Abstract
NAD glycohydrolases are enzymes that catalyze the hydrolisis of NAD to produce ADP-ribose and nicotinamide. Regulation of these enzymes has not been fully elucidated. We have identified an NAD-glycohydrolase activity associated with the outer surface of the plasma membrane in human lung epithelial cell line A549. This activity is negatively regulated by its substrate β-NAD but not by α-NAD. Partial restoration of NADase activity after incubation of the cells with arginine or histidine, known ADP-ribose acceptors, suggests that inhibition be regulated by ADP-ribosylation. A549 do not undergo to apoptosis upon NAD treatment indicating that this effect be likely mediated by a cellular component(s) lacking in epithelial cells.
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Balducci, E., Micossi, L.G. NAD-dependent inhibition of the NAD-glycohydrolase activity in A549 cells. Mol Cell Biochem 233, 127–132 (2002). https://doi.org/10.1023/A:1015562412828
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DOI: https://doi.org/10.1023/A:1015562412828