{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T22:26:25Z","timestamp":1790807185252,"version":"4.1.0"},"reference-count":24,"publisher":"Oxford University Press (OUP)","issue":"3","license":[{"start":{"date-parts":[[2010,9,13]],"date-time":"2010-09-13T00:00:00Z","timestamp":1284336000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/journals\/pages\/open_access\/funder_policies\/chorus\/standard_publication_model"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2011,3,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>Osteogenesis imperfecta (OI) is a genetic disorder of connective tissue characterized by bone fragility and alteration in synthesis and posttranslational modification of type I collagen. Autosomal dominant OI is caused by mutations in the genes (COL1A1 or COL1A2) encoding the chains of type I collagen. Bruck syndrome is a recessive disorder featuring congenital contractures in addition to bone fragility; Bruck syndrome type 2 is caused by mutations in PLOD2 encoding collagen lysyl hydroxylase, whereas Bruck syndrome type 1 has been mapped to chromosome 17, with evidence suggesting region 17p12, but the gene has remained elusive so far. Recently, the molecular spectrum of OI has been expanded with the description of the basis of a unique posttranslational modification of type I procollagen, that is, 3-prolyl-hydroxylation. Three proteins, cartilage-associated protein (CRTAP), prolyl-3-hydroxylase-1 (P3H1, encoded by the LEPRE1 gene), and the prolyl cis-trans isomerase cyclophilin-B (PPIB), form a complex that is required for fibrillar collagen 3-prolyl-hydroxylation, and mutations in each gene have been shown to cause recessive forms of OI. Since then, an additional putative collagen chaperone complex, composed of FKBP10 (also known as FKBP65) and SERPINH1 (also known as HSP47), also has been shown to be mutated in recessive OI. Here we describe five families with OI-like bone fragility in association with congenital contractures who all had FKBP10 mutations. Therefore, we conclude that FKBP10 mutations are a cause of recessive osteogenesis imperfecta and Bruck syndrome, possibly Bruck syndrome Type 1 since the location on chromosome 17 has not been definitely localized. \u00a9 2011 American Society for Bone and Mineral Research.<\/jats:p>","DOI":"10.1002\/jbmr.250","type":"journal-article","created":{"date-parts":[[2010,9,13]],"date-time":"2010-09-13T19:22:28Z","timestamp":1284405748000},"page":"666-672","source":"Crossref","is-referenced-by-count":170,"title":["Mutations in <i>FKBP10<\/i> cause recessive osteogenesis imperfecta and bruck syndrome"],"prefix":"10.1093","volume":"26","author":[{"given":"Brian P","family":"Kelley","sequence":"first","affiliation":[{"name":"Howard Hughes Medical Institute, Houston, TX, USA"},{"name":"Department of Molecular and Human Genetics, Baylor College of Medicine, Houston, TX, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fransiska","family":"Malfait","sequence":"additional","affiliation":[{"name":"Center for Medical Genetics, Ghent University Hospital, Ghent, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Luisa","family":"Bonafe","sequence":"additional","affiliation":[{"name":"Division of Molecular Pediatrics, Centre Hospitalier Universitaire Vaudois, Lausanne, Switzerland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dustin","family":"Baldridge","sequence":"additional","affiliation":[{"name":"Department of Molecular and Human Genetics, Baylor College of Medicine, Houston, TX, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Erica","family":"Homan","sequence":"additional","affiliation":[{"name":"Department of Molecular and Human Genetics, Baylor College of Medicine, Houston, TX, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sofie","family":"Symoens","sequence":"additional","affiliation":[{"name":"Center for Medical Genetics, Ghent University Hospital, Ghent, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andy","family":"Willaert","sequence":"additional","affiliation":[{"name":"Center for Medical Genetics, Ghent University Hospital, Ghent, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nursel","family":"Elcioglu","sequence":"additional","affiliation":[{"name":"Department of Pediatric Genetics, Marmara University Medical Faculty, Istanbul, Turkey"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lionel","family":"Van Maldergem","sequence":"additional","affiliation":[{"name":"Centre de G\u00e9n\u00e9tique Humaine, Universite de Li\u00e8ge, Li\u00e8ge, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christine","family":"Verellen-Dumoulin","sequence":"additional","affiliation":[{"name":"Center for Human Genetics, Cliniques Universitaires St Luc and University of Louvain Medical School, Brussels, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yves","family":"Gillerot","sequence":"additional","affiliation":[{"name":"Center for Human Genetics, Cliniques Universitaires St Luc and University of Louvain Medical