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

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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 … continued below

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xiv, 136 leaves : ill.

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Coyle, Donna L. (Donna Lynn) December 1993.

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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.

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xiv, 136 leaves : ill.

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Coyle, Donna L. (Donna Lynn). Modification of Cardiac Membrane Gsα by an Endogenous Arginine-Specific Mono-Adp-Ribosyltransferase, dissertation, December 1993; Denton, Texas. (https://digital.library.unt.edu/ark:/67531/metadc332726/: accessed May 26, 2024), University of North Texas Libraries, UNT Digital Library, https://digital.library.unt.edu; .

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