Glycosylated Human Recombinant Interleukin-1α, Neo Interleukin-1α, with D-Mannose Dimer Exhibits Selective ActivitiesIn Vivo

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Abstract
To investigate the effect of carbohydrate-introduction on IL-1 activity, especially in vivo, and to develop IL-1 with less deleterious effects, recombinant human IL-1α was coupled with mannose dimer, α-D-Man-1-6-D-Man [Man2α(1-6)] by an acyl azide method. Previous studies demonstrated that the glycosylated IL-1 exhibited reduced activities compared with original IL-1 in all the experiments performed in vitro. In this study, we investigated the in vivo activities of Man2α(1-6)-conjugated IL-1α. The glycosylated IL-1α exhibited very low pyrogenic activity and α1-acid glycoprotein induction compared with untreated IL-1α. Untreated IL-1α increased the serum level of IL-6, but the glycosylated IL-1α did not. However, the glycosylated IL-1α possessed the same potency as untreated IL-1α in reduction of serum levels of glucose and triglyceride and in recovery of peripheral white blood cells in 5-fluorouracil-treated mice. Therefore, glycosylation of IL-1 appeared to be useful for the development of neoIL-1 with selective activity in vivo.