The presence of NADPH-glyceraldehyde 3-phosphate oxidoreductase in macrophages.
The existence of an NADPH-oxidoreductase which utilizes D-glyceraldehyde 3-phosphate as substrate has been demonstrated in mouse peritoneal macrophages. D-Glyceraldehyde could also serve as substrate, albeit with a 10-fold lower efficiency. No NADH oxidation could be demonstrated with either substrate. Addition of D-glyceraldehyde to cultured macrophages increased the rate of activity of the hexose monophosphate shunt to about 65% of the level observed in zymosan A-stimulated macrophages. The possible involvement of the oxidoreductase in this phenomenon and in the inhibitory effect of D-glyceraldehyde on the production of oxygen free radicals by zymosan-stimulated cells is discussed.
D000818:Animals; D001202:Ascitic Fluid; D005985:Glyceraldehyde / Q000378:metabolism / Q000494:pharmacology; D005986:Glyceraldehyde 3-Phosphate / Q000378:metabolism; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000378:metabolism*; D006600:Hexosephosphates / Q000378:metabolism; D008264:Macrophages / Q000187:drug effects / Q000201:enzymology*; D051379:Mice; D008810:Mice, Inbred C57BL; D009249:NADP / Q000494:pharmacology*; D013379:Substrate Specificity; D015054:Zymosan / Q000494:pharmacology
D006600:Hexosephosphates; D005986:Glyceraldehyde 3-Phosphate; D005985:Glyceraldehyde; D009249:NADP; D015054:Zymosan; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases