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Inhibition of Matrix Metalloproteinase Activities and Tightening of Tight Junctions by Diallyl Disulfide in AGS Human Gastric Carcinoma Cells
Author(s) -
Park Hyun Soo,
Kim GiYoung,
Choi IlWhan,
Kim Nam Deuk,
Hwang Hye Jin,
Choi YoungWhan,
Choi Yung Hyun
Publication year - 2011
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1750-3841.2011.02114.x
Subject(s) - diallyl disulfide , tight junction , chemistry , claudin , motility , matrix metalloproteinase , microbiology and biotechnology , cancer cell , biochemistry , cancer research , cancer , biology , medicine , apoptosis
The effect of diallyl disulfide (DADS), a major component of an oil‐soluble allyl sulfide garlic ( Allium sativum ) derivative, on the correlation between anti‐invasive activity and tightening of tight junctions (TJs) was investigated in human gastric adenocarcinoma AGS cells. Our data indicated that the inhibitory effects of DADS on cell motility and invasiveness were found to be associated with increased tightness of the TJs, which was demonstrated by an increase in transepithelial electrical resistance. Activities of matrix metalloprotease (MMP)‐2 and ‐9 in AGS cells were dose‐dependently inhibited by treatment with DADS, and this was also correlated with a decrease in expression of their mRNA and proteins; however, tissue inhibitor of metalloproteinase (TIMP)‐1 and ‐2 mRNA levels and proteins were increased. Additionally, immunoblotting results indicated that DADS repressed the levels of claudin proteins (claudin‐2, ‐3, and ‐4), major components of TJs that play key roles in control and selectivity of paracellular transport. Although further studies are needed, these results suggest that DADS treatment may inhibit tumor cell motility and invasion and, therefore, act as a dietary source to decrease the risk of cancer metastasis.