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TNFRSF11B (tumor necrosis factor receptor superfamily, member 11b)

Identity

Other namesMGC29565
OCIF
OPG
Osteoprotegerin
TR1
HGNC (Hugo) TNFRSF11B
LocusID (NCBI) 4982
Location 8q24.12
Location_base_pair Starts at 119935796 and ends at 119964383 bp from pter ( according to hg19-Feb_2009)  [Mapping]

DNA/RNA

 
  Organization of the human OPG gene.
Description START: 120,004,977 BP from PTER
END: 120,033,492 BP from PTER
SIZE: 28,516 bases
ORIENTATION: Minus strand
REFSEQ GENOMIC ASSEMBLIES: NC-000008.9 NT-008046.15
Transcription 5 exons; cDNA SIZE 2354 BP (NM-002546); CDS: 1206 nt.
Pseudogene No known pseudogenes.

Protein

Note RefSeq NP-002537.3; Size: 401 amino acids; 46040 Da; Subunit: Homodimer; Subcellular location: Secreted.
Osteoprotegerin (OPG) was isolated independently by two laboratories in 1997 (Tsuda et al., 1997; Simonet et al., 1997), as being a protein that exhibits a protective effect on bone. OPG is a member of the TNF-receptor superfamily, which consists of proteins that evoke different signal transduction, mediating several biological responses, such as cytotoxicity, apoptosis and cell survival, proliferation and differentiation. OPG has two known TNF family ligands: receptor activator of NF-kB ligand (RANKL) (Yasuda et al., 1998b) and TRAIL (Emery et al.,1998) (Diagram 1). RANKL normally binds to its membrane receptor RANK inducing differentiation, activation, and survival of osteoclasts. By binding to RANKL, OPG acts as a soluble inhibitor that prevents RANKL/RANK interaction and subsequent osteoclastogenesis (Yasuda et al., 1998b) (Diagram 1). However, it has been reported that also OPG binding to TRAIL inhibits TRAIL/TRAIL-receptors (TR-R1/R2) interaction, as revealed by the inhibition of TRAIL-induced apoptosis (Emery et al.,1998) (Diagram 1). Vice-versa, TRAIL can block the inhibitory activity of OPG on osteoclastogenesis (Emery et al.,1998).
 
