RESPONSE OF HUMAN OLIGODENDROCYTES TO INTERLEUKIN-2

Citation
Gc. Otero et Je. Merrill, RESPONSE OF HUMAN OLIGODENDROCYTES TO INTERLEUKIN-2, Brain, behavior, and immunity, 11(1), 1997, pp. 24-38
Citations number
44
Categorie Soggetti
Neurosciences,Immunology
ISSN journal
08891591
Volume
11
Issue
1
Year of publication
1997
Pages
24 - 38
Database
ISI
SICI code
0889-1591(1997)11:1<24:ROHOTI>2.0.ZU;2-U
Abstract
Interleukin 2 (IL-2) directly affects the function of both neurons and glia in the nervous system. It can induce proliferation and different iation or cause cell death in oligodendrocytes. We have previously clo ned the cDNAs for the alpha (alpha), beta (beta), and gamma (gamma) ch ains of the IL-2 receptor (IL-2R) complex from a human oligodendroglio ma cell line TC620. In an effort to characterize the IL-2 receptor (IL -2R) on oligodendrocytes, experiments were performed using recombinant human IL-2 on normal human oligodendrocytes from adult brain tissue a nd the IL-2-responsive subclone TC620.6A2 of the oligodendroglioma lin e. The TC620 subclone has the phenotype of an immature oligodendrocyte . At 5 nM IL-2, there was a 2.5-fold increase in proliferation of both normal and malignant human oligodendrocytes. This response was recept or-mediated in that binding of I-125-IL-2 to TC620.6A2 cells detected a single receptor class for IL-2 with an affinity of 3.6 nM. Immunohis tochemical staining of TC620.6A2 cells with a panel of monoclonal anti bodies to different epitopes of the human IL-2R alpha chain demonstrat ed the presence of IL-2R alpha on the surface of these cells, in stain ing patterns which did not always coincide with those found on T cells . Neither the beta nor the gamma chain of the IL-2R complex was detect ed on human oligodendrocytes by immunohistochemistry. Those antibodies which recognized cell surface IL-2R alpha epitopes on TC620.6A2 block ed IL-2-induced proliferation, while those which did not detect cell s urface IL-2R alpha epitopes were not inhibitory. This same panel of mo noclonal antibodies, when used to probe membrane preparations of TC620 .6A2 cells on a Western blot, defected three proteins of 100, 83, and 47 kDa, in contrast to the 55-kDa IL-2R alpha observed on T cells. (C) 1997 Academic Press.