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Am J Physiol Cell Physiol 273: C1225-C1232, 1997;
0363-6143/97 $5.00
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Vol. 273, Issue 4, C1225-C1232, October 1997

Protein synthesis-dependent potentiation by thyroxine of antiviral activity of interferon-gamma

Hung-Yun Lin, Paul M. Yen, Faith B. Davis, and Paul J. Davis

Department of Medicine, Albany Medical College and Stratton Veterans Affairs Medical Center, Albany, New York 12208; and Division of Genetics, Department of Medicine, Brigham and Women's Hospital and Harvard Medical School, Boston, Massachusetts 02115

We have studied the prenuclear signal transduction pathway by which thyroid hormone potentiates the antiviral activity of human interferon-gamma (IFN-gamma ) in HeLa cells, which are deficient in thyroid hormone receptor (TR). The action of thyroid hormone was compared with that of milrinone, which has structural homologies with thyroid hormone. L-Thyroxine (T4), 3,5,3'-L-triiodothyronine (T3), and milrinone enhanced the antiviral activity of IFN-gamma up to 100-fold, a potentiation blocked by cycloheximide. The 5'-deiodinase inhibitor 6-n-propyl-2-thiouracil did not block the T4 effect. 3,3',5,5'-Tetraiodothyroacetic acid prevented the effect of T4 but not of milrinone. The effects of T4 and milrinone were blocked by inhibitors of protein kinases C (PKC) and A (PKA) and restored by PKC and PKA agonists; only the effect of T4 was blocked by genistein, a tyrosine kinase inhibitor. In separate models, milrinone was shown not to interact with nuclear TR-beta . T4 potentiation of the antiviral activity of IFN-gamma requires PKC, PKA, and tyrosine kinase activities but not traditional TR.

thyroid hormone action; protein kinase C; protein kinase A; tyrosine kinase


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