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Prepublished online as a Blood First Edition Paper on June 21, 2002; DOI 10.1182/blood-2002-04-1190. This Article Full Text (PDF) All Versions of this Article: 2002-04-1190v1 100/8/3002    most recent Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Standal, T. Articles by Sundan, A. Search for Related Content PubMed PubMed Citation Articles by Standal, T. Articles by Sundan, A. Social Bookmarking                   What's this? Submitted April 22, 2002 Accepted June 9, 2002 Osteoprotegerin is bound, internalized and degraded by multiple myeloma cells Therese Standal*, Carina Seidel, Oyvind Hjertner, Torben Plesner, Ralph D Sanderson, Anders Waage, Magne Borset, and Anders Sundan Institute of Cancer Research and Molecular Biology, Norwegian University of Science and Technology, Trondheim, Norway Department of Oncology, Division of Hematology, Vejle Hospital, Vejle, Denmark Arkansas Cancer Research Center and Departments of Pathology and Anatomy, University of Arkansas for Medical Science, Little Rock, AR, USA * Corresponding author; email: therese.standal{at}medisin.ntnu.no. Multiple myeloma is a hematological malignancy characterized by accumulation of plasma cells in the bone marrow. Bone destruction is a complication of the disease, and is usually associated with severe morbidity. The balance between receptor activator of NF-B ligand and osteoprotegerin is of major importance in bone homeostasis. We have recently shown that serum osteoprotegerin levels are lower in myeloma patients than in healthy individuals. Here we show that myeloma cells can bind, internalize and degrade osteoprotegerin, thereby providing a possible explanation for the lower levels of osteoprotegerin in the bone marrow of multiple myeloma patients. This process is dependent on interaction of OPG with heparan sulfates on the myeloma cells. The results suggest a novel biological mechanism for the bone disease associated with multiple myeloma, and that treatment of the bone disease with osteoprotegerin lacking the heparin binding domain should be considered. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: S. Kwan Tat, N. Amiable, J.-P. Pelletier, C. Boileau, D. Lajeunesse, N. Duval, and J. 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