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Baicalin and Scutellarin Are Proteasome Inhibitors that Specifically Target Chymotrypsin‐like Catalytic Activity
Author(s) -
Wu YiXin,
Sato Eiji,
Kimura Wataru,
Miura Naoyuki
Publication year - 2013
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.4878
Subject(s) - scutellarin , baicalin , chemistry , chymotrypsin , pharmacology , traditional medicine , medicine , biochemistry , enzyme , organic chemistry , high performance liquid chromatography , trypsin
Baicalin and scutellarin are the major active principal flavonoids extracted from the Chinese herbal medicines Scutellaria baicalensis and Erigeron breviscapus (Vant.) Hand‐Mazz. It has recently been reported that baicalin and scutellarin have antitumor activity. However, the mechanisms of action are unknown. We previously reported that some flavonoids have a specific role in the inhibition of the activity of proteasome subunits and induced apoptosis in tumor cells. To further investigate these pharmacological effects, we examined the inhibitory activity of baicalin and scutellarin on the extracted proteasomes from mice and cancer cells. Using fluorogenic substrates for proteasome catalytic subunits, we found that baicalin and scutellarin specifically inhibited chymotrypsin‐like activity but did not inhibit trypsin‐like and peptidyl‐glutamyl peptide hydrolyzing activities. These data suggested that baicalin and scutellarin specifically inhibit chymotrypsin‐like catalytic activity in the proteasome. Copyright © 2012 John Wiley & Sons, Ltd.