Date of Award
Master of Science
Dr. Leonard C. Ginsberg
Masters Thesis-Open Access
Interleukin-1 (IL-1) demonstrated a concentration dependent, specific binding to the human, large granular lymphocyte cell line, YT.NCI with a dissociation constant of 0.2 nM. There were approximately 500 IL-1 receptors/cell.
IL-1 binding to YT.NCI cells could be inhibited by unlabeled-IL-1 and the plant lectins, WGA and Con A. Lectin inhibition of IL-1 binding could be completely abrogated by exposing lectins to specific simple sugars prior to the addition of ligand.
Tunicamycin, an inhibitor of glycosylation, decreased IL-l binding to YT cells in a reversible, time- and concentration-dependent manner.
These observations suggest that glycosylation of cell surface proteins may be important for IL-1 receptor orientation, expression, and/or functional ligand binding. Furthermore, the demonstration that specific plant lectins effectively compete with iodinated IL-1 for IL-1 receptor occupancy could facilitate the establishment of conditions for successful isolation and purification of IL-1 membrane receptors via affinity chromatography on immobilized lectins.
Speziale, Susan Catherine, "Characteristics of Binding of Interleukin-1 to YT.NCI Cells" (1988). Master's Theses. 1173.