Interferon β2/B‐Cell Stimulating Factor 2/Interleukin 6 Affects Glycosylation of Acute Phase Proteins in Human Hepatoma Cell Lines

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Abstract
Undefined monocyte-derived cytokines have previously been shown to affect glycan processing in glycoproteins secreted by human hepatoma cell lines. Hep 3B cells, when incubated with the cytokine interferon .beta.2/B-cell stimulating factor 2/interleukin 6, secreted forms of .alpha.1-protease inhibitor, ceruloplasmin, and .alpha.-fetoprotein with increased reactivity with concanavalin A (Con A) while incubation of Hep G2 cells with this cytokine led to secretion of forms of these proteins with decreased reactivity with Con A, reflecting changes in their oligosaccharide chains. The difference in response of these two transformed cell lines to this cytokine undoubtedly reflects differences in their intracellular glycan processing mechanisms. Changes in glycosylation patterns were dissociated from changes in rate of synthesis: this cytokine caused increased synthesis of .alpha.1-protease inhibitor and ceruloplasmin, and decreased synthesis of .alpha.-fetoprotein in both cell lines.

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