The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Comparative Serum Glycoproteomics Using Lectin Selected Sialic Acid Glycoproteins with Mass Spectrometric Analysis: Application to Pancreatic Cancer Serum
Abstract
A strategy is developed in this study for identifying sialylated glycoprotein markers in human cancer serum. This method consists of three steps: lectin affinity selection, a liquid separation and characterization of the glycoprotein markers using mass spectrometry. In this work, we use three different lectins (Wheat Germ Agglutinin, (WGA) Elderberry lectin,(SNA), Maackia amurensis lectin, (MAL)) to extract sialylated glycoproteins from normal and cancer serum. Twelve highly abundant proteins are depleted from the serum using an IgY-12 antibody column. The use of the different lectin columns allows one to monitor the distribution of alpha(2,3) and alpha(2,6) linkage type sialylation in cancer serum vs that in normal samples. Extracted glycoproteins are fractionated using NPS-RP-HPLC followed by SDS-PAGE. Target glycoproteins are characterized further using mass spectrometry to elucidate the carbohydrate structure and glycosylation site. We applied this approach to the analysis of sialylated glycoproteins in pancreatic cancer serum. Approximately 130 sialylated glycoproteins are identified using microLC-MS/MS. Sialylated plasma protease C1 inhibitor is identified to be down-regulated in cancer serum. Changes in glycosylation sites in cancer serum are also observed by glycopeptide mapping using microLC-ESI-TOF-MS where the N83 glycosylation of alpha1-antitrypsin is down regulated. In addition, the glycan structures of the altered proteins are assigned using MALDI-QIT-MS. This strategy offers the ability to quantitatively analyze changes in glycoprotein abundance and detect the extent of glycosylation alteration as well as the carbohydrate structure that correlate with cancer.
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Citations
Cites
Intracellular Functions of N-Linked Glycans
Helenius, A., & Aebi, A. M. (2001) · Science · doi:10.1126/science.291.5512.2364 · Cited by 2,405
Cited by
High-sensitivity Analytical Approaches for the Structural Characterization of Glycoproteins
Alley, W. R., Mann, B. F., & Novotny, M. V. (2013) · Chemical Reviews · doi:10.1021/cr3003714 · Cited by 310
Determination of glycosylation sites and site-specific heterogeneity in glycoproteins
An, H. J., Froehlich, J. W., & Lebrilla, C. B. (2009) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2009.07.022 · Cited by 280
New Technologies for Glycomic Analysis: Toward a Systematic Understanding of the Glycome
Rakus, J. F., & Mahal, L. K. (2011) · Annual Review of Analytical Chemistry · doi:10.1146/annurev-anchem-061010-113951 · Cited by 117
Production of α2,6-sialylated IgG1 in CHO cells
Raymond, C., Robotham, A., Spearman, M., Butler, M., Kelly, J., & Durocher, Y. (2015) · mAbs · doi:10.1080/19420862.2015.1029215 · Cited by 106
Capillary electrophoresis–mass spectrometry for direct structural identification of serum N-glycans
Snyder, C. M., Zhou, X., Karty, J. A., Fonslow, B. R., Novotny, M. V., & Jacobson, S. C. (2017) · Journal of Chromatography A · doi:10.1016/j.chroma.2017.09.009 · Cited by 58
Metadata
- Authors
- Zhao, J., Simeone, D. M., Heidt, D., Anderson, M. A., & Lubman, D. M.
- Venue
- Journal of Proteome Research
- Publisher
- American Chemical Society (ACS)
- Published
- 2006-05-26
- Volume
- 5
- Issue
- 7
- Pages
- 1792-1802
- ISSN
- 1535-3893 (ISSN-L)
- 1535-3907
- OpenAlex
- W2053799156
- Cited by
- 214
- References
- 1
- FWCI
- 7.98
- Type
- journal article
- Language
- en
- Open access
- closed
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