{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,3]],"date-time":"2026-06-03T02:47:33Z","timestamp":1780454853861,"version":"3.54.1"},"reference-count":75,"publisher":"The Company of Biologists","license":[{"start":{"date-parts":[[2016,8,15]],"date-time":"2016-08-15T00:00:00Z","timestamp":1471219200000},"content-version":"vor","delay-in-days":227,"URL":"http:\/\/www.biologists.com\/user-licence-1-1"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"abstract":"<jats:p>Cartilage oligomeric matrix protein (COMP) is an abundant component in the extracellular matrix (ECM) of load-bearing tissues such as tendons and cartilage. It serves adaptor functions by bridging different ECM structures. We previously showed that COMP is also a constitutive component of healthy human skin and strongly induced in fibrosis. It binds directly and with high affinity to collagen I and to collagen XII that decorates the surface of collagen I fibrils.<\/jats:p>\n               <jats:p>We demonstrate here that lack of COMP-collagen interaction in the extracellular space leads to changes in collagen fibril morphology and density resulting in altered skin biomechanical properties. Surprisingly, COMP also fulfills an important intracellular function in assisting efficient secretion of collagens, which were retained in the endoplasmic reticulum of COMP-null fibroblasts. Accordingly COMP-null mice showed severely attenuated fibrotic responses in skin. Collagen secretion was fully restored by introducing wild type COMP. Hence, our work unravels a novel, non-structural and intracellular function of the ECM protein COMP in controlling collagen secretion.<\/jats:p>","DOI":"10.1242\/jcs.180216","type":"journal-article","created":{"date-parts":[[2016,1,9]],"date-time":"2016-01-09T02:59:25Z","timestamp":1452308365000},"source":"Crossref","is-referenced-by-count":48,"title":["COMP-assisted collagen secretion - a novel intracellular function required for fibrosis"],"prefix":"10.1242","author":[{"given":"Jan-Niklas","family":"Schulz","sequence":"first","affiliation":[{"name":"Department of Dermatology, University of Cologne, Cologne, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Julian","family":"N\u00fcchel","sequence":"additional","affiliation":[{"name":"Center for Biochemistry, University of Cologne, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anja","family":"Niehoff","sequence":"additional","affiliation":[{"name":"Cologne Center for Musculoskeletal Biomechanics (CCMB), University of Cologne, Germany"},{"name":"German Sport University, Cologne, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wilhelm","family":"Bloch","sequence":"additional","affiliation":[{"name":"German Sport University, Cologne, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Katrin","family":"Sch\u00f6nborn","sequence":"additional","affiliation":[{"name":"Department of Dermatology, University of Cologne, Cologne, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shujiro","family":"Hayashi","sequence":"additional","affiliation":[{"name":"Department of Dermatology, University of Cologne, Cologne, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Matthias","family":"Kamper","sequence":"additional","affiliation":[{"name":"Center for Biochemistry, University of Cologne, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"J\u00fcrgen","family":"Brinckmann","sequence":"additional","affiliation":[{"name":"Department of Dermatology, University of L\u00fcbeck, L\u00fcbeck, Germany"},{"name":"Institute of Virology and Cell Biology, University of L\u00fcbeck, L\u00fcbeck, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Markus","family":"Plomann","sequence":"additional","affiliation":[{"name":"Center for Biochemistry, University of Cologne, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mats","family":"Paulsson","sequence":"additional","affiliation":[{"name":"Center