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Kim, Hye-Jin,Kwon, Sojung,Nam, Seo Hee,Jung, Jae Woo,Kang, Minkyung,Ryu, Jihye,Kim, Ji Eon,Cheong, Jin-Gyu,Cho, Chang Yun,Kim, Somi,Song, Dae-Geun,Kim, Yong-Nyun,Kim, Tai Young,Jung, Min-Kyo,Lee, Kyun The Federation of American Societies for Experimen 2017 The FASEB Journal Vol.31 No.4
<P>Membrane proteins sense extracellular cues and transduce intracellular signaling to coordinate directionality and speed during cellular migration. They are often localized to specific regions, as with lipid rafts or tetraspanin-enriched microdomains; however, the dynamic interactions of tetraspanins with diverse receptors within tetraspanin-enriched microdomains on cellular surfaces remain largely unexplored. Here, we investigated effects of tetraspan(in) TM4SF5 (transmembrane 4 L6 family member 5)-enriched microdomains (T5ERMs) on the directionality of cell migration. Physical association of TM4SF5 with epidermal growth factor receptor (EGFR) and integrin alpha 5 was visualized by live fluorescence cross-correlation spectroscopy and higher-resolution microscopy at the leading edge of migratory cells, presumably forming TM4SF5-enriched microdomains. Whereas TM4SF5 and EGFR colocalized at themigrating leading region more than at the rear, TM4SF5 and integrin a5 colocalized evenly throughout cells. Cholesterol depletion and disruption in TM4SF5 post-translational modifications, including N-glycosylation and palmitoylation, altered TM4SF5 interactions and cellular localization, which led to less cellular migration speed and directionality in 2-or 3-dimensional conditions. TM4SF5 controlled directional cell migration and invasion, and importantly, these TM4SF5 functions were dependent on cholesterol, TM4SF5 post-translational modifications, and EGFR and integrin alpha 5 activity. Altogether, we showed that TM4SF5 dynamically interacted with EGFR and integrin a5 in migratory cells to control directionality and invasion.-Kim, H.-J., Kwon, S., Nam, S. H., Jung, J. W., Kang, M., Ryu, J., Kim, J. E., Cheong, J.-G., Cho, C. Y., Kim, S., Song, D.-G., Kim, Y.-N., Kim, T. Y., Jung, M.-K., Lee, K.-M., Pack, C.-G., Lee, J. W. Dynamic and coordinated single-molecular interactions at TM4SF5-enriched microdomains guide invasive behaviors in 2-and 3-dimensional environments. FASEB J. 31, 1461-1481 (2017). www.fasebj.org</P>
Kim, Somi,Cho, Chang Yun,Lee, Doohyung,Song, Dae-Geun,Kim, Hye-Jin,Jung, Jae Woo,Kim, Ji Eon,Park, Dasomi,Lee, Haesong,Um, Hyejin,Park, Jinsoo,Choi, Yoonjeong,Kim, Yoomin,Nam, Seo Hee,Lee, Jung Weon Elsevier 2018 Cancer letters Vol.438 No.-
<P><B>Abstract</B></P> <P>CD133 is a surface marker of liver cancer stem cells. Transmembrane 4 L six family member 5 (TM4SF5) promotes sphere growth and circulation. However, it is unknown how CD133 and TM4SF5 cross-talk with each other for cancer stem cell properties. Here, we investigated the significance of inter-relationships between CD133, TM4SF5, CD44, and protein tyrosine phosphatase receptor type F (PTPRF) in a three-dimensional (3D) sphere growth system. We found that CD133 upregulated TM4SF5 and CD44, whereas TM4SF5 and CD44 did not affect CD133 expression. Signaling activity following CD133 phosphorylation caused TM4SF5 expression and sphere growth. TM4SF5 bound to CD133 and promoted c-Src activity for CD133 phosphorylation as a positive feedback loop, leading to CD133-mediated sphere growth that was inhibited by TM4SF5 inhibition or suppression. TM4SF5 also bound PTPRF and promoted paxillin phosphorylation. Decreased sphere growth upon CD133 suppression was recovered by TM4SF5 expression and partially by PTPRF suppression. TM4SF5 inhibition enhanced PTPRF levels and abolished PTPRF suppression-mediated sphere growth. Altogether, CD133-induced TM4SF5 expression and function were important for liver cancer sphere growth and may be a promising target to block metastasis.</P> <P><B>Highlights</B></P> <P> <UL> <LI> The role of TM4SF5 and CD133 cross-talk in the CSC properties of HCC is unknown. </LI> <LI> CD133-induced c-Src, Akt, and β-catenin signaling mediates TM4SF5 induction. </LI> <LI> TM4SF5 drives CD133 phosphorylation via a bidirectional positive feedback loop. </LI> <LI> TM4SF5 binds PTPRF to regulate cellular signaling for anchorage-independent growth. </LI> <LI> CD133/TM4SF5/PTPRF and CD44 are potential biomarkers for HCC metastasis. </LI> </UL> </P>