School, Brussels, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dobrawa","family":"Napierala","sequence":"additional","affiliation":[{"name":"Department of Molecular and Human Genetics, Baylor College of Medicine, Houston, TX, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Deborah","family":"Krakow","sequence":"additional","affiliation":[{"name":"Medical Genetics Institute, Cedars-Sinai Medical Center, David Geffen School of Medicine at UCLA, Los Angeles, CA, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Peter","family":"Beighton","sequence":"additional","affiliation":[{"name":"Division of Human Genetics, University of Capetown, Observatory, South Africa"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrea","family":"Superti-Furga","sequence":"additional","affiliation":[{"name":"Division of Molecular Pediatrics, Centre Hospitalier Universitaire Vaudois, Lausanne, Switzerland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anne","family":"De Paepe","sequence":"additional","affiliation":[{"name":"Center for Medical Genetics, Ghent University Hospital, Ghent, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Brendan","family":"Lee","sequence":"additional","affiliation":[{"name":"Howard Hughes Medical Institute, Houston, TX, USA"},{"name":"Department of Molecular and Human Genetics, Baylor College of Medicine, Houston, TX, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2010,9,13]]},"reference":[{"key":"2024020318062911500_bib1","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1016\/j.cell.2006.08.039","article-title":"CRTAP is required for prolyl 3- hydroxylation and mutations cause recessive osteogenesis imperfecta","volume":"127","author":"Morello","year":"2006","journal-title":"Cell."},{"key":"2024020318062911500_bib2","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1007\/s00441-009-0872-0","article-title":"Null mutations in LEPRE1 and CRTAP cause severe recessive osteogenesis imperfecta","volume":"339","author":"Marini","year":"2010","journal-title":"Cell Tissue Res."},{"key":"2024020318062911500_bib3","doi-asserted-by":"crossref","first-page":"521","DOI":"10.1016\/j.ajhg.2009.09.001","article-title":"PPIB mutations cause severe osteogenesis imperfecta","volume":"85","author":"van Dijk","year":"2009","journal-title":"Am J Hum Genet."},{"key":"2024020318062911500_bib4","doi-asserted-by":"crossref","first-page":"1435","DOI":"10.1002\/humu.20799","article-title":"CRTAP and LEPRE1 mutations in recessive osteogenesis imperfecta","volume":"29","author":"Baldridge","year":"2008","journal-title":"Hum Mutat."},{"key":"2024020318062911500_bib5","doi-asserted-by":"crossref","first-page":"389","DOI":"10.1016\/j.ajhg.2010.01.034","article-title":"Homozygosity for a missense mutation in SERPINH1, which encodes the collagen chaperone protein HSP47, results in severe recessive osteogenesis imperfecta","volume":"86","author":"Christiansen","year":"2010","journal-title":"Am J Hum Genet."},{"key":"2024020318062911500_bib6","doi-asserted-by":"crossref","first-page":"551","DOI":"10.1016\/j.ajhg.2010.02.022","article-title":"Mutations in the gene encoding the RER chaperone FKBP65 produce autosomal recessive osteogenesis imperfecta","volume":"86","author":"Alanay","year":"2010","journal-title":"Am J Hum Genet."},{"key":"2024020318062911500_bib7","doi-asserted-by":"crossref","first-page":"1054","DOI":"10.1073\/pnas.96.3.1054","article-title":"Defective collagen crosslinking in bone, but not in ligament or cartilage, in Bruck syndrome: indications for a bone-specific telopeptide lysyl hydroxylase on chromosome 17","volume":"96","author":"Bank","year":"1999","journal-title":"Proc Natl Acad Sci U S A."},{"key":"2024020318062911500_bib8","doi-asserted-by":"crossref","first-page":"717","DOI":"10.1146\/annurev.bi.53.070184.003441","article-title":"Cross-linking in collagen and elastin","volume":"53","author":"Eyre","year":"1984","journal-title":"Annu Rev Biochem."},{"key":"2024020318062911500_bib9","doi-asserted-by":"crossref","first-page":"170","DOI":"10.1016\/0304-4165(85)90199-0","article-title":"Low-angle X-ray diffraction analysis of the collagen-proteoglycan interactions in articular cartilage","volume":"842","author":"Ronziere","year":"1985","journal-title":"Biochim Biophys Acta."},{"key":"2024020318062911500_bib10","doi-asserted-by":"crossref","first-page":"2439","DOI":"10.1096\/fasebj.6.7.1348714","article-title":"Enzymatic and nonenzymatic cross-linking of collagen and elastin","volume":"6","author":"Reiser","year":"1992","journal-title":"FASEB J."},{"key":"2024020318062911500_bib11","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1002\/9780470110485.ch8","article-title":"Analysis of the crosslinking components in collagen and elastin","volume":"28","author":"Robins","year":"1982","journal-title":"Methods Biochem Anal."},{"key":"2024020318062911500_bib12","doi-asserted-by":"crossref","first-page":"380","DOI":"10.1016\/0003-2697(84)90101-5","article-title":"Quantitation of hydroxypyridinium crosslinks in collagen by high-performance liquid chromatography","volume":"137","author":"Eyre","year":"1984","journal-title":"Anal Biochem."