Multi-lectin Affinity Chromatography and Quantitative Proteomic Analysis Reveal Differential Glycoform Levels between Prostate Cancer and Benign Prostatic Hyperplasia Sera

摘要: Currently prostate-specific antigen is used for prostate cancer (PCa) screening, however it lacks the necessary specificity differentiating PCa from other diseases of such as benign prostatic hyperplasia (BPH), presenting a clinical need to distinguish these cases at molecular level. Protein glycosylation plays an important role in number cellular processes involved neoplastic progression and aberrant PCa. In this study, we systematically interrogate alterations circulating levels hundreds serum proteins their glycoforms BPH samples using multi-lectin affinity chromatography quantitative mass spectrometry-based proteomics. Specific lectins (AAL, PHA-L PHA-E) were target chromatographically separate core-fucosylated highly-branched protein analysis, differential expression glycan types have been previously associated with Global CD5L, CFP, C8A, BST1, C7 significantly increased samples. Notable glycoform-specific between identified among CD163, C4A, ATRN PHA-L/E fraction C4BPB AZGP1 AAL fraction. Despite modest differences, substantial similarities glycoproteomic profiles observed sera.