for Biochemistry, University of Cologne, Germany"},{"name":"Cologne Center for Musculoskeletal Biomechanics (CCMB), University of Cologne, Germany"},{"name":"Center for Molecular Medicine Cologne (CMMC), University of Cologne, Germany"},{"name":"Cologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of Cologne, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Thomas","family":"Krieg","sequence":"additional","affiliation":[{"name":"Department of Dermatology, University of Cologne, Cologne, Germany"},{"name":"Center for Molecular Medicine Cologne (CMMC), University of Cologne, Germany"},{"name":"Cologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of Cologne, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Frank","family":"Zaucke","sequence":"additional","affiliation":[{"name":"Center for Biochemistry, University of Cologne, Germany"},{"name":"Cologne Center for Musculoskeletal Biomechanics (CCMB), University of Cologne, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Beate","family":"Eckes","sequence":"additional","affiliation":[{"name":"Department of Dermatology, University of Cologne, Cologne, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"237","published-online":{"date-parts":[[2016,1,1]]},"reference":[{"key":"2021042614054855700_JCS180216C1","doi-asserted-by":"publisher","first-page":"22549","DOI":"10.1074\/jbc.M111.335935","article-title":"Collagen XII and XIV, new partners of cartilage oligomeric matrix protein in the skin extracellular matrix suprastructure","volume":"287","author":"Agarwal","year":"2012","journal-title":"J. Biol. Chem."},{"key":"2021042614054855700_JCS180216C2","doi-asserted-by":"publisher","first-page":"325","DOI":"10.1016\/j.matbio.2013.02.010","article-title":"Enhanced deposition of cartilage oligomeric matrix protein is a common feature in fibrotic skin pathologies","volume":"32","author":"Agarwal","year":"2013","journal-title":"Matrix Biol."},{"key":"2021042614054855700_JCS180216C3","doi-asserted-by":"publisher","first-page":"1882","DOI":"10.1089\/ten.tea.2011.0497","article-title":"Identification of a 3Kbp mechanoresponsive promoter region in the human cartilage oligomeric matrix protein gene","volume":"18","author":"Amanatullah","year":"2012","journal-title":"Tissue Eng. A"},{"key":"2021042614054855700_JCS180216C4","doi-asserted-by":"publisher","first-page":"735","DOI":"10.1016\/S0047-6374(01)00225-1","article-title":"Molecular mechanisms of ageing in connective tissues","volume":"122","author":"Bailey","year":"2001","journal-title":"Mech. Ageing Dev."},{"key":"2021042614054855700_JCS180216C5","doi-asserted-by":"publisher","first-page":"3872","DOI":"10.1242\/jcs.063024","article-title":"Defective granulation tissue formation in mice with specific ablation of integrin-linked kinase in fibroblasts - role of TGFbeta1 levels and RhoA activity","volume":"123","author":"Blumbach","year":"2010","journal-title":"J. Cell Sci."},{"key":"2021042614054855700_JCS180216C6","doi-asserted-by":"publisher","first-page":"330","DOI":"10.1038\/ng0795-330","article-title":"Pseudoachondroplasia and multiple epiphyseal dysplasia due to mutations in the cartilage oligomeric matrix protein gene","volume":"10","author":"Briggs","year":"1995","journal-title":"Nat. Genet."},{"key":"2021042614054855700_JCS180216C7","doi-asserted-by":"publisher","first-page":"7","DOI":"10.1007\/s00441-009-0864-0","article-title":"Suprastructures of extracellular matrices: paradigms of functions controlled by aggregates rather than molecules","volume":"339","author":"Bruckner","year":"2010","journal-title":"Cell Tissue Res."},{"key":"2021042614054855700_JCS180216C8","doi-asserted-by":"publisher","first-page":"6694","DOI":"10.1093\/emboj\/16.22.6694","article-title":"The C-propeptide domain of procollagen can be replaced with a transmembrane domain without affecting trimer formation or collagen triple helix folding during biosynthesis","volume":"16","author":"Bulleid","year":"1997","journal-title":"EMBO J."