},{"key":"2024020318062911500_bib13","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1097\/01202412-199801000-00006","article-title":"Bruck syndrome: a rare combination of bone fragility and multiple congenital joint contractures","volume":"7","author":"Breslau-Siderius","year":"1998","journal-title":"J Pediatr Orthop B."},{"key":"2024020318062911500_bib14","doi-asserted-by":"crossref","first-page":"40967","DOI":"10.1074\/jbc.M307380200","article-title":"Identification of PLOD2 as telopeptide lysyl hydroxylase, an important enzyme in fibrosis","volume":"278","author":"van der Slot","year":"2003","journal-title":"J Biol Chem."},{"key":"2024020318062911500_bib15","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1083\/jcb.140.2.295","article-title":"Identification of tropoelastin as a ligand for the 65-kD FK506-binding protein, FKBP65, in the secretory pathway","volume":"140","author":"Davis","year":"1998","journal-title":"J Cell Biol."},{"key":"2024020318062911500_bib16","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1042\/bj3300109","article-title":"Chicken FK506-binding protein, FKBP65, a member of the FKBP family of peptidylprolyl cis-trans isomerases, is only partially inhibited by FK506","volume":"330","author":"Zeng","year":"1998","journal-title":"Biochem J."},{"key":"2024020318062911500_bib17","doi-asserted-by":"crossref","first-page":"31584","DOI":"10.1074\/jbc.M802535200","article-title":"The rough endoplasmic reticulum-resident FK506-binding protein FKBP65 is a molecular chaperone that interacts with collagens","volume":"283","author":"Ishikawa","year":"2008","journal-title":"J Biol Chem."},{"key":"2024020318062911500_bib18","doi-asserted-by":"crossref","first-page":"2346","DOI":"10.1091\/mbc.e05-11-1065","article-title":"Type I collagen in Hsp47-null cells is aggregated in endoplasmic reticulum and deficient in N-propeptide processing and fibrillogenesis","volume":"17","author":"Ishida","year":"2006","journal-title":"Mol Biol Cell."},{"key":"2024020318062911500_bib19","doi-asserted-by":"crossref","first-page":"e1000579","DOI":"10.1371\/journal.pgen.1000579","article-title":"A missense mutation in the SERPINH1 gene in Dachshunds with osteogenesis imperfecta","volume":"5","author":"Drogemuller","year":"2009","journal-title":"PLoS Genet."},{"key":"2024020318062911500_bib20","doi-asserted-by":"crossref","first-page":"641","DOI":"10.1007\/s00776-005-0958-9","article-title":"Bruck syndrome: congenital joint contractures with bone fragility","volume":"10","author":"Mokete","year":"2005","journal-title":"J Orthop Sci."},{"key":"2024020318062911500_bib21","doi-asserted-by":"crossref","first-page":"122","DOI":"10.1111\/j.1399-0004.1989.tb03174.x","article-title":"Osteogenesis imperfecta with congenital joint contractures (Bruck syndrome)","volume":"36","author":"Viljoen","year":"1989","journal-title":"Clin Genet."},{"key":"2024020318062911500_bib22","first-page":"285","volume-title":"Connective tissue and it heritable disorders: molecular, genetic, and medical aspects","author":"Byers","year":"2002"},{"key":"2024020318062911500_bib23","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1002\/humu.20429","article-title":"Consortium for osteogenesis imperfecta mutations in the helical domain of type I collagen: regions rich in lethal mutations align with collagen binding sites for integrins and proteoglycans","volume":"28","author":"Marini","year":"2006","journal-title":"Hum Mut."},{"key":"2024020318062911500_bib24","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1002\/ajmg.a.30231","article-title":"Phenotypic and molecular characterization of Bruck syndrome (osteogenesis imperfecta with contractures of the large joints) caused by a recessive mutation in PLOD2","volume":"131","author":"Ha-Vinh","year":"2004","journal-title":"Am J Med Genet A."}],"container-title":["Journal of Bone and Mineral Research"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.wiley.com\/onlinelibrary\/tdm\/v1\/articles\/10.1002%2Fjbmr.250","content-type":"unspecified","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/academic.oup.com\/jbmr\/article-pdf\/26\/3\/666\/56559752\/250_ftp.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/academic.oup.com\/jbmr\/article-pdf\/26\/3\/666\/56559752\/250_ftp.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,3,13]],"date-time":"2024-03-13T14:54:02Z","timestamp":1710341642000},"score":1,"resource":{"primary":{"URL":"https:\/\/academic.oup.com\/jbmr\/article\/26\/3\/666-672\/7598201"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2010,9,13]]},"references-count":24,"journal-issue":{"issue":"3","published-online":{"date-parts":[[2010,9,13]]},"published-print":{"date-parts":[[2011,3,1]]}},"URL":"https:\/\/doi.org\/10.1002\/jbmr.250","relation":{},"ISSN":["0884-0431","1523-4681"],"issn-type":[{"value":"0884-0431","type":"print"},{"value":"1523-4681","type":"electronic"}],"subject":[],"published-other":{"date-parts":[[2011,3,1]]},"published":{"date-parts":[[2010,9,13]]}}}