| First Author | Mailliet F | Year | 2004 |
| Journal | FEBS Lett | Volume | 578 |
| Issue | 1-2 | Pages | 116-20 |
| PubMed ID | 15581627 | Mgi Jnum | J:94264 |
| Mgi Id | MGI:3511721 | Doi | 10.1016/j.febslet.2004.10.083 |
| Citation | Mailliet F, et al. (2004) Organs from mice deleted for NRH:quinone oxidoreductase 2 are deprived of the melatonin binding site MT3. FEBS Lett 578(1-2):116-20 |
| abstractText | 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. |
