Melanin-concentrating hormone-1 receptor binding activity of pheophorbides isolated from morus alba leaves

Autor:	Kwang-il Kwon, Young Sup Kim, Byung Ho Lee, Kwang-Seok Oh, Byung Koo Oh, Shi Yong Ryu
Rok vydání:	2009
Předmět:	Pharmacology MAPK/ERK pathway Kinase Chinese hamster ovary cell Ligand binding assay respiratory system Biology chemistry.chemical_compound chemistry Biochemistry Pheophorbide A Phosphorylation Receptor IC50 hormones hormone substitutes and hormone antagonists
Zdroj:	Phytotherapy Research. 24:919-923
ISSN:	0951-418X
Popis:	The time-resolved fluorescence technique based on melanin-concentrating hormone (MCH) receptor subtype-1 (MCH-1 receptor) binding assay was adopted to carry out a bioassay-guided fractionation of the methanol extract of Morus alba leaves. This fractionation and purification led to the isolation of two compounds identified as pheophorbide a methyl ester and 132(S)-hydroxypheophorbide a methyl ester. These active pheophorbides exhibited potent inhibitory activity in binding of europium-labeled MCH to the human recombinant MCH-1 receptor (IC50 value; 4.03 and 0.33 ?M, respectively). Besides binding activity, the pheophorbides inhibited MCH-mediated extracellular signal-regulated kinase (ERK) phosphorylation in Chinese hamster ovary cells expressing human MCH-1 receptor. These results suggest that pheophorbide a methyl ester and 132(S)-hydroxypheophorbide a methyl ester act as modulators of MCH-1 receptor and MCH-mediated ERK signaling. Copyright © 2009 John Wiley & Sons, Ltd.
Databáze:	OpenAIRE
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