Related Experiment Videos
Comparative proteomics of glycoproteins based on lectin selection and isotope coding
Li Xiong1, Dina Andrews, Fred Regnier
1Department of Chemistry, Purdue University, West Lafayette, Indiana 47907, USA.
Journal of Proteome Research
|December 25, 2003
Summary
This study developed a quantitative proteomics method to identify disease-associated glycan modifications, revealing decreased fucosylated proteins like CD44 and E-selectin during canine lymphosarcoma chemotherapy.
Area of Science:
- Biochemistry
- Proteomics
- Glycoscience
Background:
- Lectins are crucial for glycan structure analysis.
- Aberrant glycosylation is linked to diseases like cancer.
- Quantitative proteomics enables comparative analysis of protein modifications.
Purpose of the Study:
- To develop a comparative proteomics method for examining aberrant glycosylation in cancer.
- To identify disease-associated glycopeptides using lectin affinity selection and stable isotope coding.
- To investigate changes in fucosylated proteins during canine lymphosarcoma chemotherapy.
Main Methods:
- Coupling lectin affinity selection with stable isotope coding for quantitative proteomics.
- Using Lotus tetragonolobus agglutinin (LTA) to select alpha-L-fucose-containing glycopeptides.
- Deglycosylation with PNGase F, followed by reversed-phase chromatography (RPC) and mass spectrometry (MALDI-MS, ESI-MS).
Main Results:
- A comparative proteomics method was established for analyzing aberrant glycosylation.
- Fucosylated proteins, including CD44 and E-selectin, decreased more than 2-fold during chemotherapy in canine lymphosarcoma.
- Identified proteins CD44 and E-selectin are implicated in cancer cell adhesion and migration.
Conclusions:
- The developed method effectively identifies disease-associated glycopeptides.
- Aberrant fucosylation of CD44 and E-selectin may play a role in cancer metastasis.
- Findings support the hypothesis that CD44 and E-selectin are key players in cancer cell spread.