substrate may be responsible, at least partly, for development of .beta.-receptor functions during culture of hepatocytes. Its possible relation to accompanying inhibition of .alpha.1-receptor functions is discussed.

(PDF emailed within 1 workday: $29.90)

Accession: 005053360

Download citation: RISBibTeXText



Related references

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. Journal of Biological Chemistry 259(24): 15464-15473, 1984

Conversion of adrenergic mechanism from an a- to a b-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. The Journal of Biological Chemistry 259: 464-73, 1984

Loss of the inhibitory function of the guanine nucleotide regulatory component of adenylate cyclase due to its ADP ribosylation by islet-activating protein, pertussis toxin, in adipocyte membranes. Journal of Biological Chemistry 258(5): 3319-3326, 1983

Islet activating protein pertussis toxin a probe for functions of the inhibitory guanine nucleotide regulatory component of adenylate cyclase. Trends in Pharmacological Sciences 5(7): 277-279, 1984

ADP-ribosylation of the inhibitory guanine nucleotide regulatory protein (Ni) as a possible mechanism underlying development of beta-adrenergic responses during primary culture of rat hepatocytes. Advances in Cyclic Nucleotide and Protein Phosphorylation Research 19: 195-205, 1985

The inhibitory guanine nucleotide-binding regulatory component of adenylate cyclase. Subunit dissociation and the inhibition of adenylate cyclase in S49 lymphoma cyc- and wild type membranes. Journal of Biological Chemistry 259(6): 3586-3595, 1984

The inhibitory guanine nucleotide binding regulatory component of adenylate cyclase subunit dissociation and the inhibition of adenylate cyclase in s 49 lymphoma cyc minus and wild type membranes. Journal of Biological Chemistry 259(6): 3586-3595, 1984

Conversion of adrenergic mechanism from an alpha 1 type to a beta 2 type during primary culture of rat hepatocytes. Japanese Journal of Pharmacology 40(SUPPL): 17P-18P, 1986

The inhibitory guanine nucleotide-binding regulatory component of adenylate cyclase. Properties and function of the purified protein. Journal of Biological Chemistry 259(6): 3568-3577, 1984

Protein kinase C phosphorylates the inhibitory guanine-nucleotide-binding regulatory component and apparently suppresses its function in hormonal inhibition of adenylate cyclase. European Journal of Biochemistry 151(2): 431-437, 1985

Role of inhibitory guanine nucleotide binding regulatory proteins of adenylate cyclase in coupling angiotensin receptors to inhibition of adenylate cyclase in hepatocytes. Journal of Biological Chemistry 260(30): 16200-16209, 1985

The inhibitory guanine nucleotide-binding regulatory component of adenylate cyclase. Subunit dissociation and guanine nucleotide-dependent hormonal inhibition. Journal of Biological Chemistry 259(6): 3578-3585, 1984

Conversion of adrenergic regulation of glycogen phosphorylase and synthase from an alpha type to a beta type during primary culture of rat hepatocytes. Archives of Biochemistry & Biophysics 213(2): 658-668, 1982

Mechanisms for inhibition of the catalytic activity of adenylate cyclase by the guanine nucleotide-binding proteins serving as the substrate of islet-activating protein, pertussis toxin. Journal of Biological Chemistry 261(11): 5215-5221, 1986