Evidence that recombinant IL 1 alpha exhibits lectin-like specificity and binds to homogeneous uromodulin via N-linked oligosaccharides.
Uromodulin, a recently described immunosuppressive glycoprotein isolated from human pregnancy urine, has been shown to inhibit T cell proliferative assays dependent upon interleukin 1 (IL 1). We have also recently demonstrated that uromodulin binds specifically to IL 1. We now show that not only the biologic activity but also the binding affinity of uromodulin for recombinant IL 1 is dependent upon intact glycosylation. Furthermore, oligosaccharides isolated from pronase-digested uromodulin are immunosuppressive by themselves and are able to compete with native uromodulin for binding to IL 1. We conclude that recombinant IL 1 exhibits lectin-like specificity, and uromodulin is a biologically functional glycoprotein target of the lectin-like specificity of IL 1.
D002236:Carbohydrate Conformation; D006023:Glycoproteins / Q000378:metabolism*; D006801:Humans; D007108:Immune Tolerance; D007375:Interleukin-1 / Q000378:metabolism*; D037102:Lectins / Q000378:metabolism*; D009005:Monosaccharides / Q000494:pharmacology; D009088:Mucoproteins; D009844:Oligosaccharides / Q000378:metabolism*; D011257:Pregnancy Proteins / Q000378:metabolism*; D011485:Protein Binding / Q000187:drug effects; D011994:Recombinant Proteins / Q000378:metabolism; D058949:Uromodulin
D006023:Glycoproteins; D007375:Interleukin-1; D037102:Lectins; D009005:Monosaccharides; D009088:Mucoproteins; D009844:Oligosaccharides; D011257:Pregnancy Proteins; D011994:Recombinant Proteins; C548612:UMOD protein, human; D058949:Uromodulin