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Characterization of ovolin, an orally active tryptic peptide released from ovalbumin with anxiolytic-like activity
Ayako Oda1, Kentaro Kaneko, Takafumi Mizushige
1Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Gokasho Uji, Kyoto, Japan.
Abstract:
We found that tryptic digest of ovalbumin after oral (p.o.) and intraperitoneal (i.p.) administration exhibited anxiolytic-like activity in mice, and then searched for orally active low-molecular-weight peptides with anxiolytic-like activity in the tryptic digest. Val-Tyr-Leu-Pro-Arg, named ovolin, corresponding to ovalbumin (280-284), mimicked the anxiolytic-like activity after p.o. and i.p. administration. The anxiolytic-like activity of ovolin was inhibited by indomethacin, a cyclooxygenase (COX) inhibitor, or BWA868C, an antagonist of the DP1 receptor for prostaglandin (PG) D2 . Ovolin-induced anxiolytic-like activity was also blocked by SCH58261 or bicuculline, antagonists of the adenosine A2A and GABAA receptors, respectively. Ovolin has no affinity for the DP1 , A2A and GABAA receptors. Taken together, ovolin may exhibit anxiolytic-like activity in a manner dependent on the PGD2 -DP1 system coupled to the A2A and GABAA receptors.
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