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- W1969353460 abstract "The biosynthesis and secretion of human interleukin‐6 (IL‐6) was studied in monocyte cultures stimulated with endotoxin. After labeling with [ 35 S]methionine and immunoprecipitation with a specific antiserum one major (24 kDa) and four minor (27.5, 23.3, 22.5 and 21.8 kDa) molecular mass forms of IL‐6 could be found in the cells and media. Incubation of monocyte media with sialidase and subsequently with endo‐α‐ N ‐acetylgalactosaminidase, which cleaves Ga1(β1‐3)Gal‐NAc from serine or threonine, led to the formation of only two forms of IL‐6 with apparent molecular masses of 25 and 21.8 kDa. The latter had an electrophoretic mobility indistinguishable from that of 125 I‐labeled recombinant human IL‐6. The results suggest that human monocyte IL‐6 carries O ‐glycosidically bound carbohydrates with a Ga1(β1‐3)Gal‐NAc core to which only sialic acid is bound. Differences in O ‐glycosylation are the major cause for the molecular heterogeneity of IL‐6. A small part of IL‐6 (27.5 kDa form) is in addition N ‐glycosylated. Incubation of monocytes with tunicamycin and 1‐deoxymynnojirimycin and treatment of IL‐6 with endoglucosaminidase H suggested that the 27.5 kDa form of IL‐6 carries at least one N ‐linked complex‐type oligosaccharide chain." @default.
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- W1969353460 date "1989-04-24" @default.
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- W1969353460 title "<i>O</i>- and<i>N</i>-glycosylation lead to different molecular mass forms of human monocyte interleukin-6" @default.
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- W1969353460 doi "https://doi.org/10.1016/0014-5793(89)81361-4" @default.
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