  Diagram 1. Schematic representation of OPG/OPG-ligands and cellular processes inhibited from their interactions.
Diagram 2. Schematic representation of the structure of OPG protein.
Description OPG comprises 401 amino acids of which 21 are a signal peptide which is cleaved, generating a mature form of 380 amino acids. OPG is produced as a monomer (55-62 kDa), but undergoes homodimerization and is secreted as a disulphide-linked homodimeric glycoprotein with four or five potential glycosylation sites, generating a mature form of OPG of 110-120 kDa (Yamaguchi et al., 1998). OPG consists of 7 structural domains, of which the amino-terminal cysteine rich domains 1 to 4 (D1-D4) are necessary for binding to RANKL (Schneeweis et al., 2005) and share some features with the extracellular domains of other members of the TNF-receptor family (Diagram 2) (Baker et al., 1998). The carboxy-terminal portion of the protein contains two putative death domain homologous regions (D5 and D6). Finally, domain 7 (D7) harbors a heparin-binding region, a common feature of peptide growth factors and signal molecules, as well as an unpaired cysteine residue, at position 400, required for disulfide bond formation and dimerization (Diagram 2) (Yamaguchi et al., 1998). It is the dimeric form of the protein, which has the highest heparin-binding capacity and also the highest hypocalcemic ability.
Expression OPG is expressed ubiquitously and abundantly in many tissues and cell types. First of all it is produced from osteoblasts (Wada et al., 2006), where its expression is regulated by most of the factors that induce RANKL expression by osteoblasts. Although there are contradictory data, in general upregulation of RANKL is associated with downregulation of OPG, or at least lower induction of OPG, such that the ratio of RANKL to OPG changes in favor of osteoclastogenesis. Many reports have supported the assertion that the RANKL/OPG ratio is a major determinant of bone mass (Hofbauer et al., 2004). Concerning the cellular sources of OPG, it has been shown that besides cells belonging to the osteoblastic lineage, also bone marrow stromal cells (reviewed in Theoleyre et al., 2004), hematopoietic and immune cells (B cells and dendritic cells) (Tan et al., 1997) produce and release OPG. Importantly, OPG is also produced by endothelial (Collin-Osdoby et al., 2001) and vascular smooth muscle cells (Olesen et al., 2005), which likely represent the major contributors to the circulating pool of OPG. Recent studies on the intracellular localization of OPG in endothelial cells have indicated that OPG protein is found in the Weibel-Palade Bodies (WPB), in physical association with von Willebrand Factor (Zannettino et al., 2005).
Finally, OPG is produced by a variety of tissues including the cardiovascular system (heart, arteries, veins), lung, kidney, liver, spleen, intestine, stomach (Simonet et al., 1997; Wada et al., 2006).
Localisation OPG, unlike all other receptors of the family, lacks a transmembrane and cytoplasmic domain and is secreted as a soluble protein (Yamaguchi et al., 1998). It has also been detected in a cell surface-associated form with some cell types (Yun et al., 1998), although sequence analysis failed to detect a classical hydrophobic transmembrane domain.
Function The best characterized activity of OPG is the inhibition of osteoclast differentiation and activity (Simonet et al., 1997; Yasuda et al., 1998a), by binding to RANKL. Initially, the physiological roles of OPG have been revealed by studies in OPG knockout mice, produced by targeted disruption of the gene (Bucay et al., 1998; Mizuno et al.,1998). OPG (-/-) mice were viable and fertile, but they exhibited severe osteoporosis caused by enhanced osteoclast formation and function. These results have indicated that OPG is a physiological regulator of osteoclast-mediated bone resorption during postnatal bone growth.
In the context of vascular system, it has been reported that exposure of both micro and macro-vascular endothelial cells to the inflammatory cytokines elevates OPG expression and release (Collin-Osdoby et al., 2001; Secchiero et al., 2006), and OPG in turn promotes leukocyte adhesion (Zauli et al., 2007; Mangan et al., 2007), acting as a chemotactic factor for monocyte. These observations strongly support a modulatory role of OPG in hemostasis, vascular injury and inflammation, suggesting an involvement of OPG in the inflammatory functions of endothelial cells, with endothelium acting as both cellular source and target of vascular OPG production. In this respect, there are accumulating data in vitro indicating a role for OPG in endothelial cell biology and angiogenesis; in particular in the regulation of endothelial cell survival (Scatena et al., 2002; Pritzker et al., 2004), stimulation of endothelial cell growth, as well as the formation of cord-like structures on a matrigel substrate (Cross et al., 2006), providing the evidence that OPG may modulate also endothelial cell migration and differentiation. In this context, OPG also appears to protect large blood vessels from medial calcification, based on the observation of renal and aortic calcification occurring in OPG knockout mice (Bucay et al., 1998). Furthermore, the absence of OPG in OPG/apolipoprotein E double knockout mice accelerates the calcific atherosclerosis that develops in apolipoprotein E knockout mice, suggesting that OPG protects against this complication of atherosclerosis (Bennett et al., 2006).
Moreover, OPG has also been shown to regulate B-cell development and function and dendritic cell function (Yun et al., 1998; Yun et al., 2001), making OPG a paracrine mediator of both bone metabolism and immune functions.
 