Kim, So-Hyun,K. Cho, Somi,Min, Tae-Sun,Kim, Yujin,Yang, Seung-Ok,Kim, Hee-Su,Hyun, Sun-Hee,Kim, Hana,Kim, Young-Suk,Choi, Hyung-Kyoon the Society for Free Radical Research Japan 2011 Journal of clinical biochemistry and nutrition Vol.48 No.3
<P>The ameliorating effects of Mango (<I>Mangifera indica</I> L.) flesh and peel samples on plasma ethanol level were investigated using a mouse model. Mango fruit samples remarkably decreased mouse plasma ethanol levels and increased the activities of alcohol dehydrogenase and acetaldehyde dehydrogenase. The <SUP>1</SUP>H-NMR-based metabolomic technique was employed to investigate the differences in metabolic profiles of mango fruits, and mouse plasma samples fed with mango fruit samples. The partial least squares-discriminate analysis of <SUP>1</SUP>H-NMR spectral data of mouse plasma demonstrated that there were clear separations among plasma samples from mice fed with buffer, mango flesh and peel. A loading plot demonstrated that metabolites from mango fruit, such as fructose and aspartate, might stimulate alcohol degradation enzymes. This study suggests that mango flesh and peel could be used as resources for functional foods intended to decrease plasma ethanol level after ethanol uptake.</P>
Functional regulation of Slug / Snail2 is dependent on GSK‐3β‐mediated phosphorylation
Kim, Jin Young,Kim, Young Mee,Yang, Chang Hee,Cho, Somi K.,Lee, Jung Weon,Cho, Moonjae Blackwell Publishing Ltd 2012 The FEBS journal Vol.279 No.16
<P>Snail family proteins regulate transcription of molecules for cell–cell adhesion during epithelial–mesenchymal transition (EMT). Based on putative glycogen synthase kinase 3β (GSK‐3β) phosphorylation sites within the Slug/Snail2, we explored the significance of GSK‐3β‐mediated phosphorylation in Slug/Snail2 expression during EMT. Mutation of the putative GSK‐3β phosphorylation sites (S92/96A or S100/104A) enhanced the Slug/Snail2‐mediated EMT properties of E‐cadherin repression and vimentin induction, compared with wild‐type Slug/Snail2. S92/96A mutation inhibited degradation of Slug/Snail2 and S100/104A mutation extended nuclear stabilization. Inhibition of GSK‐3β activity caused similar effects, as did the phosphorylation mutations. Thus, our study suggests that GSK‐3β‐mediated phosphorylation of Slug/Snail2 controls its turnover and localization during EMT.</P>
Kim, Chulwon,Lee, Il Ho,Hyun, Ho Bong,Kim, Jong-Chan,Gyawali, Rajendra,Lee, Seok-Geun,Lee, Junhee,Kim, Sung-Hoon,Shim, Bum Sang,Cho, Somi K.,Ahn, Kwang Seok SAGE Publications 2017 Integrative cancer therapies Vol.16 No.2
<P>Activation of signal transducer and activator of transcription 3 (STAT3) is well known to play a major role in the cell growth, survival, proliferation, metastasis, and angiogenesis of various cancer cells. Most of the citrus species offer large quantities of phytochemicals that have beneficial effects attributed to their chemical components. Our study was carried out to evaluate the anticancer effects of the pericarp of Iyokan (<I>Citrus iyo</I> Hort. ex Tanaka), locally known as yeagam in Korea, through modulation of the STAT3 signaling pathway in both tumor cells and a nude mice model. The effect of supercritical extracts of yeagam peel (SEYG) on STAT3 activation, associated protein kinases, STAT3-regulated gene products, cellular proliferation, and apoptosis was examined. The in vivo effect of SEYG on the growth of DU145 human prostate xenograft tumors in athymic <I>nu/nu</I> male mice was also investigated. We found SEYG exerted substantial inhibitory effect on STAT3 activation in human prostate cancer DU145 cells as compared to other tumor cells analyzed. SEYG inhibited proliferation and downregulated the expression of various STAT3-regulated gene products such as bcl-2, bcl-xL, survivin, IAP-1/2, cyclin D1, cyclin E, COX-2, VEGF, and MMP-9. This correlated with an increase in apoptosis as indicated by an increase in the expression of p53 and p21 proteins, the sub-G1 arrest, and caspase-3-induced PARP cleavage. When administered intraperitoneally, SEYG reduced the growth of DU145 human prostate xenograft tumors through downmodulation of STAT3 activation in athymic <I>nu/nu</I> male mice. Overall, these results suggest that SEYG extract has the potential source of STAT3 inhibitors that may have a potential in chemoprevention of human prostate cancer cells.</P>