phate (NADP) acts as a hydride ion acceptor or donor in many biological redox reactions. NAD has also been shown to be required for important nonredox adenosine diphosphate (ADP) —ribose transfer reactions involved in deoxyribonucleic acid (DNA) repair and calcium mobilization (Kim et al., 1994; Lautier et al., 1993; Lee et al., 1989). The amino acid tryptophan is converted in part to nicotinamide and thus can contribute to meeting the requirement for niacin.
In the form of the coenzymes NAD and NADP, niacin functions in many biological redox reactions. NAD functions in intracellular respiration and as a codehydrogenase with enzymes involved in the oxidation of fuel molecules such as glyceraldehyde 3-phosphate, lactate, alcohol, 3-hydroxybutyrate, pyruvate, and α-ketoglutarate. NADP functions in reductive biosyntheses such as in fatty acid and steroid syntheses and, like NAD, as a codehydrogenase—as in the oxidation of glucose 6-phosphate to ribose 5-phosphate in the pentose phosphate pathway.
Three classes of enzymes cleave the β-N-glycosylic bond of NAD to free nicotinamide and catalyze the transfer of ADP-ribose in nonredox reactions (Lautier et al., 1993). Two of the three classes catalyze ADP-ribose transfer to proteins: mono-ADP-ribosyltransferases and poly-ADP-ribose polymerase (PARP). The third class promotes the formation of cyclic ADP-ribose, which mobilizes calcium from intracellular stores in many types of cells (Kim et al., 1994).
The enzyme PARP is found in the nuclei of eukaryotic cells and catalyzes the transfer of many ADP-ribose units from NAD to an acceptor protein and also to the enzyme itself. These nuclear poly-ADP-ribose proteins seem to function in DNA replication and repair and in cell differentiation. DNA damage greatly enhances the activity of PARP (Stierum et al., 1994); PARP activity is strongly correlated with cellular apoptosis (Stierum et al., 1994).
Absorption of nicotinic acid and nicotinamide from the stomach and the intestine is rapid (Bechgaard and Jespersen, 1977) and at low concentrations is mediated by sodium ion-dependent facilitated diffusion. At higher concentrations, passive diffusion predominates,