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Nitric oxide-induced modification of glyceraldehyde-3-phosphate dehydrogenase with NAD+ is not ADP-ribosylation.

Nitric oxide-induced modification of glyceraldehyde-3-phosphate dehydrogenase with NAD+ is not ADP-ribosylation. Research Abstract Details 

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  • Nitric oxide-induced modification of glyceraldehyde-3-phosphate dehydrogenase with NAD+ is not ADP-ribosylation. Abstract Text:

    m itogaM Itoga,m tsuchiyaM Tsuchiya,h ishinoH Ishino,m shimoyamaM Shimoyama,

    One biological effect of nitric oxide (NO) has been believed to be exerted through induction of the ADP-ribosyltransferase activity of glyceraldehyde-3-phosphate dehydrogenase (GAPDH). Though this notion is based on the finding that NO increases the auto-ADP-ribosylation of GAPDH, controversial data have also been reported. To determine whether or not NO really activates ADP-ribosylation, we re-examined the NO-induced modification of GAPDH with NAD+. GAPDH was modified equally with [adenosine-14C]NAD+ and [carbonyl-14C]NAD+, indicating that the glycoside bond of NAD+ between ADP-ribose and nicotinamide is intact. The release of nicotinamide from NAD+ was not evident during incubation of GAPDH with [carbonyl-14C]NAD+. Thus, the modification of GAPDH is apparently not ADP-ribosylation. In addition, we found that basal and glyceraldehyde-3-phosphate-induced modifications of GAPDH, both of which have also been explained as ADP-ribosylation, were not ADP-ribosylation, and that the modification of GAPDH in the absence and presence of NO or GA3P was distinct in the dithiothreitol effect or resistance to HgCl2.

    Nitric oxide-induced modification of glyceraldehyde-3-phosphate dehydrogenase with NAD+ is not ADP-ribosylation. Publishing Authors By Initials

    m itogaM Itoga,m tsuchiyaM Tsuchiya,h ishinoH Ishino,m shimoyamaM Shimoyama,

    For similar inorganic chemicals: isotopes: phosphorus isotopes: phosphorus radioisotopes research abstracts see: inorganic chemicals: isotopes: phosphorus isotopes: phosphorus radioisotopes research

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    Nitric oxide-induced modification of glyceraldehyde-3-phosphate dehydrogenase with NAD+ is not ADP-ribosylation. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: Journal of biochemistry

    VOLUME: 121

    Page Numbers: 1041-6

    Journal Abbreviation: J. Biochem.

    ISSN: 0021-924X

    DAY: 19

    MONTH: Jun

    YEAR: 1997

    Nitric oxide-induced modification of glyceraldehyde-3-phosphate dehydrogenase with NAD+ is not ADP-ribosylation. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 376600

    Nitric oxide-induced modification of glyceraldehyde-3-phosphate dehydrogenase with NAD+ is not ADP-ribosylation. Keywords Mesh Terms:

    KEYWORDS: Phosphorus Radioisotopes

    MESH TERMS: diagnostic use

    Chemical & Substance for Abstract: Nitric oxide-induced modification of glyceraldehyde-3-phosphate dehydrogenase with NAD+ is not ADP-ribosylation. Information

    Substance Name: Glyceraldehyde-3-Phosphate Dehydrogenase

    Registry Number: EC 1.2.1.-

    Grant and Affiliation Information for Nitric oxide-induced modification of glyceraldehyde-3-phosphate dehydrogenase with NAD+ is not ADP-ribosylation.

    AFFILIATION: Department of Biochemistry, Shimane Medical University, Izumo.

    Country: JAPAN

    JAPAN Research PublicationJAPAN Research Publication

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    MEDLINETA: J Biochem

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