  For details see: http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=Retrieve&db=homologene&dopt=AlignmentScores&list_uids=1912

Mutations

Note http://www.ncbi.nlm.nih.gov/sites/entrez (look for TNFRSF11B into dbSNP)
 
  11 Esonic variations
For details see: http://www.ncbi.nlm.nih.gov/SNP/snp_ref.cgi?locusId=4982

Implicated in

Entity Cancer
Note A potential role of full-lenght OPG in tumor cell biology is supported by different studies that have investigated the OPG serum levels, OPG tissue expression and OPG polymorphisms in cancer patients. In fact, it has been shown that the serum levels of OPG are elevated in a variety of human malignancies, in particular in patients with more advanced cancer. Of note, OPG levels were increased in the serum of patients with prostate or breast cancer metastatized to the bone (Lipton et al., 2001). Surprisingly, OPG serum levels were elevated also in other types of tumors, which do not show a preferential tropism for bone, such as B cell lymphomas (Lipton et al., 2001), but also in patients with bladder carcinoma (Mizutani et al., 2004), where OPG levels were found to be associated with high tumour stage and grade. After a follow up period of 5 years, patients who had low serum OPG levels had a longer post-operative tumour-free interval and increased survival compared with patients with high levels of serum OPG (Mizutani et al., 2004), suggesting that serum OPG correlates with tumour stage and is also predictive of early recurrence of bladder carcinoma.
Moreover, in different studies, it was shown that OPG is overexpressed in epithelial carcinomas of the gastroenteric tract (Ito et al., 2003; Pettersen et al., 2005). In particular, it was reported a significant correlation between OPG expression and tumor stage, suggesting that OPG expression may be a marker of aggressive gastric carcinomas. In addition, investigation of various human cancers demonstrated that OPG is highly expressed by endothelial cells in the majority of malignant tumors examined (60% of malignant tumors), although endothelial cells in benign tumors do not express high levels of OPG. In particular, in breast cancers endothelial expression of OPG seems to be associated with increasing tumor grade (Cross et al., 2006). Taken together, these observations suggest that the increased levels of OPG expression may be associated with tumor development and/or progression.
Finally, a recent study has addressed the possible role of OPG promoter polymorphisms as genetic modifiers in the etiology of prostate cancer and disease progression (Narita et al., 2008). Patients affected by prostate cancer with TC and TT genotypes in the 950 T/C polymorphism had a significantly increased risk of extraprostatic and metastatic disease compared with those with the CC genotype. In addition, analysis of the metastatic prostatic cancer patients showed that the presence of the T allele of the OPG 950 T/C polymorphism was an independent risk factor, predicting survival by Cox proportional hazard regression analyses (Narita et al., 2008).
  
Entity Vascular diseases
Note A growing number of experimental data have demonstrated that the serum levels of OPG are significantly increased in both diabetic and non-diabetic patients affected by coronary artery disease (Jono et al., 2002; Schoppet et al., 2003; Avignon et al., 2005; Rasmussen et al., 2006), with a strong association between levels of OPG and the presence and severity of coronary artery disease (Browner et al., 2001). Serum OPG levels have shown to have prognostic value in heart failure after acute myocardial infarction as well as in patients affected by abdominal aortic aneurysm and peripheral artery disease (Karan et al., 2005; Ziegler et al., 2005). Remarkably, two OPG genetic polymorphisms have been associated with an increased risk of coronary artery disease in Caucasian men, and serum OPG levels correlated with one of these polymorphisms (Soufi et al., 2004). Thus, these studies strongly indicate that serum OPG levels frequently rise in clinical conditions that favor vascular dysfunction or atherosclerosis. In this respect, the presence of OPG has been documented in atherosclerotic lesions (Schoppet et al., 2004). Moreover, in a large observational study, plasma concentrations of OPG were higher in diabetic than in non-diabetic subjects, in particular in diabetic patients with vascular complications (Knudsen et al., 2003), suggesting that elevated levels of OPG may reflect vascular damage among patients with diabetes rather than the diabetic state per se.
At present it is unclear whether OPG plays a pathogenetic or compensatory role in the vascular dysfunction and atherosclerosis. However, the ability of recombinant OPG to enhance the recruitment and infiltration of monocyte/macrophages ( Mosheimer et al., 2005) is particularly noteworthy in the hypothesis that an abnormal and prolonged elevation of OPG levels may be involved in the devolopment of vascular dysfunction.
  

