| pubmed-article:12637569 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12637569 | lifeskim:mentions | umls-concept:C1330957 | lld:lifeskim |
| pubmed-article:12637569 | lifeskim:mentions | umls-concept:C0887838 | lld:lifeskim |
| pubmed-article:12637569 | lifeskim:mentions | umls-concept:C1100660 | lld:lifeskim |
| pubmed-article:12637569 | lifeskim:mentions | umls-concept:C0596311 | lld:lifeskim |
| pubmed-article:12637569 | lifeskim:mentions | umls-concept:C0178499 | lld:lifeskim |
| pubmed-article:12637569 | lifeskim:mentions | umls-concept:C1709450 | lld:lifeskim |
| pubmed-article:12637569 | lifeskim:mentions | umls-concept:C1527178 | lld:lifeskim |
| pubmed-article:12637569 | pubmed:issue | 20 | lld:pubmed |
| pubmed-article:12637569 | pubmed:dateCreated | 2003-5-12 | lld:pubmed |
| pubmed-article:12637569 | pubmed:abstractText | Bone morphogenetic protein (BMP)-1 is a zinc-dependent metalloproteinase that cleaves a variety of extracellular matrix substrates, including type I procollagen. Little is known about the site of action of BMP-1, although the extracellular matrix seems likely to be it. BMP-1 is synthesized with an N-terminal prodomain. The removal of the prodomain presumably activates the proteinase. In this study we show that the prodomain is cleaved in the trans-Golgi network (TGN) and by furin-like/paired basic proprotein convertases. Inhibitors of furin resulted in the secretion of pro-BMP-1, which could not cleave procollagen. Recombinant furin cleaved the prodomain from pro-BMP-1. Site-directed mutagenesis of the prodomain cleavage site (RSRR) to RSAA resulted in efficient secretion of pro-BMP-1. Therefore, prodomain cleavage was not required for secretion. Using peptide N-glycosidase and neuraminidase digestion to determine the post-translational status of pro-BMP-1 during its conversion to BMP-1, we showed that BMP-1 first appears in the TGN during sialylation of the molecule. Furthermore, immunofluorescence studies using an antibody to the nascent N terminus of BMP-1 showed localization to the TGN and plasma membrane. The observation that BMP-1 occurs inside the cell raises the possibility that BMP-1 might begin to cleave its substrates prior to secretion to the extracellular matrix. | lld:pubmed |
| pubmed-article:12637569 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:12637569 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:12637569 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12637569 | pubmed:month | May | lld:pubmed |
| pubmed-article:12637569 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:12637569 | pubmed:author | pubmed-author:KadlerKarl... | lld:pubmed |
| pubmed-article:12637569 | pubmed:author | pubmed-author:LeightonMatM | lld:pubmed |
| pubmed-article:12637569 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12637569 | pubmed:day | 16 | lld:pubmed |
| pubmed-article:12637569 | pubmed:volume | 278 | lld:pubmed |
| pubmed-article:12637569 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12637569 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12637569 | pubmed:pagination | 18478-84 | lld:pubmed |
| pubmed-article:12637569 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:12637569 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12637569 | pubmed:articleTitle | Paired basic/Furin-like proprotein convertase cleavage of Pro-BMP-1 in the trans-Golgi network. | lld:pubmed |
| pubmed-article:12637569 | pubmed:affiliation | Wellcome Trust Centre for Cell-Matrix Research, School of Biological Sciences, University of Manchester, Stopford Building 2.205, Oxford Road, Manchester M13 9PT, United Kingdom. | lld:pubmed |
| pubmed-article:12637569 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12637569 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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