缺失NRH：醌氧化还原酶2的小鼠的器官缺乏褪黑素结合位点MT3。
Organs from mice deleted for NRH:quinone oxidoreductase 2 are deprived of the melatonin binding site MT3.
作者信息
Mailliet François, Ferry Gilles, Vella Fanny, Thiam Kader, Delagrange Philippe, Boutin Jean A
机构信息
Pharmacologie Moléculaire et Cellulaire, Institut de Recherches Servier, 125 chemin de Ronde, 78290 Croissy-sur-Seine, France.
出版信息
FEBS Lett. 2004 Dec 3;578(1-2):116-20. doi: 10.1016/j.febslet.2004.10.083.
Two melatonin receptors (MT1 and MT2) have been cloned. A third melatonin binding site, MT3, is known with remarkable and distinct pharmacological properties. We previously reported the purification of MT3 and identified it as the enzyme dihydronicotinamide riboside:quinone reductase 2 (NQO2). To investigate the relationship between NQO2 and MT3, we generated a NQO2-/- mouse strain. These mice no longer present MT3 binding sites as measured with 2-[125I]-iodo, 5-methoxycarbonylamino-N-acetyltryptamine, the specific MT3 radioligand. These data establish NQO2 as part of the MT3 binding sites in vivo and resolve the matter of the nature of the third melatonin binding site.
已克隆出两种褪黑素受体（MT1和MT2）。已知存在第三种褪黑素结合位点MT3，其具有显著且独特的药理学特性。我们之前报道了MT3的纯化，并将其鉴定为二氢烟酰胺核糖：醌还原酶2（NQO2）。为了研究NQO2与MT3之间的关系，我们培育出了NQO2基因敲除小鼠品系。用特异性MT3放射性配体2-[¹²⁵I]-碘-5-甲氧基羰基氨基-N-乙酰色胺检测发现，这些小鼠不再存在MT3结合位点。这些数据证实NQO2是体内MT3结合位点的一部分，解决了第三种褪黑素结合位点的性质问题。
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