External links

Nomenclature
HGNC (Hugo)TNFRSF11B   11909
Cards
AtlasTNFRSF11BID42610ch8q24
Entrez_Gene (NCBI)TNFRSF11B  4982  tumor necrosis factor receptor superfamily, member 11b
GeneCards (Weizmann)TNFRSF11B
Ensembl hg19 (Hinxton)ENSG00000164761 [Gene_View]  chr8:119935796-119964383 [Contig_View]  TNFRSF11B [Vega]
Ensembl hg38 (Hinxton)ENSG00000164761 [Gene_View]  chr8:119935796-119964383 [Contig_View]  TNFRSF11B [Vega]
ICGC DataPortalENSG00000164761
cBioPortalTNFRSF11B
AceView (NCBI)TNFRSF11B
Genatlas (Paris)TNFRSF11B
WikiGenes4982
SOURCE (Princeton)TNFRSF11B
Genomic and cartography
GoldenPath hg19 (UCSC)TNFRSF11B  -     chr8:119935796-119964383 -  8q24   [Description]    (hg19-Feb_2009)
GoldenPath hg38 (UCSC)TNFRSF11B  -     8q24   [Description]    (hg38-Dec_2013)
EnsemblTNFRSF11B - 8q24 [CytoView hg19]  TNFRSF11B - 8q24 [CytoView hg38]
Mapping of homologs : NCBITNFRSF11B [Mapview hg19]  TNFRSF11B [Mapview hg38]
OMIM239000   602643   
Gene and transcription
Genbank (Entrez)AB002146 AF134187 AK223155 AK308524 AK313710
RefSeq transcript (Entrez)NM_002546
RefSeq genomic (Entrez)AC_000140 NC_000008 NC_018919 NG_012202 NT_008046 NW_001839136 NW_004929340
Consensus coding sequences : CCDS (NCBI)TNFRSF11B
Cluster EST : UnigeneHs.81791 [ NCBI ]
CGAP (NCI)Hs.81791
Alternative Splicing : Fast-db (Paris)GSHG0029813
Alternative Splicing GalleryENSG00000164761
Gene ExpressionTNFRSF11B [ NCBI-GEO ]     TNFRSF11B [ SEEK ]   TNFRSF11B [ MEM ]
SOURCE (Princeton)Expression in : [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
Protein : pattern, domain, 3D structure
UniProt/SwissProtO00300 (Uniprot)
NextProtO00300  [Medical]
With graphics : InterProO00300
Splice isoforms : SwissVarO00300 (Swissvar)
Domaine pattern : Prosite (Expaxy)TNFR_NGFR_1 (PS00652)    TNFR_NGFR_2 (PS50050)   
Domains : Interpro (EBI)DEATH-like_dom    Death_domain    TNFR/NGFR_Cys_rich_reg    TNFR_11    TNFR_11B   
Related proteins : CluSTrO00300
Domain families : Pfam (Sanger)Death (PF00531)    TNFR_c6 (PF00020)   
Domain families : Pfam (NCBI)pfam00531    pfam00020   
Domain families : Smart (EMBL)TNFR (SM00208)  
DMDM Disease mutations4982
Blocks (Seattle)O00300
PDB (SRS)3URF   
PDB (PDBSum)3URF   
PDB (IMB)3URF   
PDB (RSDB)3URF   
Human Protein AtlasENSG00000164761
Peptide AtlasO00300
HPRD04032
IPIIPI00298362   IPI00974201   
Protein Interaction databases
DIP (DOE-UCLA)O00300
IntAct (EBI)O00300
FunCoupENSG00000164761
BioGRIDTNFRSF11B
IntegromeDBTNFRSF11B
STRING (EMBL)TNFRSF11B
Ontologies - Pathways
QuickGOO00300
