| http://purl.uniprot.org/citations/17600318 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17600318 | http://www.w3.org/2000/01/rdf-schema#comment | "Bone morphogenetic proteins (BMPs) are multifunctional cytokines, which play a key role in vascular development and remodeling. Heme oxygenase-1 (HO-1), the rate-limiting enzyme in heme catabolism, has been shown to be protective against vascular and lung injury. In a microarray study, we identified HO-1 as a major target of BMP4 signaling in human pulmonary artery smooth muscle cells (PASMCs), and confirmed the induction of HO-1 mRNA and protein by RT-PCR and Western blotting, respectively. Immunoblotting demonstrated that incubation of PASMCs with BMP4 rapidly phosphorylated Smad1/5 and activated the mitogen-activated protein kinases, p38(MAPK) and ERK1/2, in PASMCs, but not JNK. Using pathway selective inhibitors, the induction of HO-1 mRNA and protein was shown to be dependent on activation of p38(MAPK). Induction was independent of Smad1/5 signaling, since HO-1 mRNA and protein induction was intact in PASMCs harboring mutations in the kinase domain of BMP type II receptor, with disrupted Smad signaling. In addition, adenoviral transfection of kinase-deficient BMPR-II also failed to inhibit BMP4-induced HO-1 expression. In functional studies, the HO-1 inhibitor, ZnPP-IX, partly reversed the growth-inhibitory effects of BMP4, and overexpression of HO-1 in PASMCs inhibited serum-stimulated [3H]-thymidine incorporation. Taken together, these findings show that HO-1 is an important Smad-independent target of BMP signaling in vascular smooth muscle. Inhibition of HO-1 function or expression will further increase the proproliferative capacity of BMPR-II-deficient PASMCs and may thus represent a potential "second hit" necessary for disease manifestation."xsd:string |
| http://purl.uniprot.org/citations/17600318 | http://purl.org/dc/terms/identifier | "doi:10.1165/rcmb.2006-0360oc"xsd:string |
| http://purl.uniprot.org/citations/17600318 | http://purl.uniprot.org/core/author | "Yang X."xsd:string |
| http://purl.uniprot.org/citations/17600318 | http://purl.uniprot.org/core/author | "Trembath R.C."xsd:string |
| http://purl.uniprot.org/citations/17600318 | http://purl.uniprot.org/core/author | "Morrell N.W."xsd:string |
| http://purl.uniprot.org/citations/17600318 | http://purl.uniprot.org/core/author | "Lee P.J."xsd:string |
| http://purl.uniprot.org/citations/17600318 | http://purl.uniprot.org/core/author | "Long L."xsd:string |
| http://purl.uniprot.org/citations/17600318 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
| http://purl.uniprot.org/citations/17600318 | http://purl.uniprot.org/core/name | "Am J Respir Cell Mol Biol"xsd:string |
| http://purl.uniprot.org/citations/17600318 | http://purl.uniprot.org/core/pages | "598-605"xsd:string |
| http://purl.uniprot.org/citations/17600318 | http://purl.uniprot.org/core/title | "BMP4 induces HO-1 via a Smad-independent, p38MAPK-dependent pathway in pulmonary artery myocytes."xsd:string |
| http://purl.uniprot.org/citations/17600318 | http://purl.uniprot.org/core/volume | "37"xsd:string |
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