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.
| Identifer | oai:union.ndltd.org:unt.edu/info:ark/67531/metadc332726 |
| Date | 12 1900 |
| Creators | Coyle, Donna L. (Donna Lynn) |
| Contributors | Jacobson, Myron K., Jacobson, Elaine L. |
| Publisher | University of North Texas |
| Source Sets | University of North Texas |
| Language | English |
| Detected Language | English |
| Type | Thesis or Dissertation |
| Format | xiv, 136 leaves : ill., Text |
| Rights | Public, Coyle, Donna L. (Donna Lynn), Copyright, Copyright is held by the author, unless otherwise noted. All rights reserved. |
Page generated in 0.0053 seconds