Glycoproteomics approaches that depict differential membrane glycoproteome profiles of fucosyltransferase IV-overexpressed A549 cell
Date Issued
2011
Date
2011
Author(s)
Chi, Min-Chieh
Abstract
Aberrant glycosylation play a pivotal role in cancer biology. In this study, we employed A549Mock and A549FucT4 cell lines as the models to comprehend the fucosyltransferase IV affecting glycosylation and cancer progression with a focus on cell membrane proteins by comparative glycoproteomic approaches. All previous data, not only in vitro assay but also in vivo animal experiments, demonstrated that A549FucT4 cell line is more malignant than A549Mock and possesses higher capacity of metastasis. The A549FucT4 over-expresses fucosyltransferase IV, which contribute to Lewis glycoepitopes so that carbohydrates attaching to proteins are likely to be highly fucosylated. The entire set of N-glycan was analyzed by MALDI-TOF mass spectrometry. The MS profile of A549FucT4 N-glycan revealed that additional molecular ion was detected, unique carbohydrate structures from mock transfectant. Lectin-based strategy coupling with LC/ESI-MS/MS was adopted for our purpose of identification of the membrane protsins which were decorated with more fucosyl glycoepitopes. The searching results against MASCOT software by MS/MS data revealed assignment of 19 specific proteins in the result of A549FucT4. All identified peptides containing N-X-S/T sequon were quantitatively analyzed by the automated software, IDEAL-Q. Most of the identified proteins are involved in cell adhesion, such as contactin-1, CD166, and integrin-α 3. In addition, some of them are thought to modulate signaling pathway. We anticipate that our finding can facilitate us to understand the role of the fucosylated membrane proteins in lung cancer.
Subjects
lung cancer
membrane proteins
fucosyltransferase IV
glycoproteomics
label-free quantitative mass spectrometry
SDGs
Type
thesis
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