},{"key":"2021042614054855700_JCS180216C9","doi-asserted-by":"publisher","first-page":"553","DOI":"10.1083\/jcb.200312071","article-title":"Coalignment of plasma membrane channels and protrusions (fibripositors) specifies the parallelism of tendon","volume":"165","author":"Canty","year":"2004","journal-title":"J. Cell Biol."},{"key":"2021042614054855700_JCS180216C10","doi-asserted-by":"publisher","first-page":"1410","DOI":"10.1161\/CIRCRESAHA.111.256743","article-title":"Thrombospondin-4 is required for stretch-mediated contractility augmentation in cardiac muscle","volume":"109","author":"Cingolani","year":"2011","journal-title":"Circ. Res."},{"key":"2021042614054855700_JCS180216C11","doi-asserted-by":"publisher","first-page":"738","DOI":"10.1016\/j.ajpath.2011.10.033","article-title":"D469del-COMP retention in chondrocytes stimulates caspase-independent necroptosis","volume":"180","author":"Coustry","year":"2012","journal-title":"Am. J. Pathol."},{"key":"2021042614054855700_JCS180216C12","doi-asserted-by":"publisher","first-page":"927","DOI":"10.1111\/j.1432-1033.1994.tb19070.x","article-title":"Cartilage oligomeric matrix protein and thrombospondin 1. Purification from articular cartilage, electron microscopic structure, and chondrocyte binding","volume":"223","author":"Di Cesare","year":"1994","journal-title":"Eur. J. Biochem."},{"key":"2021042614054855700_JCS180216C13","doi-asserted-by":"publisher","first-page":"461","DOI":"10.1016\/S0945-053X(02)00015-X","article-title":"Matrix\u2013matrix interaction of cartilage oligomeric matrix protein and fibronectin","volume":"21","author":"Di Cesare","year":"2002","journal-title":"Matrix Biol."},{"key":"2021042614054855700_JCS180216C14","doi-asserted-by":"publisher","first-page":"505","DOI":"10.1172\/JCI0214386","article-title":"Pseudoachondroplasia is caused through both intra- and extracellular pathogenic pathways","volume":"110","author":"Dinser","year":"2002","journal-title":"J. Clin. Invest."},{"key":"2021042614054855700_JCS180216C15","doi-asserted-by":"publisher","first-page":"4","DOI":"10.1186\/1755-1536-3-4","article-title":"Cell-matrix interactions in dermal repair and scarring","volume":"3","author":"Eckes","year":"2010","journal-title":"Fibrogenesis Tissue Repair"},{"key":"2021042614054855700_JCS180216C16","doi-asserted-by":"publisher","first-page":"913","DOI":"10.1007\/s00109-014-1190-x","article-title":"Molecular and cellular basis of scleroderma","volume":"92","author":"Eckes","year":"2014","journal-title":"J. Mol. Med."},{"key":"2021042614054855700_JCS180216C17","doi-asserted-by":"publisher","first-page":"435","DOI":"10.1136\/ard.2007.086850","article-title":"Cartilage oligomeric matrix protein expression in systemic sclerosis reveals heterogeneity of dermal fibroblast responses to transforming growth factor beta","volume":"68","author":"Farina","year":"2009","journal-title":"Ann. Rheum. Dis."},{"key":"2021042614054855700_JCS180216C18","doi-asserted-by":"publisher","first-page":"580","DOI":"10.1002\/art.27220","article-title":"A four-gene biomarker predicts skin disease in patients with diffuse cutaneous systemic sclerosis","volume":"62","author":"Farina","year":"2010","journal-title":"Arthritis Rheum."},{"key":"2021042614054855700_JCS180216C19","doi-asserted-by":"publisher","first-page":"2363","DOI":"10.1096\/fj.11-190728","article-title":"Thrombospondin-4 regulates fibrosis and remodeling of the myocardium in response to pressure overload","volume":"26","author":"Frolova","year":"2012","journal-title":"FASEB J."},{"key":"2021042614054855700_JCS180216C20","doi-asserted-by":"publisher","first-page":"1989","DOI":"10.1056\/NEJMra0806188","article-title":"Scleroderma","volume":"360","author":"Gabrielli","year":"2009","journal-title":"N. Engl. J. Med."