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Interaction of the Oncofetal Thomsen–Friedenreich Antigen with Galectins in Cancer Progression and Metastasis

机译:胎粪汤姆森-弗里登赖希抗原与半乳凝集素在癌症进展和转移中的相互作用

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摘要

Aberrant glycosylation of cell membrane proteins is a universal feature of cancer cells. One of the most common glycosylation changes in epithelial cancer is the increased occurrence of the oncofetal Thomsen–Friedenreich disaccharide Galβ1–3GalNAc (T or TF antigen), which appears in about 90% of cancers but is rarely seen in normal epithelium. Over the past few years, increasing evidence has revealed that the increased appearance of TF antigen on cancer cell surface plays an active role in promoting cancer progression and metastasis by interaction with the β-galactoside-binding proteins, galectins, which themselves are also frequently overexpressed in cancer and pre-cancerous conditions. This review summarizes the current understanding of the molecular mechanism of the increased TF occurrence in cancer, the structural nature, and biological impact of TF interaction with galectins, in particular galectin-1 and -3, on cancer progression and metastasis.
机译:细胞膜蛋白的异常糖基化是癌细胞的普遍特征。上皮癌中最常见的糖基化变化之一是胎生汤姆森-弗里登赖希二糖Galβ1-3GalNAc(T或TF抗原)的发生率增加,这种情况出现在约90%的癌症中,但在正常上皮中很少见。在过去的几年中,越来越多的证据表明,在癌细胞表面上增加的TF抗原的出现通过与β-半乳糖苷结合蛋白(半乳糖凝集素)相互作用而在促进癌症进展和转移中起着积极作用,而半乳糖苷结合蛋白本身也经常被过度表达在癌症和癌前状态。这篇综述总结了目前对癌症中TF发生增加的分子机制,TF与半乳糖凝集素(尤其是半乳糖凝集素-1和-3)相互作用对癌症进展和转移的分子机制,结构性质以及生物学影响的理解。

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