TY - JOUR
T1 - Theaflavins, dimeric catechins, inhibit peptide transport across Caco-2 cell monolayers via down-regulation of AMP-activated protein kinase-mediated peptide transporter PEPT1
AU - Takeda, Junko
AU - Park, Ha Young
AU - Kunitake, Yuri
AU - Yoshiura, Keiko
AU - Matsui, Toshiro
N1 - Funding Information:
This study was supported by a Grant-in-aid from the Ministry of Education, Science, Sports and Culture of Japan (No. 22248014 ) to Toshiro Matsui. The authors thank Jin Yin for her kind support in the transport experiments.
PY - 2013/6/15
Y1 - 2013/6/15
N2 - In the small intestine, peptide transporter 1 (PEPT1) plays a role in the transport of di- and tripeptides. In this study, we investigated whether theaflavins (TFs) affect the absorption of small peptides in human intestinal Caco-2 cells, since TFs do not penetrate through the cells and might be involved in intestinal transport systems. In transport experiments, the transport of glycyl-sarcosine (Gly-Sar, a model molecule for PEPT1 transport) and other dipeptides (Val-Tyr and Ile-Phe) were significantly reduced (P < 0.05) in TFs-pretreated cells. In TF 3′-O-gallate-pretreated cells, Western blot analysis revealed attenuated expression of PEPT1 transporter and Gly-Sar transport was completely ameliorated by 10 μM Compound C, an AMP-activated protein kinase (AMPK) inhibitor. In conclusion, the present study demonstrated that TFs inhibit peptide transport across Caco-2 cell monolayers, probably through suppression of AMPK-mediated PEPT1 expression, which should be considered a new bioactivity of TFs in black tea.
AB - In the small intestine, peptide transporter 1 (PEPT1) plays a role in the transport of di- and tripeptides. In this study, we investigated whether theaflavins (TFs) affect the absorption of small peptides in human intestinal Caco-2 cells, since TFs do not penetrate through the cells and might be involved in intestinal transport systems. In transport experiments, the transport of glycyl-sarcosine (Gly-Sar, a model molecule for PEPT1 transport) and other dipeptides (Val-Tyr and Ile-Phe) were significantly reduced (P < 0.05) in TFs-pretreated cells. In TF 3′-O-gallate-pretreated cells, Western blot analysis revealed attenuated expression of PEPT1 transporter and Gly-Sar transport was completely ameliorated by 10 μM Compound C, an AMP-activated protein kinase (AMPK) inhibitor. In conclusion, the present study demonstrated that TFs inhibit peptide transport across Caco-2 cell monolayers, probably through suppression of AMPK-mediated PEPT1 expression, which should be considered a new bioactivity of TFs in black tea.
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U2 - 10.1016/j.foodchem.2012.12.026
DO - 10.1016/j.foodchem.2012.12.026
M3 - Article
C2 - 23497868
AN - SCOPUS:84874016283
SN - 0308-8146
VL - 138
SP - 2140
EP - 2145
JO - Food Chemistry
JF - Food Chemistry
IS - 4
ER -