},{"key":"2021042614054855700_JCS180216C21","doi-asserted-by":"publisher","first-page":"648","DOI":"10.1074\/jbc.M704035200","article-title":"Cartilage oligomeric matrix protein protects cells against death by elevating members of the IAP family of survival proteins","volume":"283","author":"Gagarina","year":"2008","journal-title":"J. Biol. Chem."},{"key":"2021042614054855700_JCS180216C22","doi-asserted-by":"publisher","first-page":"314","DOI":"10.1038\/nature07039","article-title":"Wound repair and regeneration","volume":"453","author":"Gurtner","year":"2008","journal-title":"Nature"},{"key":"2021042614054855700_JCS180216C23","doi-asserted-by":"publisher","first-page":"31166","DOI":"10.1074\/jbc.M705735200","article-title":"COMP acts as a catalyst in collagen fibrillogenesis","volume":"282","author":"Halasz","year":"2007","journal-title":"J. Biol. Chem."},{"key":"2021042614054855700_JCS180216C24","doi-asserted-by":"publisher","first-page":"325","DOI":"10.1038\/ng0795-325","article-title":"Mutations in exon 17B of cartilage oligomeric matrix protein (COMP) cause pseudoachondroplasia","volume":"10","author":"Hecht","year":"1995","journal-title":"Nat. Genet."},{"key":"2021042614054855700_JCS180216C25","doi-asserted-by":"publisher","first-page":"625","DOI":"10.1016\/S0945-053X(98)90113-5","article-title":"Retention of cartilage oligomeric matrix protein (COMP) and cell death in redifferentiated pseudoachondroplasia chondrocytes","volume":"17","author":"Hecht","year":"1998","journal-title":"Matrix Biol."},{"key":"2021042614054855700_JCS180216C26","doi-asserted-by":"publisher","first-page":"525","DOI":"10.1016\/j.matbio.2004.09.006","article-title":"COMP mutations, chondrocyte function and cartilage matrix","volume":"23","author":"Hecht","year":"2005","journal-title":"Matrix Biol."},{"key":"2021042614054855700_JCS180216C27","doi-asserted-by":"crossref","first-page":"6132","DOI":"10.1016\/S0021-9258(18)42671-3","article-title":"Cartilage matrix proteins. An acidic oligomeric protein (COMP) detected only in cartilage","volume":"267","author":"Hedbom","year":"1992","journal-title":"J. Biol. Chem."},{"key":"2021042614054855700_JCS180216C28","doi-asserted-by":"publisher","first-page":"575","DOI":"10.1111\/j.1365-2613.2009.00695.x","article-title":"Proteoglycans and more - from molecules to biology","volume":"90","author":"Heineg\u00e5rd","year":"2009","journal-title":"Int. J. Exp. Pathol."},{"key":"2021042614054855700_JCS180216C29","doi-asserted-by":"publisher","first-page":"50","DOI":"10.1038\/nrrheum.2010.198","article-title":"The role of the cartilage matrix in osteoarthritis","volume":"7","author":"Heineg\u00e5rd","year":"2011","journal-title":"Nat. Rev. Rheumatol."},{"key":"2021042614054855700_JCS180216C30","doi-asserted-by":"publisher","first-page":"1340","DOI":"10.1016\/j.ajpath.2012.02.004","article-title":"Recent developments in myofibroblast biology: paradigms for connective tissue remodeling","volume":"180","author":"Hinz","year":"2012","journal-title":"Am. J. Pathol."},{"key":"2021042614054855700_JCS180216C31","doi-asserted-by":"publisher","first-page":"6046","DOI":"10.1074\/jbc.M009507200","article-title":"Cartilage oligomeric matrix protein interacts with type IX collagen, and disruptions to these interactions identify a pathogenetic mechanism in a bone dysplasia family","volume":"276","author":"Holden","year":"2001","journal-title":"J. Biol. Chem."