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Melanin‐concentrating hormone‐1 receptor binding activity of pheophorbides isolated from morus alba leaves
Author(s) -
Oh Byung Koo,
Oh KwangSeok,
Kwon Kwangil,
Ryu Shi Yong,
Kim Young Sup,
Lee Byung Ho
Publication year - 2010
Publication title -
phytotherapy research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.019
H-Index - 129
eISSN - 1099-1573
pISSN - 0951-418X
DOI - 10.1002/ptr.3081
Subject(s) - pheophorbide a , chinese hamster ovary cell , receptor , mapk/erk pathway , biochemistry , melanin concentrating hormone , estrogen receptor , recombinant dna , chemistry , kinase , biology , microbiology and biotechnology , chlorophyll , botany , gene , genetics , cancer , neuropeptide , breast cancer
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 13 2 (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 (IC 50 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 13 2 (S)‐hydroxypheophorbide a methyl ester act as modulators of MCH‐1 receptor and MCH‐mediated ERK signaling. Copyright © 2009 John Wiley & Sons, Ltd.
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