Ontology : AmiGOskeletal system development  receptor activity  cytokine activity  extracellular region  proteinaceous extracellular matrix  extracellular space  apoptotic process  signal transduction  response to nutrient  extracellular matrix organization  response to magnesium ion  negative regulation of odontogenesis of dentin-containing tooth  response to drug  response to estrogen  negative regulation of bone resorption  response to arsenic-containing substance  
Ontology : EGO-EBIskeletal system development  receptor activity  cytokine activity  extracellular region  proteinaceous extracellular matrix  extracellular space  apoptotic process  signal transduction  response to nutrient  extracellular matrix organization  response to magnesium ion  negative regulation of odontogenesis of dentin-containing tooth  response to drug  response to estrogen  negative regulation of bone resorption  response to arsenic-containing substance  
Pathways : KEGGCytokine-cytokine receptor interaction    Osteoclast differentiation   
Protein Interaction DatabaseTNFRSF11B
DoCM (Curated mutations)TNFRSF11B
Wikipedia pathwaysTNFRSF11B
Gene fusion - rearrangements
Polymorphisms : SNP, variants
NCBI Variation ViewerTNFRSF11B [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)TNFRSF11B
dbVarTNFRSF11B
ClinVarTNFRSF11B
1000_GenomesTNFRSF11B 
Exome Variant ServerTNFRSF11B
SNP (GeneSNP Utah)TNFRSF11B
SNP : HGBaseTNFRSF11B
Genetic variants : HAPMAPTNFRSF11B
Genomic VariantsTNFRSF11B  TNFRSF11B [DGVbeta]
Mutations
ICGC Data PortalENSG00000164761 
Somatic Mutations in Cancer : COSMICTNFRSF11B 
CONAN: Copy Number AnalysisTNFRSF11B 
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD - Leiden Open Variation Database
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] 
Diseases
DECIPHER (Syndromes)8:119935796-119964383
Mutations and Diseases : HGMDTNFRSF11B
OMIM239000    602643   
MedgenTNFRSF11B
NextProtO00300 [Medical]
GENETestsTNFRSF11B
Disease Genetic AssociationTNFRSF11B
Huge Navigator TNFRSF11B [HugePedia]  TNFRSF11B [HugeCancerGEM]
snp3D : Map Gene to Disease4982
DGIdb (Drug Gene Interaction db)TNFRSF11B
General knowledge
Homologs : HomoloGeneTNFRSF11B
Homology/Alignments : Family Browser (UCSC)TNFRSF11B
Phylogenetic Trees/Animal Genes : TreeFamTNFRSF11B
Chemical/Protein Interactions : CTD4982
Chemical/Pharm GKB GenePA36602
Clinical trialTNFRSF11B
Cancer Resource (Charite)ENSG00000164761
Other databases
Probes
Litterature
PubMed453 Pubmed reference(s) in Entrez
CoreMineTNFRSF11B
GoPubMedTNFRSF11B
iHOPTNFRSF11B

