Unique antigen of cultured Hodgkin's cells. A putative sialyltransferase

E. Paietta, R. J. Stockert, A. G. Morell, V. Diehl, P. H. Wiernik

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Abstract

Hodgkin's disease-derived giant cell lines (HD-cells) express high levels of ectosialyltransferase activity presumed to be a galactose-specific lectin recognizing the desialylated 3-fucosyl-N-acetyllactosamine structure (X-hapten). Both the anti-X-hapten monoclonal antibody VIM-D5 and a polyclonal antiserum to another galactose-lectin, the hepatic asialoglycoprotein receptor (HBP), recognize a 55,000-mol wt HD-cell protein (Paietta, E., R.J. Stockert, A.G. Morell, V. Diehl, and P.H. Weirnik. 1986. Proc. Natl. Acad. Sci. USA. 83:3451-3455). That the expression of the 55,000-mol wt protein is restricted to HD-cells among X-hapten positive cell lines is confirmed in this study. The 55,000-mol wt protein is shown to be present on the cell surface and intracellularly, where an additional immunocrossreactive 150,000-mol wt protein is recognized. Extraction of the 55,000 mol wt protein from HD-cell lysates by affinity chromatography results in the loss of sialyltransferase activity. While evidence for a single protein possessing both the antigenic and the enzymatic activity is not direct, these results suggest that the ectosialyltransferase unique to HD-cells is a 55,000-mol wt membrane glycoprotein possessing the X-hapten oligosaccharide.

Original languageEnglish (US)
Pages (from-to)349-354
Number of pages6
JournalJournal of Clinical Investigation
Volume78
Issue number2
DOIs
StatePublished - Jan 1 1986

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ASJC Scopus subject areas

  • Medicine(all)

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