| pubmed-article:16436676 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16436676 | lifeskim:mentions | umls-concept:C0262950 | lld:lifeskim |
| pubmed-article:16436676 | lifeskim:mentions | umls-concept:C0014257 | lld:lifeskim |
| pubmed-article:16436676 | lifeskim:mentions | umls-concept:C0031437 | lld:lifeskim |
| pubmed-article:16436676 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
| pubmed-article:16436676 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:16436676 | pubmed:dateCreated | 2006-1-26 | lld:pubmed |
| pubmed-article:16436676 | pubmed:abstractText | The transforming growth factor-beta superfamily member bone morphogenetic protein-2 (BMP-2) is up-regulated in atherosclerotic arteries; however, its effects on the endothelium are not well characterized. Using microdissected coronary arterial endothelial cells (CAECs) and cultured primary CAECs, we demonstrated endothelial mRNA expression of BMP-2 and BMP-4. The proinflammatory cytokine tumor necrosis factor-alpha and H2O2 significantly increased endothelial expression of BMP-2 but not BMP-4. In organ culture, BMP-2 substantially decreased relaxation of rat carotid arteries to acetylcholine and increased production of reactive oxygen species, events inhibited by pharmacologically blocking protein kinase C (PKC) or NAD(P)H oxidase. BMP-2 activated nuclear factor-kappaB in CAECs, and BMP-2 and BMP-4 substantially increased adhesion of monocytic THP-1 cells, which was reduced by pharmacologically inhibiting p42/44 MAP kinase pathway (also by siRNA down-regulating ERK-1/2) or PKC. Incubation of rat carotid arteries with BMP-2 ex vivo also increased adhesion of mononuclear cells to the endothelium, requiring p42/44 MAP kinase and PKC. Western blotting showed that in CAECs and carotid arteries BMP-2 elicited phosphorylation of p42/44 MAP kinase, which was reduced by blocking MAP kinase kinase and PKC. Collectively, expression of BMP-2 is regulated by proinflammatory stimuli, and increased levels of BMP-2 induce endothelial dysfunction, oxidative stress, and endothelial activation. Thus, the proinflammatory effects of BMP-2 may play a role in vascular pathophysiology. | lld:pubmed |
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| pubmed-article:16436676 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:16436676 | pubmed:citationSubset | AIM | lld:pubmed |
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| pubmed-article:16436676 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16436676 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:16436676 | pubmed:issn | 0002-9440 | lld:pubmed |
| pubmed-article:16436676 | pubmed:author | pubmed-author:CoxL GLG | lld:pubmed |
| pubmed-article:16436676 | pubmed:author | pubmed-author:KaleyGaborG | lld:pubmed |
| pubmed-article:16436676 | pubmed:author | pubmed-author:UngvariZoltan... | lld:pubmed |
| pubmed-article:16436676 | pubmed:author | pubmed-author:CsiszarAnnaA | lld:pubmed |
| pubmed-article:16436676 | pubmed:author | pubmed-author:EdwardsJohn... | lld:pubmed |
| pubmed-article:16436676 | pubmed:author | pubmed-author:WolinMichael... | lld:pubmed |
| pubmed-article:16436676 | pubmed:author | pubmed-author:AhmadMansoorM | lld:pubmed |
| pubmed-article:16436676 | pubmed:author | pubmed-author:SmithKira EKE | lld:pubmed |
| pubmed-article:16436676 | pubmed:author | pubmed-author:LabinskyyNaza... | lld:pubmed |
| pubmed-article:16436676 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16436676 | pubmed:volume | 168 | lld:pubmed |
| pubmed-article:16436676 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16436676 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16436676 | pubmed:pagination | 629-38 | lld:pubmed |
| pubmed-article:16436676 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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