},{"key":"2021042614054855700_JCS180216C32","doi-asserted-by":"publisher","first-page":"309","DOI":"10.1054\/ceca.2000.0125","article-title":"Delta 469 mutation in the type 3 repeat calcium binding domain of cartilage oligomeric matrix protein (COMP) disrupts calcium binding","volume":"27","author":"Hou","year":"2000","journal-title":"Cell Calcium"},{"key":"2021042614054855700_JCS180216C33","doi-asserted-by":"publisher","first-page":"1216","DOI":"10.1126\/science.1176009","article-title":"The extracellular matrix: not just pretty fibrils","volume":"326","author":"Hynes","year":"2009","journal-title":"Science"},{"key":"2021042614054855700_JCS180216C34","doi-asserted-by":"publisher","first-page":"495","DOI":"10.1038\/nature10822","article-title":"Ubiquitin-dependent regulation of COPII coat size and function","volume":"482","author":"Jin","year":"2012","journal-title":"Nature"},{"key":"2021042614054855700_JCS180216C35","doi-asserted-by":"publisher","first-page":"36575","DOI":"10.1074\/jbc.M101602200","article-title":"Fibroblasts in mechanically stressed collagen lattices assume a \u201csynthetic\u201d phenotype","volume":"276","author":"Kessler","year":"2001","journal-title":"J. Biol. Chem."},{"key":"2021042614054855700_JCS180216C36","doi-asserted-by":"publisher","first-page":"320","DOI":"10.1016\/j.biocel.2010.12.010","article-title":"The matrilins: modulators of extracellular matrix assembly","volume":"43","author":"Klatt","year":"2011","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"2021042614054855700_JCS180216C37","doi-asserted-by":"publisher","first-page":"10581","DOI":"10.1074\/jbc.M109944200","article-title":"Disease-causing mutations in cartilage oligomeric matrix protein cause an unstructured Ca2+ binding domain","volume":"277","author":"Kleerekoper","year":"2002","journal-title":"J. Biol. Chem."},{"key":"2021042614054855700_JCS180216C38","doi-asserted-by":"publisher","first-page":"557","DOI":"10.1016\/S0014-5793(97)01070-3","article-title":"Properties of the extracellular calcium binding module of the proteoglycan testican","volume":"414","author":"Kohfeldt","year":"1997","journal-title":"FEBS Lett."},{"key":"2021042614054855700_JCS180216C39","doi-asserted-by":"publisher","first-page":"419","DOI":"10.1083\/jcb.140.2.419","article-title":"Mice that lack thrombospondin 2 display connective tissue abnormalities that are associated with disordered collagen fibrillogenesis, an increased vascular density, and a bleeding diathesis","volume":"140","author":"Kyriakides","year":"1998","journal-title":"J. Cell Biol."},{"key":"2021042614054855700_JCS180216C40","doi-asserted-by":"publisher","first-page":"1257","DOI":"10.1016\/j.cell.2012.03.050","article-title":"A thrombospondin-dependent pathway for a protective ER stress response","volume":"149","author":"Lynch","year":"2012","journal-title":"Cell"},{"key":"2021042614054855700_JCS180216C41","doi-asserted-by":"publisher","first-page":"30993","DOI":"10.1074\/jbc.272.49.30993","article-title":"The fate of cartilage oligomeric matrix protein is determined by the cell type in the case of a novel mutation in pseudoachondroplasia","volume":"272","author":"Maddox","year":"1997","journal-title":"J. Biol. Chem."},{"key":"2021042614054855700_JCS180216C42","doi-asserted-by":"publisher","first-page":"11412","DOI":"10.1074\/jbc.275.15.11412","article-title":"A cartilage oligomeric matrix protein mutation associated with pseudoachondroplasia changes the structural and functional properties of the type 3 domain","volume":"275","author":"Maddox","year":"2000","journal-title":"J. Biol. Chem."},{"key":"2021042614054855700_JCS180216C43","doi-asserted-by":"publisher","first-page":"25294","DOI":"10.1074\/jbc.M403778200","article-title":"Interactions between the cartilage oligomeric matrix protein and matrilins: implications for matrix assembly and the pathogenesis of chondrodysplasias","volume":"279","author":"Mann","year":"2004","journal-title":"J. Biol. Chem."},{"key":"2021042614054855700_JCS180216C44","doi-asserted-by":"publisher","first-page":"293","DOI":"10.2353\/ajpath.2007.060530","article-title":"Unique matrix structure in the rough endoplasmic reticulum cisternae of pseudoachondroplasia chondrocytes","volume":"170","author":"Merritt","year":"2007","journal-title":"Am. J. Pathol."