Department of Life Technologies, University of Turku, Kiinamyllynkatu 10, 20520, Turku, Finland.
InFLAMES Research Flagship, University of Turku, 20014, Turku, Finland.
BMC Cancer. 2024 Apr 10;24(1):443. doi: 10.1186/s12885-024-12161-5.
Altered glycosylation is a hallmark of cancer associated with therapy resistance and tumor behavior. In this study, we investigated the glycosylation profile of stemness-related proteins OCT4, CIP2A, MET, and LIMA1 in HNSCC tumors.
Tumor, adjacent normal tissue, and blood samples of 25 patients were collected together with clinical details. After tissue processing, lectin-based glycovariant screens were performed.
Strong correlation between glycosylation profiles of all four stemness-related proteins was observed in tumor tissue, whereas glycosylation in tumor tissue, adjacent normal tissue, and serum was differential.
A mannose- and galactose-rich glycosylation niche associated with stemness-related proteins was identified.
糖基化改变是癌症的一个标志,与治疗耐药性和肿瘤行为有关。在这项研究中,我们研究了与 HNSCC 肿瘤相关的干性相关蛋白 OCT4、CIP2A、MET 和 LIMA1 的糖基化谱。
收集了 25 名患者的肿瘤、相邻正常组织和血液样本,并附有临床详细信息。在组织处理后,进行了基于凝集素的糖变异筛选。
在肿瘤组织中观察到所有四个干性相关蛋白的糖基化谱之间存在强烈的相关性,而肿瘤组织、相邻正常组织和血清中的糖基化则存在差异。
鉴定了与干性相关蛋白相关的富含甘露糖和半乳糖的糖基化小生境。