Oligosaccharide components of surface glycoproteins from leukemic lymphocytes of chronic lymphocytic leukemia and non-Hodgkin's lymphoma |
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Authors: | A E Roxburgh |
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Affiliation: | Haematology Research Unit, Peter MacCallum Cancer Institute, Melbourne, Victoria, Australia. |
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Abstract: | Oligosaccharide components of surface glycoproteins of leukemic cells have been studied in a group of eight patients with chronic lymphocytic leukemia (CLL) and non-Hodgkin's lymphoma (NHL). Labelled surface glycoproteins were separated by electrophoresis and treated with mild alkaline borohydride, prior to exclusion chromatography on Sephadex G-50. Five peaks were detected, of which peaks I and II consisted largely of N-linked chains and peaks III and IV of O-linked chains. Peak V contained monosaccharides and non-carbohydrate material. On both peripheral blood and lymph node cells of the CLL and nodular poorly differentiated lymphocytic lymphoma (NPDLL) patients studied, glycosylation was altered on leukocyte-common antigen (L-CA) forms of different relative molecular mass (Mr). The ratio of peak II oligosaccharides to those of peaks III and IV in different forms of L-CA correlated closely with Mr of the L-CA. Glycosylation of L-CA on cells of two patients with diffuse large cell lymphoma differed from that of the CLL and NPDLL patients, but was also to some extent related to Mr. Most of the oligosaccharides on the large sialoglycoprotein were O-linked, only a minor amount of N-linked being detected. Two surface glycoproteins of Mr 87 and 83 k differed markedly in their content of O- and N-linked chains. The specific glycosylation patterns described may have a role in control of cell behaviour and disease patterns of leukemia and lymphoma. |
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