},{"key":"2021042614054855700_JCS180216C45","doi-asserted-by":"crossref","first-page":"6137","DOI":"10.1016\/S0021-9258(18)42672-5","article-title":"Electron microscopy of native cartilage oligomeric matrix protein purified from the Swarm rat chondrosarcoma reveals a five-armed structure","volume":"267","author":"Morgelin","year":"1992","journal-title":"J. Biol. Chem."},{"key":"2021042614054855700_JCS180216C46","doi-asserted-by":"publisher","first-page":"1499","DOI":"10.1083\/jcb.150.6.1499","article-title":"Embryonic lethality of molecular chaperone hsp47 knockout mice is associated with defects in collagen biosynthesis","volume":"150","author":"Nagai","year":"2000","journal-title":"J. Cell Biol."},{"key":"2021042614054855700_JCS180216C47","doi-asserted-by":"publisher","first-page":"1505","DOI":"10.1074\/jbc.M113.529933","article-title":"Matrilin-1 is essential for zebrafish development by facilitating collagen II secretion","volume":"289","author":"Neacsu","year":"2014","journal-title":"J. Biol. Chem."},{"key":"2021042614054855700_JCS180216C48","doi-asserted-by":"publisher","first-page":"217","DOI":"10.1093\/jb\/mvr143","article-title":"CHOP is a multifunctional transcription factor in the ER stress response","volume":"151","author":"Nishitoh","year":"2012","journal-title":"J. Biochem."},{"key":"2021042614054855700_JCS180216C49","doi-asserted-by":"publisher","first-page":"52","DOI":"10.1093\/hmg\/ddp466","article-title":"A mouse model offers novel insights into the myopathy and tendinopathy often associated with pseudoachondroplasia and multiple epiphyseal dysplasia","volume":"19","author":"Pirog","year":"2010","journal-title":"Hum. Mol. Genet."},{"key":"2021042614054855700_JCS180216C50","doi-asserted-by":"publisher","first-page":"869","DOI":"10.2174\/138945008785909293","article-title":"The role of cartilage oligomeric matrix protein (COMP) in skeletal disease","volume":"9","author":"Posey","year":"2008","journal-title":"Curr. Drug Targets"},{"key":"2021042614054855700_JCS180216C51","doi-asserted-by":"publisher","first-page":"1555","DOI":"10.2353\/ajpath.2009.090184","article-title":"An inducible cartilage oligomeric matrix protein mouse model recapitulates human pseudoachondroplasia phenotype","volume":"175","author":"Posey","year":"2009","journal-title":"Am. J. Pathol."},{"key":"2021042614054855700_JCS180216C52","doi-asserted-by":"publisher","first-page":"228","DOI":"10.1016\/0003-2697(60)90050-6","article-title":"A specific method for the analysis of hydroxyproline in tissues and urine","volume":"1","author":"Prockop","year":"1960","journal-title":"Anal. Biochem."},{"key":"2021042614054855700_JCS180216C53","doi-asserted-by":"publisher","first-page":"a004978","DOI":"10.1101\/cshperspect.a004978","article-title":"The collagen family","volume":"3","author":"Ricard-Blum","year":"2011","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"2021042614054855700_JCS180216C54","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.ymgmr.2014.11.005","article-title":"Insights in the etiopathology of galactosyltransferase II (GalT-II) deficiency from transcriptome-wide expression profiling of skin fibroblasts of two sisters with compound heterozygosity for two novel B3GALT6 mutations","volume":"2","author":"Ritelli","year":"2015","journal-title":"Mol. Genet. Metab. Rep."},{"key":"2021042614054855700_JCS180216C55","doi-asserted-by":"publisher","first-page":"20397","DOI":"10.1074\/jbc.273.32.20397","article-title":"Cartilage oligomeric matrix protein shows high affinity zinc-dependent interaction with triple helical collagen","volume":"273","author":"Rosenberg","year":"1998","journal-title":"J. Biol. Chem."