Bibliography

Osteoprotegerin: a novel secreted protein involved in the regulation of bone density.
Simonet WS, Lacey DL, Dunstan CR, Kelley M, Chang MS, Luthy R, Nguyen HQ, Wooden S, Bennett L, Boone T, Shimamoto G, DeRose M, Elliott R, Colombero A, Tan HL, Trail G, Sullivan J, Davy E, Bucay N, Renshaw-Gegg L, Hughes TM, Hill D, Pattison W, Campbell P, Sander S, Van G, Tarpley J, Derby P, Lee R, Boyle WJ.
Cell 1997; 89: 159-161.
PMID 9108485
 
Characterization of a novel TNF-like ligand and recently described TNF ligand and TNF receptor superfamily genes and their constitutive and inducible expression in hematopoietic and nonhematopoietic cells.
Tan KB, Harrop J, Reddy M, Young P, Terrett J, Emery J, Moore G, Truneh A.
Gene 1997; 204: 35-46.
PMID 9434163
 
Isolation of a novel cytokine from human fibroblasts that specifically inhibits osteoclastogenesis.
Tsuda E, Goto M, Mochizuki SI, Yano K, Kobayashi F, Morinaga T, Higashio K.
Biochem Biophys Res Commun 1997; 234: 137-142.
PMID 9168977
 
Modulation of life and death by the TNF receptor superfamily.
Baker SJ, Reddy EP.
Oncogene 1998; 17: 3261-3270.
PMID 9916988
 
Osteoprotegerin deficient mice develop early onset osteoporosis and arterial calcification.
Bucay N, Sarosi I, Dunstan CR, Morony S, Tarpley J, Capparelli C, Scully S, Tan HL, Xu W, Lacey DL, Boyle WJ, Simonet WS.
Genes Dev 1998; 12: 1260-1268.
PMID 9573043
 
Osteoprotegerin is a receptor for the cytotoxic ligand TRAIL.
Emery JG, McDonnell P, Burke MB, Deen KC, Lyn S, Silverman C, Dul E, Appelbaum ER, Eichman C, DiPrinzio R, Dodds RA, James IE, Rosenberg M, Lee JC, Young PR.
J Biol Chem 1998; 273; 14363-14367.
PMID 9603945
 
Severe osteoporosis in mice lacking osteoclastogenesis inhibitory factor/osteoprotegerin.
Mizuno A, Amizuka N, Irie K, Murakami A, Fujise N, Kanno T, Sato Y, Nakagawa N, Yasuda H, Mochizuki S, Gomibuchi T, Yano K, Shima N, Washida N, Tsuda E, Morinaga T, Higashio K, Ozawa H.
Biochem Biophys Res Comm 1998; 247; 610-615.
PMID 9647741
 
Characterization of structural domains of human osteoclastogenesis inhibitory factor.
Yamaguchi K, Kinosaki M, Goto M, Kobayashi F, Tsuda E, Morinaga T, Higashio K.
J Biol Chem 1998; 273: 5117-5123.
PMID 9478964
 
Identity of osteoclastogenesis inhibitory factor (OCIF) and osteoprotegerin (OPG): a mechanism by which OPG/OCIF inhibits osteoclastogenesis in vitro.
Yasuda H, Shima N, Nakagawa N, Mochizuki SI, Yano K, Fujise N, Sato Y, Goto M, Yamaguchi K, Kuriyama M, Kanno T, Murakami A, Tsuda E, Morinaga T, Higashio K.
Endocrinology 1998a; 39: 1329-1337.
PMID 9492069
 
Osteoclast differentiation factor is a ligand for osteoprotegerin/osteoclastogenesis inhibitory factor and is identical to TRANCE/RANKL.
Yasuda H, Shima N, Nakagawa N, Yamaguchi K, Kinosaki M, Mochizuki S, Tomoyasu A, Yano K, Goto M, Murakami A, Tsuda E, Morinaga T, Higashio K, Udagawa N, Takahashi N, Suda T.
Proc Natl Acad Sci U S A 1998b; 95: 3597-3602.
PMID 9520411
 
OPG/FDCR-1, a TNF receptor family member, is expressed in lymphoid cells and is up-regulated by ligating CD40.
Yun TJ, Chaudhary PM, Shu GL, Frazer JK, Ewings MK, SSchwartz SM, Pascual V, Hood LE, Clark EA.
J Immunol 1998; 161: 6113-6121.
PMID 9834095
 
Associations of serum osteoprotegerin levels with diabetes, stroke, bone density, fractures, and mortality in elderly women.
Browner WS, Lui LY, Cummings SR.
J Clin Endocrinol Metab 2001; 86: 631-637.
PMID 11158021
 
Receptor activator of NF-kB and osteoprotegerin expression by human microvascular endothelial cells, regulation by inflammatory cytokines, and role in human osteoclastogenesis.
Collin-Osdoby P, Rothe L, Anderson F, Nelson M, Maloney W, Osdoby P.
J Biol Chem 2001; 276: 20659-20672.
PMID 11274143
 
