Receptor-mediated endocytosis of interleukin 2 in a human tumor T cell line. Degradation of interleukin 2 and evidence for the absence of recycling of interleukin receptors.
We have previously described a human tumor T cell line, IARC 301, which constitutively expresses biologically functional interleukin 2 (IL2) receptors. The fate of IL2 after binding to surface high affinity receptors was investigated. After a few minutes, IL2 is internalized at 37 degrees C and is subsequently degraded and released in the medium. The half-life for surface high affinity IL2 receptors, as measured in the presence of cycloheximide, is about 1 h and does not depend upon the presence of IL2. After trypsin digestion of cell surface high affinity receptors in the absence of protein biosynthesis, we could not detect any receptor reappearance on the cell membrane, whether IL2 was added or not. Taken together these results show that IL2 receptors are constantly internalized in these cells in the presence or absence of IL2 and that they do not recycle to the plasma membrane after receptor-mediated endocytosis.
D002460:Cell Line; D002462:Cell Membrane / Q000378:metabolism; D003513:Cycloheximide / Q000494:pharmacology; D004705:Endocytosis; D006207:Half-Life; D006801:Humans; D007376:Interleukin-2 / Q000502:physiology*; D008223:Lymphoma / Q000378:metabolism; D011971:Receptors, Immunologic / Q000187:drug effects / Q000378:metabolism*; D015375:Receptors, Interleukin-2; D013601:T-Lymphocytes / Q000378:metabolism*
D007376:Interleukin-2; D011971:Receptors, Immunologic; D015375:Receptors, Interleukin-2; D003513:Cycloheximide