},{"key":"2021042614054855700_JCS180216C56","doi-asserted-by":"publisher","first-page":"2301","DOI":"10.1091\/mbc.E11-02-0143","article-title":"cTAGE5 mediates collagen secretion through interaction with TANGO1 at endoplasmic reticulum exit sites","volume":"22","author":"Saito","year":"2011","journal-title":"Mol. Biol. Cell"},{"key":"2021042614054855700_JCS180216C57","doi-asserted-by":"publisher","first-page":"32587","DOI":"10.1074\/jbc.M601976200","article-title":"Disruption of extracellular matrix structure may cause pseudoachondroplasia phenotypes in the absence of impaired cartilage oligomeric matrix protein secretion","volume":"281","author":"Schmitz","year":"2006","journal-title":"J. Biol. Chem."},{"key":"2021042614054855700_JCS180216C58","doi-asserted-by":"publisher","first-page":"67","DOI":"10.1016\/j.matbio.2007.08.001","article-title":"Transgenic mice expressing D469Delta mutated cartilage oligomeric matrix protein (COMP) show growth plate abnormalities and sternal malformations","volume":"27","author":"Schmitz","year":"2008","journal-title":"Matrix Biol."},{"key":"2021042614054855700_JCS180216C59","doi-asserted-by":"publisher","first-page":"1435","DOI":"10.1038\/jid.2015.24","article-title":"Reduced granulation tissue and wound strength in the absence of alpha11beta1 integrin","volume":"135","author":"Schulz","year":"2015","journal-title":"J. Invest. Dermatol."},{"key":"2021042614054855700_JCS180216C60","doi-asserted-by":"publisher","first-page":"63","DOI":"10.1007\/978-1-59745-413-1_4","article-title":"Eukaryotic expression and purification of recombinant extracellular matrix proteins carrying the strep II tag","volume":"522","author":"Smyth","year":"2009","journal-title":"Methods Mol. Biol."},{"key":"2021042614054855700_JCS180216C61","doi-asserted-by":"publisher","first-page":"1433","DOI":"10.1038\/nprot.2013.086","article-title":"Using transmission electron microscopy and 3View to determine collagen fibril size and three-dimensional organization","volume":"8","author":"Starborg","year":"2013","journal-title":"Nat. Protoc."},{"key":"2021042614054855700_JCS180216C62","doi-asserted-by":"publisher","first-page":"4366","DOI":"10.1128\/MCB.22.12.4366-4371.2002","article-title":"Cartilage oligomeric matrix protein-deficient mice have normal skeletal development","volume":"22","author":"Svensson","year":"2002","journal-title":"Mol. Cell. Biol."},{"key":"2021042614054855700_JCS180216C63","doi-asserted-by":"publisher","first-page":"178","DOI":"10.1016\/j.matbio.2012.01.006","article-title":"Thrombospondin1 in tissue repair and fibrosis: TGF-\u03b2-dependent and independent mechanisms","volume":"31","author":"Sweetwyne","year":"2012","journal-title":"Matrix Biol."},{"key":"2021042614054855700_JCS180216C64","doi-asserted-by":"publisher","first-page":"1710","DOI":"10.2353\/ajpath.2010.090903","article-title":"The calreticulin-binding sequence of thrombospondin 1 regulates collagen expression and organization during tissue remodeling","volume":"177","author":"Sweetwyne","year":"2010","journal-title":"Am. J. Pathol."},{"key":"2021042614054855700_JCS180216C65","doi-asserted-by":"publisher","first-page":"6083","DOI":"10.1074\/jbc.M009512200","article-title":"Mutations in cartilage oligomeric matrix protein causing pseudoachondroplasia and multiple epiphyseal dysplasia affect binding of calcium and collagen I, II, and IX","volume":"276","author":"Thur","year":"2001","journal-title":"J. Biol. Chem."},{"key":"2021042614054855700_JCS180216C66","doi-asserted-by":"publisher","first-page":"349","DOI":"10.1038\/nrm809","article-title":"Myofibroblasts and mechano-regulation of connective tissue remodelling","volume":"3","author":"Tomasek","year":"2002","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"2021042614054855700_JCS180216C67","doi-asserted-by":"publisher","first-page":"1343","DOI":"10.1016\/S0002-9440(10)62353-X","article-title":"Regulation of alpha-smooth muscle actin expression in granulation tissue myofibroblasts is dependent on the intronic CArG element and the transforming growth factor-beta1 control element","volume":"166","author":"Tomasek","year":"2005","journal-title":"Am. J. Pathol."