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Molecular and cellular pharmacological properties of 5‐methoxycarbonylamino‐ N ‐acetyltryptamine (MCA‐NAT): a nonspecific MT3 ligand
Author(s) -
Vincent Ludwig,
Cohen William,
Delagrange Philippe,
Boutin Jean A.,
Nosjean Olivier
Publication year - 2010
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.2010.00746.x
Subject(s) - chinese hamster ovary cell , melatonin , melatonin receptor , nat , receptor , agonist , biology , ligand (biochemistry) , in vivo , hamster , chemistry , pharmacology , medicine , endocrinology , microbiology and biotechnology , biochemistry , genetics , computer network , computer science
5‐Methoxycarbonylamino‐ N ‐acetyltryptamine (MCA‐NAT) has been initially described as a ligand at non MT 1 , non MT 2 melatonin binding site (MT3) selective versus MT 1 and MT 2 , two membrane melatonin receptors. MCA‐NAT activity has been reported by others in different models, in vivo, particularly in the intra‐ocular pressure (IOP) models in rabbits and monkeys. Its activity was systematically linked to either MT3 or to a new, yet unknown, melatonin receptor. In this article, the melatonin receptor pharmacology of MCA‐NAT is described. MCA‐NAT has micromolar range affinities at the melatonin receptors MT 1 and MT 2 , while in functional studies, MCA‐NAT proved to be a powerful MT 1 /MT 2 partial agonist in the sub‐micromolar range. These data strongly suggest that MCA‐NAT actions might be mediated by these receptors in vivo. Finally, as described by others, we show that MCA‐NAT is unable to elicit any type of receptor‐like functional responses from Chinese hamster ovary cells over‐expressing quinone reductase 2, the MT3.