Osteoprotegerin, a crucial regulator of bone metabolism, also regulates B cell development and function.
Yun TJ, Tallquist MD, Aicher A, Rafferty KL, Marshall AJ, Moon JJ, Ewings ME, Mohaupt M, Herring SW, Clark EA.
J Immunol 2001; 166: 1482-1491.
PMID 11160187
 
Serum osteoprotegerin levels are associated with the presence and severity of coronary artery disease.
Jono S, Ikari Y, Shioi A, Mori K, Miki T, Hara K, Nishizawa Y.
Circulation 2002; 106: 1192-1194.
PMID 12208791
 
The alpha(v)beta3 integrin, NF-kappaB, osteoprotegerin endothelial cell survival pathway. Potential role in angiogenesis.
Scatena M, Giachelli C.
Trends Cardiovasc Med 2002; 12: 83-88.
PMID 15064358
 
Expression of osteoprotegerin correlates with aggressiveness and poor prognosis of gastric carcinoma.
Ito R., Nakayama, H., Yoshida, K Kuraoka K, Motoshita J, Oda N, Oue N, Yasui W.
Virchows Arch 2003; 443: 146-151.
PMID 12838418
 
Increased plasma concentrations of osteoprotegerin in type 2 diabetic patients with microvascular complications.
Knudsen ST, Foss CH, Poulsen PL, Andersen NH, Mogensen CE, Rasmussen LM.
Eur J Endocrinol 2003; 149: 39-42.
PMID 12824864
 
Serum osteoprotegerin levels in healthy controls and cancer patients.
Lipton A, Ali SM, Leitzel K, Chinchilli V, Witters L, Engle L, Holloway D, Bekker P, Dunstan CR.
Clin Cancer Res 2003; 8: 2306-2310.
PMID 12114435
 
Increased osteoprotegerin serum levels in men with coronary artery disease.
Schoppet M, Sattler AM, Juergen R, Schaefer JR, Herzum M, Maisch B, Hofbauer LC.
J Clin Endocrinol Metab 2003; 88: 1024-1028.
PMID 12629080
 
Clinical implications of the osteoprotegerin/RANKL/RANK system for bone and vascular diseases.
Hofbauer LC, Schoppet M.
JAMA 2004, 292: 490-495.
PMID 15280347
 
Prognostic significance of serum osteoprotegerin levels in patients with bladder carcinoma.
Mizutani Y, Matsubara H, Yamamoto K, Nan Li Y, Mikami K, Okihara K, Kawauchi A, Bonavida B, Miki T.
Cancer 2004; 101: 1794-1802.
PMID 15386310
 
The role of osteoprotegerin and tumor necrosis factor related apoptosis-inducing ligand in human microvascular endothelial cell survival.
Pritzker LB, Scatena M, Giachelli CM.
Mol Biol Cell 2004; 15: 2834-2841.
PMID 15064358
 
Localization of osteoprotegerin, tumor necrosis factor-related apoptosis-inducing ligand, and receptor activator of nuclear factor-kB in Monckeberg's sclerosis and atherosclerosis.
Schoppet M, Al-Fakhri N, Franke F, Katz N, Barth P, Maisch B, Preissner KT, Hofbauer LC.
J Clin Endocrinol Metab 2004; 89: 4104-4112.
PMID 15292354
 
Osteoprotegerin gene polymorphisms in men with coronary artery disease.
Soufi M, Schoppet M, Sattler AM, Herzum M, Maisch B, Hofbauer LC, Schaefer JR.
J Clin Endocrinol Metab 2004; 89: 3764-3768.
PMID 15292302
 
The molecular triad OPG/RANK/RANKL: involvement in the orchestration of pathophysiological bone remodeling.
Theoleyre S, Wittrant Y, Tat SK, Fortun Y, Redini F, Heymann D.
Cytokine Growth Factor Rev 2004; 15: 457-475. (REVIEW)
PMID 15561602
 
