期刊
JOURNAL OF PROTEOME RESEARCH
卷 8, 期 2, 页码 643-650出版社
AMER CHEMICAL SOC
DOI: 10.1021/pr8007495
关键词
Lectins; affinity chromatography; glycoproteomics; glycoproteins; aberrant glycosylation; breast cancer; plasma; diversity; post-translational modifications; quantification; iTRAQ; HPA; LEL; AAL; LCA
资金
- NCI NIH HHS [1U24CA126480] Funding Source: Medline
Lectin affinity chromatography using concanavalin A (Con A), Helix pomatia, agglutinin (HPA), Lycopersicon esculentum lectin (LEL), Aleuria aurantia lectin (AAL) and Lens culinaris agglutinin (LCA) was used to investigate the utility of narrow selectivity lectins in the characterization of plasma glycoproteome diversity and to recognize cancer associated aberrations in glycosylation. Following affinity chromatographic selection, proteins were tryptically digested, the peptide fragments separated by reversed phase chromatography (RPC), and fractions from RPC identified by tandem mass spectrometry. The diversity of glycosylation found with narrow selectivity lectins was generally 2/3 that of Con A and not related to protein abundance. Small groups of proteins were found with each of the affinity columns, HPA, LEL, AAL, and LCA, that changed 3-fold or more in concentration between normal and breast cancer patient plasma. Although the number of cancer patients examined was too small to validate cancer marker candidates, they are clearly worth examining in a larger, more diverse patient population.
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