},{"key":"2021042614054855700_JCS180216C68","doi-asserted-by":"publisher","first-page":"320","DOI":"10.1006\/excr.1998.4363","article-title":"Rapid and reversible regulation of collagen XII expression by changes in tensile stress","volume":"247","author":"Tr\u00e4chslin","year":"1999","journal-title":"Exp. Cell Res."},{"key":"2021042614054855700_JCS180216C69","doi-asserted-by":"publisher","first-page":"557","DOI":"10.1172\/JCI31139","article-title":"Systemic sclerosis: a prototypic multisystem fibrotic disorder","volume":"117","author":"Varga","year":"2007","journal-title":"J. Clin. Invest."},{"key":"2021042614054855700_JCS180216C70","doi-asserted-by":"publisher","first-page":"27461","DOI":"10.1074\/jbc.M603147200","article-title":"Collagen XII interacts with avian tenascin-X through its NC3 domain","volume":"281","author":"Veit","year":"2006","journal-title":"J. Biol. Chem."},{"key":"2021042614054855700_JCS180216C71","doi-asserted-by":"publisher","first-page":"439","DOI":"10.1016\/S0945-053X(01)00148-2","article-title":"Selective intracellular retention of extracellular matrix proteins and chaperones associated with pseudoachondroplasia","volume":"20","author":"Vranka","year":"2001","journal-title":"Matrix Biol."},{"key":"2021042614054855700_JCS180216C72","doi-asserted-by":"publisher","first-page":"13243","DOI":"10.1073\/pnas.1208072109","article-title":"Molecular basis for the action of the collagen-specific chaperone Hsp47\/SERPINH1 and its structure-specific client recognition","volume":"109","author":"Widmer","year":"2012","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"2021042614054855700_JCS180216C73","doi-asserted-by":"publisher","first-page":"456","DOI":"10.1046\/j.1523-1747.1999.00528.x","article-title":"Animal model of sclerotic skin. I: local injections of bleomycin induce sclerotic skin mimicking scleroderma","volume":"112","author":"Yamamoto","year":"1999","journal-title":"J. Invest. Dermatol."},{"key":"2021042614054855700_JCS180216C74","doi-asserted-by":"publisher","first-page":"1886","DOI":"10.1242\/jcs.02921","article-title":"Interactions of primary fibroblasts and keratinocytes with extracellular matrix proteins: contribution of alpha2beta1 integrin","volume":"119","author":"Zhang","year":"2006","journal-title":"J. Cell Sci."},{"key":"2021042614054855700_JCS180216C75","doi-asserted-by":"publisher","first-page":"467","DOI":"10.1038\/sj.jid.5700546","article-title":"Integrin alpha2beta1 is required for regulation of murine wound angiogenesis but is dispensable for reepithelialization","volume":"127","author":"Zweers","year":"2007","journal-title":"J. Invest. Dermatol."}],"container-title":["Journal of Cell Science"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/journals.biologists.com\/jcs\/article-pdf\/129\/4\/706\/1941705\/jcs180216.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"http:\/\/journals.biologists.com\/jcs\/article-pdf\/doi\/10.1242\/jcs.180216\/2049449\/jcs_180216v1.pdf","content-type":"application\/pdf","content-version":"am","intended-application":"syndication"},{"URL":"http:\/\/journals.biologists.com\/jcs\/article-pdf\/doi\/10.1242\/jcs.180216\/2049449\/jcs_180216v1.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,5,18]],"date-time":"2021-05-18T17:54:06Z","timestamp":1621360446000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.biologists.com\/jcs\/article\/doi\/10.1242\/jcs.180216\/260260\/COMP-assisted-collagen-secretion-a-novel"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2016,1,1]]},"references-count":75,"URL":"https:\/\/doi.org\/10.1242\/jcs.180216","relation":{},"ISSN":["1477-9137","0021-9533"],"issn-type":[{"value":"1477-9137","type":"electronic"},{"value":"0021-9533","type":"print"}],"subject":[],"published":{"date-parts":[[2016,1,1]]},"article-number":"jcs.180216"}}