Department of Cytobiochemistry, University of Lodz, 90-237 Lodz, Poland.
Int J Mol Med. 2010 Apr;25(4):643-8. doi: 10.3892/ijmm_00000387.
Single N-acetylglucosamine residues attached by O-linkage to serine or threonine (O-GlcNAc) are an abundant, dynamic and inducible post-translational modification of cytoplasmic and nuclear proteins. This study analyzes the activity of the enzyme involved in the removal of these sugar residues, i.e. beta-N-acetylglucosaminidase (O-GlcNAcase) as well as the level of O-GlcNAc in benign and malignant thyroid lesions. Our results demonstrate increased activity of the enzyme in thyroid cancers in comparison to non-neoplastic lesions and adenomas. O-GlcNAc-modified proteins in thyroid cells have a predominantly nuclear distribution and are more abundant in non-neoplastic lesions than in tumors. Understanding the aberrant O-GlcNAc metabolism in thyroid cancer cells may be helpful for developing new diagnostic or treatment methods.
通过 O 连接到丝氨酸或苏氨酸上的单个 N-乙酰葡萄糖胺残基（O-GlcNAc）是细胞质和核蛋白中丰富、动态和可诱导的翻译后修饰。本研究分析了参与去除这些糖残基的酶，即β-N-乙酰氨基葡萄糖苷酶（O-GlcNAcase）的活性以及良性和恶性甲状腺病变中 O-GlcNAc 的水平。我们的结果表明，与非肿瘤性病变和腺瘤相比，甲状腺癌中酶的活性增加。甲状腺细胞中 O-GlcNAc 修饰的蛋白主要分布在核内，并且在非肿瘤性病变中比在肿瘤中更为丰富。了解甲状腺癌细胞中异常的 O-GlcNAc 代谢可能有助于开发新的诊断或治疗方法。
