Source:http://linkedlifedata.com/resource/pubmed/id/15817489
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
24
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| pubmed:dateCreated |
2005-6-13
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| pubmed:abstractText |
Bone morphogenetic protein 1 (BMP-1), which is a tolloid member of the astacin-like family of zinc metalloproteinases, is a highly effective procollagen C-proteinase (PCP) and chordinase. On the other hand, mammalian tolloid like-2 (mTLL-2) does not cleave chordin or procollagen; procollagen is cleaved by mTLL-2 in the presence of high levels of procollagen C-proteinase enhancer-1 (PCPE-1), for reasons that are unknown. We used these differences in activity between BMP-1 and mTLL-2 to narrow in on the domains in BMP-1 that specify PCP and chordinase activity. Using a domain swap approach, we showed that: 1) the metalloproteinase and CUB2 domains of BMP-1 are absolutely required for PCP activity; swaps with either of the corresponding domains in BMP-1 and mTLL-2 did not result in procollagen cleavage and 2) the proteinase domain of mTLL-2 can cleave chordin if coupled to the CUB1 domain of BMP-1. Therefore, the minimal structure for chordinase activity comprises a metalloproteinase domain (either from BMP-1 or from mTLL-2) and the CUB1 domain of BMP-1 (the CUB1 domain of mTLL-2 cannot substitute for the CUB1 domain of BMP-1). We showed that the minimal procollagen C-proteinase (BMP-1 lacking the EGF and CUB3 domain) was enhanced by PCPE-1 but not as well as BMP-1 retaining the CUB3 domain. Further studies showed that PCPE-1 had no effect on the ability of BMP-1 to cleave chordin. The data support a previously suggested mechanism of PCPE-1 whereby PCPE-1 interacts with procollagen, but in addition, the CUB3 domain of BMP-1 appears to augment the interaction.
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| pubmed:grant | |
| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/BMP1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Bone Morphogenetic Protein 1,
http://linkedlifedata.com/resource/pubmed/chemical/Bone Morphogenetic Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Extracellular Matrix Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Intercellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Metalloendopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/PCOLCE protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/TLL2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Tolloid-Like Metalloproteinases,
http://linkedlifedata.com/resource/pubmed/chemical/chordin
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| pubmed:status |
MEDLINE
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| pubmed:month |
Jun
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| pubmed:issn |
0021-9258
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
17
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| pubmed:volume |
280
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
22616-23
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| pubmed:dateRevised |
2008-11-21
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| pubmed:meshHeading |
pubmed-meshheading:15817489-Blotting, Western,
pubmed-meshheading:15817489-Bone Morphogenetic Protein 1,
pubmed-meshheading:15817489-Bone Morphogenetic Proteins,
pubmed-meshheading:15817489-Cell Line,
pubmed-meshheading:15817489-DNA, Complementary,
pubmed-meshheading:15817489-Extracellular Matrix Proteins,
pubmed-meshheading:15817489-Gene Deletion,
pubmed-meshheading:15817489-Glycoproteins,
pubmed-meshheading:15817489-Humans,
pubmed-meshheading:15817489-Intercellular Signaling Peptides and Proteins,
pubmed-meshheading:15817489-Metalloendopeptidases,
pubmed-meshheading:15817489-Mutagenesis, Site-Directed,
pubmed-meshheading:15817489-Mutation,
pubmed-meshheading:15817489-Protein Binding,
pubmed-meshheading:15817489-Protein Structure, Tertiary,
pubmed-meshheading:15817489-Tolloid-Like Metalloproteinases
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| pubmed:year |
2005
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| pubmed:articleTitle |
Identification of the minimal domain structure of bone morphogenetic protein-1 (BMP-1) for chordinase activity: chordinase activity is not enhanced by procollagen C-proteinase enhancer-1 (PCPE-1).
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| pubmed:affiliation |
Wellcome Trust Centre for Cell-Matrix Research, University of Manchester, Faculty of Life Sciences, Michael Smith Building, Manchester, UK.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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