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Thyrotropin Stimulation of the ADP-Ribosyltransferase Activity of Bovine Thyroid Membranes

Thyrotropin increases the ADP-ribosylation activity of bovine thyroid membranes. Rapid ADP-ribosylation of membrane components is followed by increasing ADP-ribosylation of components in the supernatant of the reaction mixture. One of the major membrane proteins ADP-ribosylated in the thyrotropin-st...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1982-03, Vol.79 (5), p.1525-1529
Main Authors: Vitti, Paolo, Marc J. S. De Wolf, Acquaviva, Angela M., Epstein, Michael, Kohn, Leonard D.
Format: Article
Language:English
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Summary:Thyrotropin increases the ADP-ribosylation activity of bovine thyroid membranes. Rapid ADP-ribosylation of membrane components is followed by increasing ADP-ribosylation of components in the supernatant of the reaction mixture. One of the major membrane proteins ADP-ribosylated in the thyrotropin-stimulated reaction has an approximate molecular weight of 40,000; this same protein is also a major ADP-ribosylated product of the A protomer of cholera toxin and appears to be related to the G regulatory subunit of the adenylate cyclase complex. The ADP-ribosylated products appearing in the supernatant solution comigrate with thyrotropin and preparations of125I-labeled α subunit of thyrotropin; the α subunit, but not the β subunit, of thyrotropin can be ADP-ribosylated by the membrane ADP-ribosyltransferase activity. NAD can be shown to enhance the ability of thyrotropin to stimulate the adenylate cyclase activity of bovine thyroid membrane preparations and of membrane preparations of a rat thyroid tumor whose adenylate cyclase activity is otherwise unresponsive to thyrotropin. The β subunit of thyrotropin inhibits thyrotropin stimulation of both the ADP-ribosylation and adenylate cyclase activities of the thyroid membrane.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.79.5.1525