Elevation of nucleocytoplasmic beta-N-acetylglucosaminidase (O-GlcNAcase) activity in thyroid cancers.
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.
Krzeslak
Anna
A
Department of Cytobiochemistry, University of Lodz, 90-237 Lodz, Poland. krzeslaka@interia.pl
Pomorski
Lech
L
Lipinska
Anna
A
D000118:Acetylglucosaminidase / Q000378:metabolism*; D002467:Cell Nucleus / Q000201:enzymology*; D005260:Female; D006801:Humans; D008297:Male; D009363:Neoplasm Proteins / Q000378:metabolism; D013964:Thyroid Neoplasms / Q000201:enzymology* / Q000473:pathology*
D009363:Neoplasm Proteins; D000118:Acetylglucosaminidase