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Originally published In Press as doi:10.1074/jbc.M010153200 on March 23, 2001

J. Biol. Chem., Vol. 276, Issue 23, 20659-20672, June 8, 2001
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Receptor Activator of NF-kappa B and Osteoprotegerin Expression by Human Microvascular Endothelial Cells, Regulation by Inflammatory Cytokines, and Role in Human Osteoclastogenesis*

Patricia Collin-OsdobyDagger §, Linda RotheDagger , Fred AndersonDagger , Maureen NelsonDagger , William Maloney||, and Philip OsdobyDagger §

From the Dagger  Department of Biology, Washington University, St. Louis, Missouri 63130, the § Division of Bone and Mineral Metabolism, Washington University Medical School, and the || Department of Orthopedics, Washington University Medical School, St. Louis, Missouri 63110

The receptor activator of NF-kappa B (RANKL) is the essential signal required for full osteoclast (OC) development, activation, and survival. RANKL is highly expressed in areas of trabecular bone remodeling and inflammatory bone loss, is increased on marrow stromal cells or osteoblasts by osteotropic hormones or cytokines, and is neutralized by osteoprotegerin (OPG), a soluble decoy receptor also crucial for preventing arterial calcification. Vascular endothelial cells (VEC) are critically involved in bone development and remodeling and influence OC recruitment, formation, and activity. Although OCs develop and function in close association with bone VEC and sinusoids, signals mediating their interactions are not well known. Here, we show for the first time that human microvascular endothelial cells (HMVEC) express transcripts for both RANKL and OPG; inflammatory cytokines tumor necrosis factor-alpha and interleukin-1alpha elevate RANKL and OPG expression 5-40-fold in HMVEC (with an early OPG peak that declines as RANKL rises), and RANKL protein increases on the surface of tumor necrosis factor-alpha -activated HMVEC. Cytokine-activated HMVEC promoted the formation, fusion, and bone resorption of OCs formed in co-cultures with circulating human monocytic precursors via a RANKL-mediated mechanism fully antagonized by exogenous OPG. Furthermore, paraffin sections of human osteoporotic fractured bone exhibited increased RANKL immunostaining in vivo on VEC located near resorbing OCs in regions undergoing active bone turnover. Therefore, cytokine-activated VEC may contribute to inflammatory-mediated bone loss via regulated production of RANKL and OPG. VEC-derived OPG may also serve as an autocrine signal to inhibit blood vessel calcification.

* This work was supported by National Institutes of Health Grants DK46547 (to P. C. O.) and AR32927 (to P. O.).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.

To whom correspondence and reprint requests should be addressed: Dept. of Biology, Box 1229, Washington University, St. Louis, MO 63130. Tel.: 314-935-5304; Fax: 314-935-5134; E-mail: collin@biology.wustl.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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