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PMID: 6954463 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Direct modification of the membrane adenylate cyclase system by islet-activating protein due to ADP-ribosylation of a membrane protein.

Katada T, Ui M

Abstract

GTP and isoproterenol activation of adenylate cyclase [ATP pyrophosphate-lyase (cyclizing), EC 4.6.1.1] in washed membranes prepared from C6 gliomas cells was enhanced by incubation with islet-activating protein, one of the pertussis toxins, if the incubation mixture was supplemented with NAD and ATP. The action of the protein was observed immediately after its addition and increased progressively in magnitude as the protein concentration or the incubation time increased. There was simultaneous incorporation of radioactivity from the ADP-ribose moiety of variously labeled NAD into the membrane protein with a molecular weight of 41,000. We conclude that islet-activating protein enhances receptor-mediated GTP-induced activation of membrane adenylate cyclase as a result of ADP-ribosylation of a membrane protein, probably one of the components of the receptor-adenylate cyclase system.

MeSH Terms
Adenosine Diphosphate Ribose/metabolism Adenosine Triphosphate/metabolism Adenylyl Cyclases/metabolism Animals Cell Line Cell-Free System Glioma Kinetics Membrane Proteins/metabolism NAD/metabolism Nucleoside Diphosphate Sugars/metabolism Rats
Chemicals
Membrane Proteins Nucleoside Diphosphate Sugars NAD Adenosine Diphosphate Ribose Adenosine Triphosphate Adenylyl Cyclases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Katada T
Ui M
References (18)
18 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1982-05-00
Pages
3129-33
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC346367
Subset
IM
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