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-Induced HLA-DR Expression1
,,,
*
Division of Molecular and Cellular Medicine, Department of Medicine, and
Department of Biochemistry, Albany Medical College, Albany, NY 12208; and
Veterans Affairs Healthcare Network Upstate New York, Albany, NY 12208
We have investigated the mechanism by which thyroid hormone
potentiates IFN-
-induced HLA-DR expression. IFN--induced HLA-DR
expression requires activation of STAT1
and induction of the Class
II trans-activator, CIITA. HeLa and CV-1 cells treated only with
L-thyroxine (T4) demonstrated increased
tyrosine phosphorylation and nuclear translocation (= activation) of
STAT1; this hormone effect on signal transduction, and
T4 potentiation of IFN--induced HLA-DR expression, were
blocked by the inhibitors CGP 41251 (PKC) and genistein (tyrosine
kinase). Treatment of cells with T4-agarose also caused
activation of STAT1. In the presence of IFN-, T4
enhanced cytokine-induced STAT1 activation. Potentiation by
T4 of IFN- action was associated with increased mRNA for
both CIITA and HLA-DR, with peak enhancement at 16 h (CIITA), and
2 d (HLA-DR). T4 increased IFN--induced HLA-DR
protein 2.2-fold and HLA-DR mRNA fourfold after 2 d. Treatment
with actinomycin D after induction of HLA-DR mRNA with IFN-, with or
without T4, showed that thyroid hormone decreased the
t1/2 of mRNA from 2.4 to 1.1 h. HeLa and
CV-1 cells lack functional nuclear thyroid hormone receptor.
Tetraiodothyroacetic acid (tetrac) and 3,5,3'-triiodo-thyroacetic acid
(triac) blocked T4 potentiation of IFN--induced HLA-DR
expression and T4 activation of STAT1. These studies
define an early hormone recognition step at the cell surface that is
novel, distinct from nuclear thyroid hormone receptor, and blocked by
tetrac and triac. Thus, thyroid hormone potentiation of IFN--induced
HLA-DR transcription is mediated by a cell membrane hormone binding
site, enhanced activation of STAT1, and increased CIITA induction.
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