Osteoprotegerin: Multiple partners for multiple functions

被引：151

作者：

Baud'huin, Marc ^{[1
,2
,3
]}

Duplomb, Laurence ^{[4
]}

Teletchea, Stephane ^{[1
,2
]}

Lamoureux, Francois ^{[1
,2
]}

Ruiz-Velasco, Carmen ^{[1
,2
]}

Maillasson, Mike ^{[5
,6
]}

Redini, Francoise ^{[1
,2
,3
]}

Heymann, Marie-Francoise ^{[1
,2
,3
]}

Heymann, Dominique ^{[1
,2
,3
]}

机构：

[1] INSERM, UMR957, F-44035 Nantes 1, France

[2] Univ Nantes, Nantes Atlantique Uniiv, Lab Physiopathol Resorpt Osseuse & Therapie Tumeu, F-44035 Nantes, France

[3] CHU Nantes, Hotel Dieu, F-44035 Nantes 01, France

[4] Univ Bourgogne, Equipe Genet Anomalies Dev, Equipe Accueil 4271, F-21079 Dijon, France

[5] INSERM, UMR892, F-44035 Nantes, France

[6] SFR Bonamy Ouest Genopole, F-44035 Nantes, France

来源：

CYTOKINE & GROWTH FACTOR REVIEWS | 2013年 / 24卷 / 05期

关键词：

Osteoprotegerin; Glycosaminoglycans; Monocytes; Cell adhesion; VON-WILLEBRAND-FACTOR; OSTEOCLASTOGENESIS-INHIBITORY FACTOR; ENDOTHELIAL-CELLS; CRYSTAL-STRUCTURE; SURVIVAL FACTOR; RECEPTOR ACTIVATOR; DECOY RECEPTOR; CANCER CELLS; ONCOSTATIN-M; BONE-TUMORS;

D O I：

10.1016/j.cytogfr.2013.06.001

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

070307 [化学生物学]; 071010 [生物化学与分子生物学];

摘要：

Osteoprotegerin (OPG) is an essential secreted protein in bone turnover due to its role as a decoy receptor for the Receptor Activator of Nuclear Factor-kB ligand (RANKL) in the osteoclasts, thus inhibiting their differentiation. However, there are additional ligands of OPG that confer various biological functions. OPG can promote cell survival, cell proliferation and facilitates migration by binding TNF-related apoptosis inducing ligand (TRAIL), glycosaminoglycans or proteoglycans. A large number of in vitro, preclinical and clinical studies provide evidences of OPG involvement in vascular, bone, immune and tumor biology. This review describes an overview of the different OPG ligands regulating its biological functions. (C) 2013 Elsevier Ltd. All rights reserved.

引用

页码：401 / 409

页数：9

共 82 条

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Identification of amino acid residues essential for heparin binding by the A1 domain of human von Willebrand factor [J].