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Figure 3 | Genome Medicine

Figure 3

From: Towards an integrated proteomic and glycomic approach to finding cancer biomarkers

Figure 3

Identification of EGFR glycoforms. (a) The extracellular-domain sequence of EGFR (629 amino acids) is shown at the top. Black bars, peptides that are predicted to be generated by tryptic digestion; green boxes, peptides with known N-linked glycosylation sites; red boxes, peptides identified in a series of four LC-MS/MS experiments to identify proteins in reference pools of plasma from healthy subjects and patients with cancer. A manual inspection for known glycosylated peptides from EGFR was then carried out, leading to the identification of the peptide containing the Asn328 glycosylation (green box in experiment 4). (b) EGFR from the A431 cell line was subjected to MS analysis. Ten N-linked glycosylation sites were identified, and the main glycan proposed to be at each site is shown [41]. Curly brackets indicate that the monomer (sialic acid) is present in one of these positions (or two in the case of the glycan attached to Asn544). (c) The proposed glycan structure for one EGFR peptide differs from that of the corresponding peptide identified in A431 cells. This structure was determined following LC-MS/MS analysis of human plasma from a mixture of control individuals and patients with lung cancer (SL Wu and BL Karger, personal communication). Reproduced with permission from [40].

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