| pubmed-article:10825232 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10825232 | lifeskim:mentions | umls-concept:C0083867 | lld:lifeskim |
| pubmed-article:10825232 | lifeskim:mentions | umls-concept:C0262950 | lld:lifeskim |
| pubmed-article:10825232 | lifeskim:mentions | umls-concept:C1167267 | lld:lifeskim |
| pubmed-article:10825232 | lifeskim:mentions | umls-concept:C0031437 | lld:lifeskim |
| pubmed-article:10825232 | lifeskim:mentions | umls-concept:C1521970 | lld:lifeskim |
| pubmed-article:10825232 | lifeskim:mentions | umls-concept:C1846431 | lld:lifeskim |
| pubmed-article:10825232 | lifeskim:mentions | umls-concept:C1539322 | lld:lifeskim |
| pubmed-article:10825232 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
| pubmed-article:10825232 | lifeskim:mentions | umls-concept:C1658578 | lld:lifeskim |
| pubmed-article:10825232 | lifeskim:mentions | umls-concept:C1533691 | lld:lifeskim |
| pubmed-article:10825232 | lifeskim:mentions | umls-concept:C2745888 | lld:lifeskim |
| pubmed-article:10825232 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
| pubmed-article:10825232 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
| pubmed-article:10825232 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:10825232 | pubmed:dateCreated | 2000-7-3 | lld:pubmed |
| pubmed-article:10825232 | pubmed:abstractText | Vascular proliferative disorders are characterized by migration and proliferation of vascular smooth muscle cells (SMCs), loss of expression of SMC phenotype, and enhanced extracellular matrix synthesis (e.g., type I collagen). We report here that bone morphogenetic protein-7 (BMP-7), a member of the transforming growth factor-beta (TGF-beta) superfamily, is capable of inhibiting both serum-stimulated and growth factor-induced (platelet-derived growth factor [PDGF-BB] and TGF-beta1) cell growth as measured by (3)H-thymidine uptake into DNA synthesis and cell number in primary human aortic smooth muscle (HASM) cell cultures. Concomitantly, addition of BMP-7 stimulates the expression of SMC-specific markers, namely alpha-actin and heavy chain myosin as examined by RT-PCR and Northern blot analyses. The collagen type III/I ratio that becomes lower with the transdifferentiation of SMCs into myofibroblasts is also maintained in BMP-7-treated cultures as compared to untreated controls. Studies on the mechanism of action indicate that BMP-7 treatment inhibits cyclin-dependent kinase 2 (cdk-2) that was stimulated during PDGF-BB-induced proliferation of SMCs and upregulates the expression of the inhibitory Smad, Smad6, which was shown to inhibit TGF-beta superfamily signaling. These results collectively suggest that BMP-7 maintains the expression of vascular SMC phenotype and may prevent vascular proliferative disorders, thus potentially acting as a palliative after damage to the vascular integrity. | lld:pubmed |
| pubmed-article:10825232 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10825232 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10825232 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10825232 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10825232 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10825232 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10825232 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10825232 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10825232 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10825232 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10825232 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10825232 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10825232 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10825232 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10825232 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10825232 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:10825232 | pubmed:issn | 0021-9541 | lld:pubmed |
| pubmed-article:10825232 | pubmed:author | pubmed-author:SampathT KTK | lld:pubmed |
| pubmed-article:10825232 | pubmed:author | pubmed-author:VukicevicSS | lld:pubmed |
| pubmed-article:10825232 | pubmed:author | pubmed-author:DoraiHH | lld:pubmed |
| pubmed-article:10825232 | pubmed:copyrightInfo | Copyright 2000 Wiley-Liss, Inc. | lld:pubmed |
| pubmed-article:10825232 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10825232 | pubmed:volume | 184 | lld:pubmed |
| pubmed-article:10825232 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10825232 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10825232 | pubmed:pagination | 37-45 | lld:pubmed |
| pubmed-article:10825232 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:10825232 | pubmed:meshHeading | pubmed-meshheading:10825232... | lld:pubmed |
| pubmed-article:10825232 | pubmed:meshHeading | pubmed-meshheading:10825232... | lld:pubmed |
| pubmed-article:10825232 | pubmed:meshHeading | pubmed-meshheading:10825232... | lld:pubmed |
| pubmed-article:10825232 | pubmed:meshHeading | pubmed-meshheading:10825232... | lld:pubmed |
| pubmed-article:10825232 | pubmed:meshHeading | pubmed-meshheading:10825232... | lld:pubmed |
| pubmed-article:10825232 | pubmed:meshHeading | pubmed-meshheading:10825232... | lld:pubmed |
| pubmed-article:10825232 | pubmed:meshHeading | pubmed-meshheading:10825232... | lld:pubmed |
| pubmed-article:10825232 | pubmed:meshHeading | pubmed-meshheading:10825232... | lld:pubmed |
| pubmed-article:10825232 | pubmed:meshHeading | pubmed-meshheading:10825232... | lld:pubmed |
| pubmed-article:10825232 | pubmed:meshHeading | pubmed-meshheading:10825232... | lld:pubmed |
| pubmed-article:10825232 | pubmed:meshHeading | pubmed-meshheading:10825232... | lld:pubmed |
| pubmed-article:10825232 | pubmed:meshHeading | pubmed-meshheading:10825232... | lld:pubmed |
| pubmed-article:10825232 | pubmed:meshHeading | pubmed-meshheading:10825232... | lld:pubmed |
| pubmed-article:10825232 | pubmed:meshHeading | pubmed-meshheading:10825232... | lld:pubmed |
| pubmed-article:10825232 | pubmed:meshHeading | pubmed-meshheading:10825232... | lld:pubmed |
| pubmed-article:10825232 | pubmed:meshHeading | pubmed-meshheading:10825232... | lld:pubmed |
| pubmed-article:10825232 | pubmed:meshHeading | pubmed-meshheading:10825232... | lld:pubmed |
| pubmed-article:10825232 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10825232 | pubmed:articleTitle | Bone morphogenetic protein-7 (osteogenic protein-1) inhibits smooth muscle cell proliferation and stimulates the expression of markers that are characteristic of SMC phenotype in vitro. | lld:pubmed |
| pubmed-article:10825232 | pubmed:affiliation | Creative BioMolecules Inc., Hopkinton, Massachusetts, USA. hdorai@creativebio.com | lld:pubmed |
| pubmed-article:10825232 | pubmed:publicationType | Journal Article | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10825232 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10825232 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10825232 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10825232 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10825232 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10825232 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10825232 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10825232 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10825232 | lld:pubmed |
