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Interactions between melatonin and nicotinamide nucleotide: NADH preservation in cells and in cell‐free systems by melatonin
Author(s) -
Tan DunXian,
Manchester Lucien C.,
Sainz Rosa M.,
Mayo Juan C.,
Leon Josefa,
Hardeland Ruediger,
Poeggeler Burkhard,
Reiter Russel J.
Publication year - 2005
Publication title -
journal of pineal research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.881
H-Index - 131
eISSN - 1600-079X
pISSN - 0742-3098
DOI - 10.1111/j.1600-079x.2005.00234.x
Subject(s) - melatonin , nad+ kinase , nicotinamide adenine dinucleotide , biochemistry , antioxidant , nicotinamide , paraquat , glycerol 3 phosphate dehydrogenase , oxidative stress , oxidative phosphorylation , mitochondrion , chemistry , biology , enzyme , endocrinology
Interactions of melatonin and nicotinamide adenine dinucleotide (NADH) have been studied in different experimental models including NADH‐promoted oxyhemoglobin oxidation, vanadate‐induced NADH oxidation and paraquat‐induced NADH depletion in cultured PC12 cells. Our findings indicate that melatonin preserves NADH levels under oxidative stress both in cell‐free systems and in cultured PC12 cells. These interactions likely involve electron donation by melatonin and reduction of the NAD radical. As a result, the NAD radical is recycled to NADH and melatonin is oxidized to N 1 ‐acetyl‐ N 2 ‐formyl‐5‐methoxykynuramine (AFMK). NADH is a central molecule at the crossroads between energy metabolism and the antioxidant defense system in organisms. Recycling of NADH by melatonin might improve the efficiency of NADH as an energy carrier and as an antioxidant. Interactions between melatonin and NADH may be implicated in mitochondrial metabolism.