Re-examining the proposed lectin properties of IL-2.
Early work examining the interactions of IL-2 and the urinary glycoprotein uromodulin led to the suggestion that IL-2 was a lectin with specificity for high-mannose and mannan ligands. Subsequent studies have attributed various roles to these properties, some critical to the cell proliferative activity of IL-2. In an attempt to verify the reported interaction between IL-2 and mannose containing carbohydrate ligands we studied two biologically active forms of IL-2 using various techniques including affinity chromatography, equilibrium dialysis, and NMR methods. Despite previous reports we have not been able to demonstrate that IL-2 possesses the ability to bind carbohydrate.
Papalia
Giuseppe A
GA
Departments of Molecular and Medical Genetics and Biochemistry, University of Toronto, Toronto, Ontario, Canada M5S 1A8. jpapalia@cores.utah.edu
Rini
James M
JM
D001789:Blood Group Antigens / Q000737:chemistry / Q000378:metabolism; D002846:Chromatography, Affinity; D004797:Enzyme-Linked Immunosorbent Assay; D006801:Humans; D007376:Interleukin-2 / Q000737:chemistry / Q000378:metabolism*; D037102:Lectins / Q000737:chemistry / Q000378:metabolism*; D008024:Ligands; D009682:Magnetic Resonance Spectroscopy; D008351:Mannans; D008358:Mannose; D009088:Mucoproteins / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D058949:Uromodulin
D001789:Blood Group Antigens; D007376:Interleukin-2; D037102:Lectins; D008024:Ligands; D008351:Mannans; D009088:Mucoproteins; C548612:UMOD protein, human; D058949:Uromodulin; D008358:Mannose