Osteoprotegerin is associated with silent coronary artery disease in high-risk but asymptomatic type 2 diabetic patients.
Avignon A, Sultan A, Piot C, Elaerts S, Cristol JP, Dupuy AM.
Diabetes Care 2005; 28: 2176-2180.
PMID 16123486
 
Association of osteoprotegerin with human abdominal aortic aneurysm progression.
Moran CS, McCann M, Karan M, Normal P, Ketheesan N, Golledge J.
Circulation 2005; 111: 3119-3125.
PMID 15939823
 
Syndecan-1 is involved in OPG-induced chemotaxis in human peripheral blood monocytes.
Mosheimer BA, Kaneider NC, Feistritzer C, Djanani AM, Sturn DH, Patsch JR, Wiedermann CJ.
J Clin Endocrin Metab 2005; 90: 2964-2971.
PMID 15728209
 
Arterial osteoprotegerin: increased amounts in diabetes and modifiable synthesis from vascular smooth muscle cells by insulin and TNF-a.
Olesen P, Ledet T, Rasmussen LM.
Diabetologia 2005; 48: 561-568.
PMID 15700136
 
Osteoprotegerin is expressed in colon carcinoma cells.
Pettersen I, Bakkelund W, Smedsrod B, and Sveinbjornsson B.
Anticancer Res 2005; 25: 3809-3816.
PMID 16309167
 
Functional dissociation of osteoprotegerin and its interaction with receptor activator of NF-kB ligand.
Schneeweis LA, Willard D, Milla ME.
J Biol Chem. 2005 Dec 16;280(50):41155-64.
PMID 16215261
 
Osteoprotegerin (OPG) is localized to the Weibel-Palade bodies of human vascular endothelial cells and is physically associated with von Willebrand factor.
Zannettino AC, Holding CA, Diamond P, Atkins GJ, Kostakis P, Farrugia A, Gamble J, To LB, Findlay DM, Haynes DR.
J Cell Physiol 2005; 204: 714-723.
PMID 15799029
 
Osteoprotegerin plasma concentrations correlate with severity of peripheral artery disease.
Ziegler S, Kudlacek S, Luger A, Minar E.
Atherosclerosis 2005; 182: 175-180.
PMID 16115489
 
Osteoprotegerin inactivation accelerates advanced atherosclerotic lesion progression and calcification in older ApoE-/- mice.
Bennett BJ, Scatena M, Kirk EA, Rattazzi M, Varon RM, Averill M, Schwartz SM, Giachelli CM, Rosenfeld ME.
Arterioscler Thromb Vasc Biol 2006; 26: 2117-2124.
PMID 16840715
 
Osteoprotegerin (OPG)-a potential new role in the regulation of endothelial cell phenotype and tumour angiogenesis?
Cross SS, Yang Z, Brown NJ, Balasubramanian SP, Evans CA, Woodward JK, Neville-Webbe HL, Lippitt JM, Reed MW, Coleman RE, Holen I.
Int J Cancer 2006; 118: 1901-1908.
PMID 16287088
 
Plasma osteoprotegerin levels are associated with glycaemic status, systolic blood pressure, kidney function and cardiovascular morbidity in type 1 diabetic patients.
Rasmussen LM, Tarnow L, Hansen TK, Parving HH, Flyvbjerg A.
Eur J Endocrinol 2006; 154: 75-81.
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Contributor(s)

Written08-2008Maria Grazia Di Iasio, Federica Corallini, Paola Secchiero, Silvano Capitani
Department of Morfology and Embryology, Human Anatomy Section - Ferrara University, 44100 ferrara, Italy

Citation

This paper should be referenced as such :
Di, Iasio MG ; Corallini, F ; Secchiero, P ; Capitani, S
TNFRSF11B (tumor necrosis factor receptor superfamily, member 11b)
Atlas Genet Cytogenet Oncol Haematol. 2009;13(7):504-509.
Free online version   Free pdf version   [Bibliographic record ]
URL : http://AtlasGeneticsOncology.org/Genes/TNFRSF11BID42610ch8q24.html

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