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Organs from mice deleted for NRH:quinone oxidoreductase 2 are deprived of the melatonin binding site MT 3
Author(s) -
Mailliet François,
Ferry Gilles,
Vella Fanny,
Thiam Kader,
Delagrange Philippe,
Boutin Jean A.
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.10.083
Subject(s) - melatonin , melatonin receptor , binding site , chemistry , quinone , biochemistry , in vivo , radioligand , biology , endocrinology , microbiology and biotechnology
Two melatonin receptors (MT 1 and MT 2 ) have been cloned. A third melatonin binding site, MT 3 , is known with remarkable and distinct pharmacological properties. We previously reported the purification of MT 3 and identified it as the enzyme dihydronicotinamide riboside:quinone reductase 2 (NQO2). To investigate the relationship between NQO2 and MT 3 , we generated a NQO2 −/− mouse strain. These mice no longer present MT 3 binding sites as measured with 2‐[ 125 I]‐iodo, 5‐methoxycarbonylamino‐ N ‐acetyltryptamine, the specific MT 3 radioligand. These data establish NQO2 as part of the MT 3 binding sites in vivo and resolve the matter of the nature of the third melatonin binding site.