{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,17]],"date-time":"2026-10-17T17:14:41Z","timestamp":1792257281716,"version":"4.4.0"},"reference-count":45,"publisher":"American Physiological Society","issue":"5","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["American Journal of Physiology-Cell Physiology"],"published-print":{"date-parts":[[1999,5,1]]},"abstract":"<jats:p> Thyroid hormone [l-thyroxine (T<jats:sub>4<\/jats:sub>)] rapidly induced phosphorylation and nuclear translocation (activation) of mitogen-activated protein kinase (MAPK) in HeLa and CV-1 cells in the absence of cytokine or growth factor. A pertussis toxin-sensitive and guanosine 5\u2032- O-(3-thiotriphosphate)-sensitive cell surface mechanism responsive to T<jats:sub>4<\/jats:sub> and agarose-T<jats:sub>4<\/jats:sub>, suggesting a G protein-coupled receptor, was implicated. Cells depleted of MAPK or treated with MAPK pathway inhibitors showed reduced activation of MAPK and of the signal transducer and activator of transcription STAT1\u03b1 by T<jats:sub>4<\/jats:sub>; they also showed reduced T<jats:sub>4<\/jats:sub> potentiation of the antiviral action of interferon-\u03b3 (IFN-\u03b3). T<jats:sub>4<\/jats:sub> treatment caused tyrosine-phosphorylated MAPK-STAT1\u03b1 nuclear complex formation and enhanced Ser-727 phosphorylation of STAT1\u03b1, in the presence or absence of IFN-\u03b3. STAT1\u03b1-deficient cells transfected with STAT1\u03b1 containing an alanine-for-serine substitution at residue 727 (STAT1\u03b1<jats:sub>A727<\/jats:sub>) showed minimal T<jats:sub>4<\/jats:sub>-stimulated STAT1\u03b1 activation. IFN-\u03b3 induced the antiviral state in cells containing wild-type STAT1\u03b1 (STAT1\u03b1<jats:sub>wt<\/jats:sub>) or STAT1\u03b1<jats:sub>A727<\/jats:sub>; T<jats:sub>4<\/jats:sub> potentiated IFN-\u03b3 action in STAT1\u03b1<jats:sub>wt<\/jats:sub> cells but not in STAT1\u03b1<jats:sub>A727<\/jats:sub> cells. 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