Differences in glycosylation of intracellular proteins between benign and malignant thyroid neoplasms.
Differences in glycosylation of nuclear and cytosolic proteins isolated from benign and malignant human thyroid neoplasms were analyzed by lectin blotting and enzyme linked lectino-solid-phase assay using Erythrina cristagalli and Ricinus communis agglutinins. The results reported in this study have not shown any significant differences in lectin binding by nuclear proteins of benign and malignant tumors, however, quantitative and qualitative differences were observed in the patterns of cytosolic glycoproteins. In the majority of carcinomas samples lectin binding to cytosolic proteins was definitely weaker in comparison with adenomas and non-neoplastic specimens, which suggested alterations in glycosylation of cytosolic proteins in malignant tumors.
Krześlak
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Department of Cytobiochemistry, University of Lódz, S. Banacha 12/16, 90-237 Lódź, Poland.
Pomorski
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Gaj
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Lipińska
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D000293:Adolescent; D000328:Adult; D000368:Aged; D004797:Enzyme-Linked Immunosorbent Assay; D005260:Female; D006023:Glycoproteins / Q000378:metabolism*; D006031:Glycosylation; D006801:Humans; D008297:Male; D008875:Middle Aged; D037121:Plant Lectins / Q000494:pharmacology*; D013964:Thyroid Neoplasms / Q000378:metabolism* / Q000473:pathology
D006023:Glycoproteins; D037121:Plant Lectins