Nitric oxide-induced modification of glyceraldehyde-3-phosphate dehydrogenase with NAD+ is not ADP-ribosylation.
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.
Itoga
M
M
Department of Biochemistry, Shimane Medical University, Izumo.
Tsuchiya
M
M
Ishino
H
H
Shimoyama
M
M
D000246:Adenosine Diphosphate Ribose / Q000378:metabolism*; D000818:Animals; D002384:Catalysis; D002417:Cattle; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000378:metabolism*; D009243:NAD / Q000494:pharmacology*; D009569:Nitric Oxide / Q000502:physiology*; D010761:Phosphorus Radioisotopes
D010761:Phosphorus Radioisotopes; D009243:NAD; D000246:Adenosine Diphosphate Ribose; D009569:Nitric Oxide; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases