| pubmed-article:12213884 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12213884 | lifeskim:mentions | umls-concept:C0538161 | lld:lifeskim |
| pubmed-article:12213884 | lifeskim:mentions | umls-concept:C0961340 | lld:lifeskim |
| pubmed-article:12213884 | lifeskim:mentions | umls-concept:C0021665 | lld:lifeskim |
| pubmed-article:12213884 | lifeskim:mentions | umls-concept:C0023688 | lld:lifeskim |
| pubmed-article:12213884 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:12213884 | lifeskim:mentions | umls-concept:C1533691 | lld:lifeskim |
| pubmed-article:12213884 | lifeskim:mentions | umls-concept:C1515655 | lld:lifeskim |
| pubmed-article:12213884 | pubmed:issue | 9 | lld:pubmed |
| pubmed-article:12213884 | pubmed:dateCreated | 2002-9-5 | lld:pubmed |
| pubmed-article:12213884 | pubmed:abstractText | IGF-I, a ubiquitous polypeptide, plays a key role in longitudinal bone growth and acquisition. The most predominant effect of skeletal IGF-I is acceleration of the differentiation program for osteoblasts. However, in vivo studies using recombinant human (rh) IGF-I and/or rhGH have demonstrated stimulation of both bone formation and resorption, thereby potentially limiting the usefulness of these peptides in the treatment of osteoporosis. In this study, we hypothesized that IGF-I modulates bone resorption by regulating expression of osteoprotegerin (OPG) and receptor activator of nuclear factor-kappaB (RANK) ligand (RANKL) in bone cells. Using Northern analysis in ST2 cells, we found that human IGF-I suppressed OPG mRNA in a time- and dose-dependent manner: 100 micro g/LIGF-I (13 nM) decreased OPG expression by 37.0 +/- 1.8% (P < 0.002). The half maximal inhibitory dose of IGF-I was reached at 50 micro g/liter ( approximately 6.5 nM) with no effect of IGF-I on OPG message stability. Conditioned media from ST2 cells confirmed that IGF-I decreased secreted OPG, reducing levels by 42%, from 12.1-7 ng/ml at 48 h (P < 0.05). Similarly, IGF-I at 100 micro g/liter (13 nM) increased RANKL mRNA expression to 353 +/- 74% above untreated cells as assessed by real-time PCR. In vivo, low doses of rhGH when administered to elderly postmenopausal women only modestly raised serum IGF-I (to concentrations of 18-26 nM) and did not affect circulating OPG concentrations; however, administration of rhIGF-I (30 micro g/kg.d) for 1 yr to older women resulted in a significant increase in serum IGF-I (to concentrations of 39-45 nM) and a 20% reduction in serum OPG (P < 0.05). In summary, we conclude that IGF-I in a dose- and time-dependent manner regulates OPG and RANKL in vitro and in vivo. These data suggest IGF-I may act as a coupling factor in bone remodeling by activating both bone formation and bone resorption; the latter effect appears to be mediated through the OPG/RANKL system in bone. | lld:pubmed |
| pubmed-article:12213884 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12213884 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12213884 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12213884 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12213884 | pubmed:citationSubset | AIM | lld:pubmed |
| pubmed-article:12213884 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12213884 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12213884 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12213884 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12213884 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12213884 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12213884 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12213884 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12213884 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12213884 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12213884 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12213884 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12213884 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12213884 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12213884 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12213884 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12213884 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12213884 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12213884 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12213884 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12213884 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:12213884 | pubmed:issn | 0021-972X | lld:pubmed |
| pubmed-article:12213884 | pubmed:author | pubmed-author:MarcusRR | lld:pubmed |
| pubmed-article:12213884 | pubmed:author | pubmed-author:RubinJJ | lld:pubmed |
| pubmed-article:12213884 | pubmed:author | pubmed-author:BeamerW GWG | lld:pubmed |
| pubmed-article:12213884 | pubmed:author | pubmed-author:ZinTT | lld:pubmed |
| pubmed-article:12213884 | pubmed:author | pubmed-author:HollowayLL | lld:pubmed |
| pubmed-article:12213884 | pubmed:author | pubmed-author:FaeAA | lld:pubmed |
| pubmed-article:12213884 | pubmed:author | pubmed-author:NanesM SMS | lld:pubmed |
| pubmed-article:12213884 | pubmed:author | pubmed-author:RosenC JCJ | lld:pubmed |
| pubmed-article:12213884 | pubmed:author | pubmed-author:MurphyT CTC | lld:pubmed |
| pubmed-article:12213884 | pubmed:author | pubmed-author:Ackert-Bickne... | lld:pubmed |
| pubmed-article:12213884 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12213884 | pubmed:volume | 87 | lld:pubmed |
| pubmed-article:12213884 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12213884 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12213884 | pubmed:pagination | 4273-9 | lld:pubmed |
| pubmed-article:12213884 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:12213884 | pubmed:meshHeading | pubmed-meshheading:12213884... | lld:pubmed |
| pubmed-article:12213884 | pubmed:meshHeading | pubmed-meshheading:12213884... | lld:pubmed |
| pubmed-article:12213884 | pubmed:meshHeading | pubmed-meshheading:12213884... | lld:pubmed |
| pubmed-article:12213884 | pubmed:meshHeading | pubmed-meshheading:12213884... | lld:pubmed |
| pubmed-article:12213884 | pubmed:meshHeading | pubmed-meshheading:12213884... | lld:pubmed |
| pubmed-article:12213884 | pubmed:meshHeading | pubmed-meshheading:12213884... | lld:pubmed |
| pubmed-article:12213884 | pubmed:meshHeading | pubmed-meshheading:12213884... | lld:pubmed |
| pubmed-article:12213884 | pubmed:meshHeading | pubmed-meshheading:12213884... | lld:pubmed |
| pubmed-article:12213884 | pubmed:meshHeading | pubmed-meshheading:12213884... | lld:pubmed |
| pubmed-article:12213884 | pubmed:meshHeading | pubmed-meshheading:12213884... | lld:pubmed |
| pubmed-article:12213884 | pubmed:meshHeading | pubmed-meshheading:12213884... | lld:pubmed |
| pubmed-article:12213884 | pubmed:meshHeading | pubmed-meshheading:12213884... | lld:pubmed |
| pubmed-article:12213884 | pubmed:meshHeading | pubmed-meshheading:12213884... | lld:pubmed |
| pubmed-article:12213884 | pubmed:meshHeading | pubmed-meshheading:12213884... | lld:pubmed |
| pubmed-article:12213884 | pubmed:meshHeading | pubmed-meshheading:12213884... | lld:pubmed |
| pubmed-article:12213884 | pubmed:meshHeading | pubmed-meshheading:12213884... | lld:pubmed |
| pubmed-article:12213884 | pubmed:meshHeading | pubmed-meshheading:12213884... | lld:pubmed |
| pubmed-article:12213884 | pubmed:meshHeading | pubmed-meshheading:12213884... | lld:pubmed |
| pubmed-article:12213884 | pubmed:meshHeading | pubmed-meshheading:12213884... | lld:pubmed |
| pubmed-article:12213884 | pubmed:meshHeading | pubmed-meshheading:12213884... | lld:pubmed |
| pubmed-article:12213884 | pubmed:meshHeading | pubmed-meshheading:12213884... | lld:pubmed |
| pubmed-article:12213884 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:12213884 | pubmed:articleTitle | IGF-I regulates osteoprotegerin (OPG) and receptor activator of nuclear factor-kappaB ligand in vitro and OPG in vivo. | lld:pubmed |
| pubmed-article:12213884 | pubmed:affiliation | Emory University and Veterans Affairs Medical Center, Decatur, Georgia 30033, USA. | lld:pubmed |
| pubmed-article:12213884 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12213884 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:12213884 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:12213884 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:12213884 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:12213884 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:12213884 | lld:pubmed |
