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Am J Physiol Endocrinol Metab 280: E405-E412, 2001;
0193-1849/01 $5.00
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Vol. 280, Issue 3, E405-E412, March 2001

Parathyroid hormone induces hepatic production of bioactive interleukin-6 and its soluble receptor

Mary Ann Mitnick1, Andrew Grey1, Urszula Masiukiewicz1, Marcjanna Bartkiewicz1, Laura Rios-Velez1, Scott Friedman2, Lieming Xu2, Mark C. Horowitz1, and Karl Insogna1

1 Yale University School of Medicine, New Haven, Connecticut 06520; and 2 Division of Liver Diseases, Mount Sinai School of Medicine, New York, New York 10092

Interleukin-6 (IL-6) is an important mediator of parathyroid hormone (PTH)-induced bone resorption. Serum levels of IL-6 and its soluble receptor (IL-6sR) are regulated in part by PTH. The PTH/PTH-related protein type 1 receptor is highly expressed in the liver, and in the current study we investigated whether the liver produces IL-6 or IL-6sR in response to PTH. Perfusion of the isolated rat liver with PTH-(1-84) stimulated rapid, dose-dependent production of bioactive IL-6 and the IL-6sR. These effects were observed at near physiological concentrations of the hormone such that 1 pM PTH induced hepatic IL-6 production at a rate of ~0.6 ng/min. In vitro, hepatocytes, hepatic endothelial cells, and Kupffer cells, but not hepatic stellate cells, were each found to produce both IL-6 and IL-6sR in response to higher (10 nM) concentrations of PTH. Our data suggest that hepatic-derived IL-6 and IL-6sR contribute to the increase in circulating levels of these cytokines induced by PTH in vivo and raise the possibility that PTH-induced, liver-derived IL-6 may exert endocrine effects on tissues such as bone.

cytokines, hepatocytes, hepatic endothelial cells, Kupffer cells, bone


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