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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 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 Citation Map 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. Related Collections Neoplasia Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Blood, 15 October 2002, Vol. 100, No. 8, pp. 3002-3007 NEOPLASIA Osteoprotegerin is bound, internalized, and degraded by multiple myeloma cells Therese Standal, Carina Seidel, Øyvind Hjertner, Torben Plesner, Ralph D. Sanderson, Anders Waage, Magne Borset, and Anders Sundan From the Institute of Cancer Research and Molecular Biology, Faculty of Medicine, Norwegian University of Science and Technology, Medisinsk Teknisk Senter, Trondheim, Norway; Department of Oncology, Division of Hematology, Vejle Hospital, Vejle, Denmark; and Arkansas Cancer Research Center and Departments of Pathology and Anatomy, University of Arkansas for Medical Science, Little Rock. Multiple myeloma (MM) is a hematologic malignancy characterized by accumulation of plasma cells in the bone marrow (BM). Bone destruction is a complication of the disease and is usually associated with severe morbidity. The balance between receptor activator of nuclear factor-B (NF-B) ligand and osteoprotegerin (OPG) is of major importance in bone homeostasis. We have recently shown that serum OPG levels are lower in patients with myeloma than in healthy individuals. Here we show that myeloma cells can bind, internalize, and degrade OPG, thereby providing a possible explanation for the lower levels of OPG in the BM of patients with MM. This process is dependent on interaction of OPG with heparan sulfates on the myeloma cells. The results suggest a novel biologic mechanism for the bone disease associated with MM and that treatment of the bone disease with OPG lacking the heparin-binding domain should be considered. © 2002 by The American Society of Hematology.   CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: S. 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