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  Modification of hippocampal synaptic proteins by nitric oxide-stimulated ADP ribosylation

Sullivan, B. M., Wong, S., & Schuman, E. M. (1997). Modification of hippocampal synaptic proteins by nitric oxide-stimulated ADP ribosylation. Learn Mem, 3(5), 414-24. doi:10.1101/lm.3.5.414.

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Sullivan, B. M., Author
Wong, S., Author
Schuman, Erin M.1, Author              
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1Synaptic Plasticity Department, Max Planck Institute for Brain Research, Max Planck Society, ou_2461710              

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Free keywords: Adenosine Diphosphate Ribose/*metabolism Animals Hippocampus/drug effects/*metabolism Male Molsidomine/analogs & derivatives/pharmacology Nerve Tissue Proteins/*metabolism Nitric Oxide/*pharmacology Nitric Oxide Donors/pharmacology Nitroprusside/pharmacology Rats Rats, Sprague-Dawley Subcellular Fractions/metabolism Synapses/drug effects/*metabolism Tissue Distribution/physiology
 Abstract: Nitric oxide has been shown to be an important neuronal signaling molecule that participates in both behavioral and synaptic plasticity. To better understand the potential mechanisms by which NO regulates synaptic function, the ability of NO to stimulate the modification of synaptic proteins by ADP ribosylation was examined. Two NO donors, sodium nitroprusside and 3-morpholinosydnonimine, stimulated the ADP ribosylation of proteins at apparent molecular masses of 42, 48, 51, 54, and 74 kD in hippocampal synaptosomes. This stimulation was likely owing to the production of NO by the donors; ADP ribosylation was not stimulated by non-NO decomposition products of sodium nitroprusside, and quenching of superoxide anion did not inhibit Sin-1-induced ADP ribosylation. Experiments using NAD+ that was radiolabeled on the nicotinamide moiety demonstrated that the modification of proteins of molecular masses of 30, 33, and 38 kD are not true ADP ribosylation, whereas labeling of the 42-, 48-, 51-, 54-, and 74-kD proteins likely represent ADP ribosylation. Some of the substrates were brain specific (54 and 74 kD), whereas others (42 and 51 kD) were present in multiple nonbrain tissues.

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 Dates: 1997-01-01
 Publication Status: Published in print
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 Identifiers: Other: 10456108
DOI: 10.1101/lm.3.5.414
ISSN: 1072-0502 (Print)1072-0502 (Linking)
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Title: Learn Mem
Source Genre: Journal
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Pages: - Volume / Issue: 3 (5) Sequence Number: - Start / End Page: 414 - 24 Identifier: -