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Nitric oxide and NAD-dependent protein modification

L J McDonald1, J Moss

  • 1Laboratory of Cellular Metabolism, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892.

Molecular and Cellular Biochemistry
|September 1, 1994
PubMed
Summary
This summary is machine-generated.

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Nitric oxide (NO) does not stimulate ADP-ribosylation. Instead, NO modifies glyceraldehyde-3-phosphate dehydrogenase (GAPDH) by covalently binding the entire NAD molecule, possibly due to S-nitrosylation.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • Nitric oxide (NO) was previously hypothesized to regulate intracellular ADP-ribosylation.
  • This hypothesis was based on protein radiolabelling studies using [32P]NAD and NO in tissue homogenates.

Purpose of the Study:

  • To investigate the mechanism of NO-mediated protein modification.
  • To determine if NO stimulates an endogenous ADP-ribosyltransferase, specifically targeting glyceraldehyde-3-phosphate dehydrogenase (GAPDH).

Main Methods:

  • Replication of NO-stimulated modification in a defined system using purified GAPDH.
  • Biochemical characterization of the NO-stimulated, NAD-dependent modification of GAPDH.

Main Results:

Related Experiment Videos

  • The NO-stimulated modification of GAPDH was confirmed to be the covalent binding of the entire NAD molecule to the enzyme, not ADP-ribosylation.
  • GAPDH is known to be stoichiometrically S-nitrosylated.

    • Conclusions:

    • The initial hypothesis of NO-stimulation of ADP-ribosylation is disproven.
    • NO's role in modifying GAPDH involves the covalent attachment of NAD, potentially by inducing S-nitrosylation of a cysteine residue in the enzyme's active site, thereby altering its chemical reactivity.