Please use this identifier to cite or link to this item: https://doi.org/10.1021/pr100492x
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dc.titleCathepsin S mediates gastric cancer cell migration and invasion via a putative network of metastasis-associated proteins
dc.contributor.authorYixuan, Y.
dc.contributor.authorKiat, L.S.
dc.contributor.authorYee, C.L.
dc.contributor.authorHuiyin, L.
dc.contributor.authorYunhao, C.
dc.contributor.authorKuan, C.P.
dc.contributor.authorHassan, A.
dc.contributor.authorTing, W.T.
dc.contributor.authorManuel, S.-T.
dc.contributor.authorGuan, Y.K.
dc.contributor.authorPin, L.Y.
dc.date.accessioned2014-11-25T09:44:13Z
dc.date.available2014-11-25T09:44:13Z
dc.date.issued2010-09-03
dc.identifier.citationYixuan, Y., Kiat, L.S., Yee, C.L., Huiyin, L., Yunhao, C., Kuan, C.P., Hassan, A., Ting, W.T., Manuel, S.-T., Guan, Y.K., Pin, L.Y. (2010-09-03). Cathepsin S mediates gastric cancer cell migration and invasion via a putative network of metastasis-associated proteins. Journal of Proteome Research 9 (9) : 4767-4778. ScholarBank@NUS Repository. https://doi.org/10.1021/pr100492x
dc.identifier.issn15353893
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/108285
dc.description.abstractCancer progression is governed by multifaceted interactions of cancer cells with their microenvironment and one of these ways is through secreted compounds. Substances released by gastric cancer cells have not being profiled in a proteome-wide manner. ITRAQ-based tandem mass spectrometry was employed to quantify proteins secreted by HFE145 normal, MKN7 well-differentiated, and MKN45 poorly differentiated gastric cancer cell lines. The expression levels of 237 proteins were found to be significantly different between normal and cancer cells. Further examination of 16 gastric cell lines and 115 clinical samples validated the up-regulation of CTSS expression in gastric cancer. Silencing CTSS expression suppressed the migration and invasion of gastric cancer cells in vitro. Subsequent secretomics revealed that CTSS silencing resulted in changes in expression levels of 197 proteins, one-third of which are implicated in cellular movement. Proteome-wide comparative secretomes of normal and gastric cancer cells were produced that constitute a useful resource for gastric cancer research. CTSS was demonstrated to play novel roles in gastric cancer cell migration and invasion, putatively via a network of proteins associated with cell migration, invasion, or metastasis. Cathepsin S is member of a large group of extracellular proteases, which are attractive drug targets. The implicated role of CTSS in gastric cancer metastasis provides an opportunity to test existing compounds against CTSS for adjuvant therapy and/or treatment of metastatic gastric cancers. © 2010 American Chemical Society.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1021/pr100492x
dc.sourceScopus
dc.subjectcathepsin
dc.subjectCTSS
dc.subjectgastric cancer
dc.subjectinvasion
dc.subjectmigration
dc.subjectprotease
dc.subjectproteomics
dc.subjectsecretome
dc.typeArticle
dc.contributor.departmentCANCER SCIENCE INSTITUTE OF SINGAPORE
dc.contributor.departmentPATHOLOGY
dc.description.doi10.1021/pr100492x
dc.description.sourcetitleJournal of Proteome Research
dc.description.volume9
dc.description.issue9
dc.description.page4767-4778
dc.description.codenJPROB
dc.identifier.isiut000281443700040
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