PMID: 6979338Feb 1, 1982Paper

Glycoprotein biosynthesis in quiescent and stimulated thymocytes and a T-cell lymphoma

The Biochemical Journal
C A Rupar, G M Cook

Abstract

Quiescent thymocytes, mitogen-stimulated thymocytes and acute-leukaemic lymphoblasts provide a model for the study of protein glycosylation in quiescent cells, mitotically active non-malignant and malignant cells respectively. The biosynthesis of both complex and high-mannose-type oligosaccharides was monitored by metabolic labelling with [6-3]fucose and [2-3H]mannose. Bio-Gel P6 elution profiles of [6-3H]fucose-labelled glycopeptides showed that quiescent thymocytes and stimulated thymocytes synthesized qualitatively and quantitatively similar glycopeptides; however, higher-molecular-weight glycopeptides were synthesized by the acute-leukaemic lymphoblasts. The amount of [2(-3)H]mannose incorporated into glycopeptide by quiescent thymocytes was less than 10% of that incorporated by stimulated thymocytes. The Bio-Gel P6 elution profile of [2(-3)H]mannose-labelled glycopeptides from acute leukaemic lymphoblasts was qualitatively similar to that of stimulated thymocytes, with about 40% of the radioactivity incorporated into one glycopeptide peak. This glycopeptide was characterized by Bio-Gel P6 and concanavalin A affinity chromatography, radioactive-sugar analysis, sensitivity to alpha-mannosidase and endoglycosidase H and resis...Continue Reading

Citations

Sep 1, 1983·Journal of Clinical Pathology·G T BesleyA E Dewar
Jan 31, 2009·Veterinary and Comparative Oncology·C R WilsonS B Hooser
Mar 22, 1984·Biochimica Et Biophysica Acta·S Kato, N Akamatsu

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