Osteoprotegerin is a receptor for the cytotoxic ligand TRAIL

J Biol Chem. 1998 Jun 5;273(23):14363-7. doi: 10.1074/jbc.273.23.14363.

J G Emery ¹, P McDonnell, M B Burke, K C Deen, S Lyn, C Silverman, E Dul, E R Appelbaum, C Eichman, R DiPrinzio, R A Dodds, I E James, M Rosenberg, J C Lee, P R Young

Affiliations

Affiliation

1 Department of Molecular Biology, King of Prussia, Pennsylvania 19406, USA.

PMID: 9603945 DOI: 10.1074/jbc.273.23.14363

Abstract

TRAIL is a tumor necrosis factor-related ligand that induces Apoptosis upon binding to its death domain-containing receptors, DR4 and DR5. Two additional TRAIL receptors, TRID/DcR1 and DcR2, lack functional death domains and function as decoy receptors for TRAIL. We have identified a fifth TRAIL receptor, namely Osteoprotegerin (OPG), a secreted tumor necrosis factor receptor homologue that inhibits osteoclastogenesis and increases bone density in vivo. OPG-Fc binds TRAIL with an affinity of 3.0 nM, which is slightly weaker than the interaction of TRID-Fc or DR5-Fc with TRAIL. OPG inhibits TRAIL-induced Apoptosis of Jurkat cells. Conversely, TRAIL blocks the anti-osteoclastogenic activity of OPG. These data suggest potential cross-regulatory mechanisms by OPG and TRAIL.

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