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- aggregation classification "A1".
- aggregation creator B381423.
- aggregation creator B381424.
- aggregation creator B381425.
- aggregation creator B381426.
- aggregation creator B381427.
- aggregation creator B381428.
- aggregation creator person.
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- aggregation date "2011".
- aggregation format "application/pdf".
- aggregation hasFormat 1141189.bibtex.
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- aggregation isPartOf urn:issn:0264-6021.
- aggregation language "eng".
- aggregation rights "I have transferred the copyright for this publication to the publisher".
- aggregation subject "Medicine and Health Sciences".
- aggregation title "Identification of binding partners interacting with the α1-N-propeptide of type V collagen".
- aggregation abstract "The predominant form of type V collagen is the [α1(V)]₂α2(V) heterotrimer. Mutations in COL5A1 or COL5A2, encoding respectively the α1(V)- and α2(V)-collagen chain, cause classic EDS (Ehlers-Danlos syndrome), a heritable connective tissue disorder, characterized by fragile hyperextensible skin and joint hypermobility. Approximately half of the classic EDS cases remain unexplained. Type V collagen controls collagen fibrillogenesis through its conserved α1(V)-N-propeptide domain. To gain an insight into the role of this domain, a yeast two-hybrid screen among proteins expressed in human dermal fibroblasts was performed utilizing the N-propeptide as a bait. We identified 12 interacting proteins, including extracellular matrix proteins and proteins involved in collagen biosynthesis. Eleven interactions were confirmed by surface plasmon resonance and/or co-immunoprecipitation: α1(I)- and α2(I)-collagen chains, α1(VI)-, α2(VI)- and α3(VI)-collagen chains, tenascin-C, fibronectin, PCPE-1 (procollagen C-proteinase enhancer-1), TIMP-1 (tissue inhibitor of metalloproteinases-1), MMP-2 (matrix metalloproteinase 2) and TGF-β1 (transforming growth factor β1). Solid-phase binding assays confirmed the involvement of the α1(V)-N-propeptide in the interaction between native type V collagen and type VI collagen, suggesting a bridging function of this protein complex in the cell-matrix environment. Enzymatic studies showed that processing of the α1(V)-N-propeptide by BMP-1 (bone morphogenetic protein 1)/procollagen C-proteinase is enhanced by PCPE-1. These interactions are likely to be involved in extracellular matrix homoeostasis and their disruption could explain the pathogenetic mechanism in unresolved classic EDS cases.".
- aggregation authorList BK689041.
- aggregation endPage "381".
- aggregation issue "2".
- aggregation startPage "371".
- aggregation volume "433".
- aggregation aggregates 1141231.
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- aggregation isDescribedBy 1141189.
- aggregation similarTo BJ20101061.
- aggregation similarTo LU-1141189.