Glycoproteomics of fucosyltransferase IV-overexpressed A549 cell
Date Issued
2012
Date
2012
Author(s)
Wu, Zhi-Rong
Abstract
Protein glycosylation alterations play an important role in cancer progression, including cell proliferation, cell invasion, and cell metastasis. We use A549-FucT4 cells, which over-expressed fucosyltransferase IV, and A549-Mock cell as a control cell line, as a research model to study the influence of fucosylation in cell biology. Our previous data showed that A549-FucT4 is more malignant than A549-Mock based on the transwell migration assay, adhesion assay, zymography assay, and proliferation of cancer cell lines in SCID mice. We also found that the proliferation rate of A549-FucT4 cells are more rapid than A549-Mock cells. In our study, we used two methods of lectin affinity glycoprotein enrichment to enrich fucosylated proteins, and identified their identities through the LC/ESI-TOF-MS. In comparison to the glycoproteins identified in A549-Mock cells, there were 14 distinctive glycoproteins identified solely in A549-FucT4. Using Ingenuity Pathway Analysis software, we found that these 14 glycoproteins are involved in cell migration, cell proliferation, cell movement, and cell apoptosis. We chose HGFR and CD109 for further study based on our glycoproteomic data. The result indicated that A549-FucT4 cells have less HGFR phosphorylation levels in comparison with A549-Mock cells after treatment with HGF in different doses and different incubation times. But there was no obvious difference in smad3 phosphorylation after TGF-beta 1 treatment between the two cell. We think fucosyltransferase IV overexpression may affect particular proteins which take parts in cancer progression.
Subjects
Lung cancer
Glycoproteins
Lectin affinity enrichment
Fucosyltransferase IV
Glycoproteomic
SDGs
Type
thesis
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