| pubmed-article:9707432 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9707432 | lifeskim:mentions | umls-concept:C0042567 | lld:lifeskim |
| pubmed-article:9707432 | lifeskim:mentions | umls-concept:C0013936 | lld:lifeskim |
| pubmed-article:9707432 | lifeskim:mentions | umls-concept:C0287990 | lld:lifeskim |
| pubmed-article:9707432 | lifeskim:mentions | umls-concept:C1418391 | lld:lifeskim |
| pubmed-article:9707432 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:9707432 | lifeskim:mentions | umls-concept:C0135624 | lld:lifeskim |
| pubmed-article:9707432 | lifeskim:mentions | umls-concept:C0450694 | lld:lifeskim |
| pubmed-article:9707432 | pubmed:issue | 16 | lld:pubmed |
| pubmed-article:9707432 | pubmed:dateCreated | 1998-10-7 | lld:pubmed |
| pubmed-article:9707432 | pubmed:abstractText | Bone morphogenetic protein-4 (BMP-4) is a multifunctional developmental regulator. BMP-4 is synthesized as an inactive precursor that is proteolytically activated by cleavage following the amino acid motif -Arg-Ser-Lys-Arg-. Very little is known about processing and secretion of BMPs. The proprotein convertases (PCs) are a family of seven structurally related serine endoproteases, at least one of which, furin, cleaves after the amino acid motif -Arg-X-Arg/Lys-Arg-. To examine potential roles of PCs during embryonic development we have misexpressed a potent protein inhibitor of furin, alpha1-antitrypsin Portland (alpha1-PDX) in early Xenopus embryos. Ectopic expression of alpha1-PDX phenocopies the effect of blocking endogenous BMP activity, leading to dorsalization of mesoderm and direct neural induction. alpha1-PDX-mediated neural induction can be reversed by co-expression of downstream components of the BMP-4 signaling pathway. Thus, alpha1-PDX can block BMP activity upstream of receptor binding, suggesting that it inhibits an endogenous BMP-4 convertase(s). Consistent with this hypothesis, alpha1-PDX prevents cleavage of BMP-4 in an oocyte translation assay. Using an in vitro digestion assay, we demonstrate that four members of the PC family have the ability to cleave BMP-4, but of these, only furin and PC6B are sensitive to alpha1-PDX. These studies provide the first in vivo evidence that furin and/or PC6 proteolytically activate BMP-4 during vertebrate embryogenesis. | lld:pubmed |
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| pubmed-article:9707432 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9707432 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9707432 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9707432 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9707432 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9707432 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:9707432 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:9707432 | pubmed:author | pubmed-author:ThomasGG | lld:pubmed |
| pubmed-article:9707432 | pubmed:author | pubmed-author:JeanFF | lld:pubmed |
| pubmed-article:9707432 | pubmed:author | pubmed-author:CuiYY | lld:pubmed |
| pubmed-article:9707432 | pubmed:author | pubmed-author:ChristianJ... | lld:pubmed |
| pubmed-article:9707432 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9707432 | pubmed:day | 17 | lld:pubmed |
| pubmed-article:9707432 | pubmed:volume | 17 | lld:pubmed |
| pubmed-article:9707432 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9707432 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9707432 | pubmed:pagination | 4735-43 | lld:pubmed |
| pubmed-article:9707432 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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