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Departments of
* Human Oncology,
Molecular and Cellular Biology,
# Pediatrics, and
** Genetics, University of Wisconsin, and University of Wisconsin Comprehensive Cancer Center, Madison, Wisconsin;
H. Lee Moffitt Cancer Center and Research Institute, Tampa, Florida;
Promega Corp., Madison, Wisconsin; and
|| Arthritis and Rheumatoid Branch, National Institutes of Health, Bethesda, Maryland
Correspondence: Nancy L. Monson, Ph.D., Department of Neurology, University of Texas Southwestern Medical Center, Dallas, TX 75390-9036. E-mail: nancy.monson{at}utsouthwestern.edu
Functional forms of the IL-2, IL-4, IL-7, IL-9, and IL-15 receptors
require the
c receptor component. We have described previously a
myeloid cell line called Tf-1ß, which binds IL-2 with
intermediate-affinity and proliferates in response to IL-2. In this
study, we characterize
c expression on Tf-1ß2 cells, a derivative
of Tf-1ß cells stimulated exclusively with IL-2. Although Tf-1ß2
cells bind IL-2 with intermediate-affinity and proliferate in response
to IL-2, this cell line does not express the p64
c chain at the
protein level. This result was surprising because prior studies suggest
these cells should not be expected to proliferate in response to IL-2
or IL-15 in the absence of the p64
c chain. A p74 protein was
detected by western blot following immunoprecipitation with an
anti-
c polyclonal antibody, and a p74 protein was identified
consistently in complex with IL-2 and IL-15 on these cells. However,
the
c gene in these Tf-1ß2 cells shows no evidence of mutation by
sequence analysis. Furthermore, inhibition of glycosylation of these
Tf-1ß2 cells by tunicamycin treatment yields a standard 39-kDa
molecule recognized on western blot with anti-
c antibody, as seen
for the standard 64-kDa isoform of
c. These results demonstrate that
a 74-kDa
c receptor isoform was involved in the response of the
Tf-1ß2 cells to cytokines which normally interact with the 64-kDa
c chain.
Key Words: monocytes cytokines cytokine receptors signaling
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