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Originally published In Press as doi:10.1074/jbc.M111013200 on May 8, 2002

J. Biol. Chem., Vol. 277, Issue 31, 28109-28117, August 2, 2002
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Both N- and C-terminal Domains of Parathyroid Hormone-related Protein Increase Interleukin-6 by Nuclear Factor-kappa B Activation in Osteoblastic Cells*

Carlos GuillénDagger §, Pilar Martínez||, Arancha R. de GortázarDagger §, María Eugenia Martínez, and Pedro EsbritDagger **

From the Dagger  Bone and Mineral Metabolism Laboratory, Research Unit, Fundación Jiménez Díaz, 28040 Madrid, and the  Biochemistry Division, Hospital La Paz, 28046 Madrid, Spain

Parathyroid hormone (PTH)-related protein (PTHrP) seems to affect bone resorption by interaction with bone cytokines, among them interleukin-6 (IL-6). Recent studies suggest that nuclear factor (NF)-kappa B activation has an important role in bone resorption. We assessed whether the N-terminal fragment of PTHrP, and its C-terminal region, unrelated to PTH, can activate NF-kappa B, and its relationship with IL-6 gene induction in different rat and human osteoblastic cell preparations. Here we present molecular data demonstrating that both PTHrP (1-36) and PTHrP (107-139) activate NF-kappa B, leading to an increase in IL-6 mRNA, in these cells. Using anti-p65 and anti-p50 antibodies, we detected the presence of both proteins in the activated NF-kappa B complex. This effect induced by either the N- or C-terminal PTHrP domain in osteoblastic cells appears to occur by different intracellular mechanisms, involving protein kinase A or intracellular Ca2+/protein kinase C activation, respectively. However, the effect of each peptide alone did not increase further when added together. Our findings lend support to the hypothesis that the C-terminal domain of PTHrP, in a manner similar to its N-terminal fragment, might stimulate bone resorption. These studies also provide further insights into the putative role of PTHrP as a modulator of bone remodeling.

* This work was supported in part by Spanish Ministry of Health Grants FIS 00/0125 and 00/0534 and by a Fundación Española de Productos Químicos y Farmacéuticos (Bilbao, Spain) award. Portions of this work were presented at the 27th European Symposia on Calcified Tissues May 6-10, 2000 in Tampere, Finland, and at the 1st Joint Meeting of the International Bone and Mineral Society and the European Calcified Tissue Society June 5-10, 2001 in Madrid, Spain.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Predoctoral fellow of the Conchita Rábago Foundation, Madrid, Spain.

|| Postdoctoral fellow of the research unit at La Paz Hospital.

** To whom correspondence should be addressed: Bone and Mineral Metabolism Laboratory, Research Unit, Fundación Jiménez Díaz, Avda. Reyes Católicos 2, 28040 Madrid, Spain. E-mail: pesbrit@fjd.es.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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