pubmed-article:18625713 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:18625713 | lifeskim:mentions | umls-concept:C0460002 | lld:lifeskim |
pubmed-article:18625713 | lifeskim:mentions | umls-concept:C0031437 | lld:lifeskim |
pubmed-article:18625713 | lifeskim:mentions | umls-concept:C0011155 | lld:lifeskim |
pubmed-article:18625713 | lifeskim:mentions | umls-concept:C0439064 | lld:lifeskim |
pubmed-article:18625713 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
pubmed-article:18625713 | lifeskim:mentions | umls-concept:C0181586 | lld:lifeskim |
pubmed-article:18625713 | pubmed:issue | 37 | lld:pubmed |
pubmed-article:18625713 | pubmed:dateCreated | 2008-9-8 | lld:pubmed |
pubmed-article:18625713 | pubmed:abstractText | Microfibril-associated glycoprotein-1 (MAGP-1) is a small molecular weight component of the fibrillin-rich microfibril. Gene-targeted inactivation of MAGP-1 reveals a complex phenotype that includes increased body weight and size due to excess body fat, an altered wound healing response in bone and skin, and a bleeding diathesis. Elastic tissues rich in MAGP-1-containing microfibrils develop normally and show normal function. The penetrance of MAGP-1-null phenotypes is highly variable and mouse strain-dependent, suggesting the influence of modifier genes. MAGP-1 was found to bind active transforming growth factor-beta (TGF-beta) and BMP-7 with high affinity, suggesting that it may be an important modulator of microfibril-mediated growth factor signaling. Many of the phenotypic traits observed in MAGP-1-deficient mice are consistent with loss of TGF-beta function and are generally opposite those associated with mutations in fibrillin-1 that result in enhanced TGF-beta signaling. Increased body size and fat deposition in MAGP-1-mutant animals are particularly intriguing given the localization of obesity traits in humans to the region on chromosome 1 containing the MAGP-1 gene. | lld:pubmed |
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pubmed-article:18625713 | pubmed:language | eng | lld:pubmed |
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pubmed-article:18625713 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:18625713 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:18625713 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:18625713 | pubmed:month | Sep | lld:pubmed |
pubmed-article:18625713 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:18625713 | pubmed:author | pubmed-author:MechamRobert... | lld:pubmed |
pubmed-article:18625713 | pubmed:author | pubmed-author:BroekelmannTh... | lld:pubmed |
pubmed-article:18625713 | pubmed:author | pubmed-author:PierceRichard... | lld:pubmed |
pubmed-article:18625713 | pubmed:author | pubmed-author:SegadeFernand... | lld:pubmed |
pubmed-article:18625713 | pubmed:author | pubmed-author:WerneckClaudi... | lld:pubmed |
pubmed-article:18625713 | pubmed:author | pubmed-author:KnutsenRussel... | lld:pubmed |
pubmed-article:18625713 | pubmed:author | pubmed-author:CraftClarissa... | lld:pubmed |
pubmed-article:18625713 | pubmed:author | pubmed-author:WeinbaumJusti... | lld:pubmed |