{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T21:05:41Z","timestamp":1791234341436,"version":"4.1.0"},"reference-count":51,"publisher":"Portland Press Ltd.","issue":"2","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2011,1,15]]},"abstract":"<jats:p>The predominant form of type\u00a0V collagen is the [\u03b11(V)]2\u03b12(V) heterotrimer. Mutations in COL5A1 or COL5A2, encoding respectively the \u03b11(V)- and \u03b12(V)-collagen chain, cause classic EDS (Ehlers\u2212Danlos syndrome), a heritable connective tissue disorder, characterized by fragile hyperextensible skin and joint hypermobility. Approximately half of the classic EDS cases remain unexplained. Type\u00a0V collagen controls collagen fibrillogenesis through its conserved \u03b11(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: \u03b11(I)- and \u03b12(I)-collagen chains, \u03b11(VI)-, \u03b12(VI)- and \u03b13(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-\u03b21 (transforming growth factor \u03b21). Solid-phase binding assays confirmed the involvement of the \u03b11(V)-N-propeptide in the interaction between native type\u00a0V collagen and type\u00a0VI collagen, suggesting a bridging function of this protein complex in the cell-matrix environment. Enzymatic studies showed that processing of the \u03b11(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.<\/jats:p>","DOI":"10.1042\/bj20101061","type":"journal-article","created":{"date-parts":[[2010,10,28]],"date-time":"2010-10-28T13:25:42Z","timestamp":1288272342000},"page":"371-381","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":57,"title":["Identification of binding partners interacting with the \u03b11-N-propeptide of type\u00a0V collagen"],"prefix":"10.1042","volume":"433","author":[{"given":"Sofie","family":"Symoens","sequence":"first","affiliation":[{"name":"Center for Medical Genetics, Ghent University Hospital, 9000 Ghent, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marjolijn","family":"Renard","sequence":"additional","affiliation":[{"name":"Center for Medical Genetics, Ghent University Hospital, 9000 Ghent, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christelle","family":"Bonod-Bidaud","sequence":"additional","affiliation":[{"name":"Institut de Biologie et Chimie des Prot\u00e9ines, CNRS UMR 5086, University Lyon 1, IFR128 Biosciences-Gerland, Lyon, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Delfien","family":"Syx","sequence":"additional","affiliation":[{"name":"Center for Medical Genetics, Ghent University Hospital, 9000 Ghent, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Elisabeth","family":"Vaganay","sequence":"additional","affiliation":[{"name":"Institut de Biologie et Chimie des Prot\u00e9ines, CNRS UMR 5086, University Lyon 1, IFR128 Biosciences-Gerland, Lyon, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fransiska","family":"Malfait","sequence":"additional","affiliation":[{"name":"Center for Medical Genetics, Ghent University Hospital, 9000 Ghent, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sylvie","family":"Ricard-Blum","sequence":"additional","affiliation":[{"name":"Institut de Biologie et Chimie des Prot\u00e9ines, CNRS UMR 5086, University Lyon 1, IFR128 Biosciences-Gerland, Lyon, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Efrat","family":"Kessler","sequence":"additional","affiliation":[{"name":"Maurice and Gabriela Goldschleger Eye Research Institute, Tel Aviv University Sackler Faculty of Medicine, Sheba Medical Center, Tel-Hashomer 52621, Israel"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lut","family":"Van\u00a0Laer","sequence":"additional","affiliation":[{"name":"Center for Medical Genetics, Ghent University Hospital, 9000 Ghent, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Paul","family":"Coucke","sequence":"additional","affiliation":[{"name":"Center for Medical Genetics, Ghent University Hospital, 9000 Ghent, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Florence","family":"Ruggiero","sequence":"additional","affiliation":[{"name":"Institut de Biologie et Chimie des Prot\u00e9ines, CNRS UMR 5086, University Lyon 1, IFR128 Biosciences-Gerland, Lyon, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anne","family":"De\u00a0Paepe","sequence":"additional","affiliation":[{"name":"Center for Medical Genetics, Ghent University Hospital, 9000 Ghent, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","published-online":{"date-parts":[[2010,12,22]]},"reference":[{"key":"2021112214312878800_B1","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1016\/S0968-4328(00)00043-3","article-title":"Type V collagen: heterotypic type\u00a0I\/V collagen interactions in the regulation of fibril assembly","volume":"32","author":"Birk","year":"2001","journal-title":"Micron"},{"key":"2021112214312878800_B2","doi-asserted-by":"crossref","first-page":"6049","DOI":"10.1128\/MCB.24.13.6049-6057.2004","article-title":"Development of a functional skin matrix requires deposition of collagen V heterotrimers","volume":"24","author":"Chanut-Delalande","year":"2004","journal-title":"Mol. 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