Rhesus monkey MCH-R1 and MCH-R2 receptors were cloned. Amino acid homology is 98.8% between monkey and human MCH-R1, while monkey and human MCH-R2 are 98% homologous. Binding and intracellular signaling characteristics of the monkey receptors were compared with the human homologues. The results demonstrate that MCH binds to the monkey MCH-R1 receptor with a K-d of 6.5 nM and monkey MCH-R2 with a K-d of 2.2 nM similar to K-d values for human MCH-R1 and MCH-R2. Additionally, monkey MCH-R1 couples through G(i)/G(o) and G(q)-type G proteins similar to human MCH-R1 whereas monkey and human MCH-R2 utilize the G(q) signaling pathway. (C) 2002 Elsevier Science Inc. All rights reserved.
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Takeda Chem Ind Ltd, Div Pharmaceut Res, Discovery Res Labs 1, Tsukuba, Ibaraki 3004293, JapanTakeda Chem Ind Ltd, Div Pharmaceut Res, Discovery Res Labs 1, Tsukuba, Ibaraki 3004293, Japan
Mori, M
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Harada, M
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Harada, M
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Terao, Y
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Terao, Y
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Sugo, T
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Watanabe, T
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Watanabe, T
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Shimomura, Y
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Abe, M
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Shintani, Y
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Onda, H
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Onda, H
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Nishimura, O
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Fujino, M
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Takeda Chem Ind Ltd, Div Pharmaceut Res, Discovery Res Labs 1, Tsukuba, Ibaraki 3004293, JapanTakeda Chem Ind Ltd, Div Pharmaceut Res, Discovery Res Labs 1, Tsukuba, Ibaraki 3004293, Japan
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Harada, M
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Terao, Y
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Shimomura, Y
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Abe, M
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Abe, M
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Shintani, Y
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Onda, H
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Nishimura, O
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