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Modification of Cardiac Membrane GsĪ± by an Endogenous Arginine-Specific Mono-Adp-Ribosyltransferase

The mechanism by which nicotinamide adenine dinucleotide (NAD) stimulates the activity of adenylate cyclase (AC) in canine plasma membrane has been studied. Using [3 2P]-NAD, the activation by NAD was correlated with the radiolabeling of the stimulatory guanosine triphosphate (GTP) binding protein Gsa. Further characterization demonstrated that the modification occurred only in the presence of G-protein activators and that arginine residue(s) were modified by ADP-ribose by the action of a mono-ADP-ribosyltransferase. Inhibitors of the transferase blocked both the modification of Gsa and the activation of AC. Collectively, these studies suggest that ADP-ribosylation of Gsa by an endogenous mono-ADP-ribosyltransferase may regulate cardiac AC.

Identiferoai:union.ndltd.org:unt.edu/info:ark/67531/metadc332726
Date12 1900
CreatorsCoyle, Donna L. (Donna Lynn)
ContributorsJacobson, Myron K., Jacobson, Elaine L.
PublisherUniversity of North Texas
Source SetsUniversity of North Texas
LanguageEnglish
Detected LanguageEnglish
TypeThesis or Dissertation
Formatxiv, 136 leaves : ill., Text
RightsPublic, Coyle, Donna L. (Donna Lynn), Copyright, Copyright is held by the author, unless otherwise noted. All rights reserved.

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