Post-translational modifications of proteins play an important role in their stability, solubility and in vivo function. Also, for several reasons, such as the Golgi fragmentation during cancerogenesis, glycosylation as the most common modification is especially promising in offering high cancer specificity which, in combination with tissue-specific biomarkers available in the case of prostate diseases (PSA, PSMA, PAP), may lead to the development of novel oncodiagnostic approaches. In this review, we present the importance of subterminal glycan structures based on the N-acetylated monosaccharides GlcNAc and GalNAc in N- and also O-glycans, structures of which they are a component (LacNAc, LacdiNAc, branched structures). We also discuss the importance and clinical performance of these structures in cases of prostate cancer diagnostics using lectin-based affinity methods, which could be implemented in clinical laboratory practice in the future.
蛋白质的翻译后修饰对其稳定性、溶解性及体内功能具有重要影响。特别是在癌变过程中高尔基体发生断裂等情况下，作为最常见修饰方式的糖基化，因其能提供高度的癌症特异性而展现出巨大潜力。结合前列腺疾病中已有的组织特异性生物标志物（如PSA、PSMA、PAP），这种特性有望推动新型肿瘤诊断方法的开发。本综述重点探讨了基于N-乙酰化单糖GlcNAc和GalNAc构成的末端亚区聚糖结构在N-连接与O-连接聚糖中的重要性，这些结构作为LacNAc、LacdiNAc及分支结构的组成部分发挥作用。同时，我们通过凝集素亲和法评估了这些结构在前列腺癌诊断中的临床价值与应用前景，这些方法未来有望在临床实验室实践中得到应用。
肿瘤(癌症)患者之家