Abstract
Based on the affinity for concanavalin A (Con A), human α1-acid glycoprotein (AGP) can be separated by chromatography on Con A-Sepharose gel into three variants: Con A unreactive AGP, Con A weakly reactive AGP, and Con A strongly reactive AGP. When exposed to native AGP or to its glycan variants, murine peritoneal macrophages released a factor that inhibited the interleukin-1 (IL-1) proliferative activity as measured in terms of the thymocyte comitogenic assay. Con A unreactive AGP, which contains tri- and tetraantennary glycans and no biantennae, proved to be more effective than Con A weakly and Con A strongly reactive variants, which contain one and two diantennary glycans, respectively. The inhibitory effect was not a function of the negative charge related to the sialyl residues and was not mediated by the maanosyl-fucosyl receptor.
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Bories, P.N., Feger, J., Benbernou, N. et al. Prevalence of tri- and tetraantennary glycans of humanα 1-acid glycoprotein in release of macrophage inhibitor of interleukin-1 activity. Inflammation 14, 315–323 (1990). https://doi.org/10.1007/BF00915815
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DOI: https://doi.org/10.1007/BF00915815