000127020 001__ 127020
000127020 005__ 20240228140901.0
000127020 0247_ $$2doi$$a10.1002/jbmr.2484
000127020 0247_ $$2pmid$$apmid:25704664
000127020 0247_ $$2ISSN$$a0884-0431
000127020 0247_ $$2ISSN$$a1523-4681
000127020 0247_ $$2altmetric$$aaltmetric:3950357
000127020 037__ $$aDKFZ-2017-03046
000127020 041__ $$aeng
000127020 082__ $$a610
000127020 1001_ $$aLinz, Andrea$$b0
000127020 245__ $$aER Stress During the Pubertal Growth Spurt Results in Impaired Long-Bone Growth in Chondrocyte-Specific ERp57 Knockout Mice.
000127020 260__ $$aHoboken, NJ [u.a.]$$bWiley$$c2015
000127020 3367_ $$2DRIVER$$aarticle
000127020 3367_ $$2DataCite$$aOutput Types/Journal article
000127020 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article$$bjournal$$mjournal$$s1521624785_920
000127020 3367_ $$2BibTeX$$aARTICLE
000127020 3367_ $$2ORCID$$aJOURNAL_ARTICLE
000127020 3367_ $$00$$2EndNote$$aJournal Article
000127020 520__ $$aLong-bone growth by endochondral ossification is cooperatively accomplished by chondrocyte proliferation, hypertrophic differentiation, and appropriate secretion of collagens, glycoproteins, and proteoglycans into the extracellular matrix (ECM). Before folding and entering the secretory pathway, ECM macromolecules in general are subject to extensive posttranslational modification, orchestrated by chaperone complexes in the endoplasmic reticulum (ER). ERp57 is a member of the protein disulfide isomerase (PDI) family and facilitates correct folding of newly synthesized glycoproteins by rearrangement of native disulfide bonds. Here, we show that ERp57-dependent PDI activity is essential for postnatal skeletal growth, especially during the pubertal growth spurt characterized by intensive matrix deposition. Loss of ERp57 in growth plates of cartilage-specific ERp57 knockout mice (ERp57 KO) results in ER stress, unfolded protein response (UPR), reduced proliferation, and accelerated apoptotic cell death of chondrocytes. Together this results in a delay of long-bone growth with the following characteristics: (1) enlarged growth plates; (2) expanded hypertrophic zones; (3) retarded osteoclast recruitment; (4) delayed remodeling of the proteoglycan-rich matrix; and (5) reduced numbers of bone trabeculae. All the growth plate and bone abnormalities, however, become attenuated after the pubertal growth spurt, when protein synthesis is decelerated and, hence, ERp57 function is less essential.
000127020 536__ $$0G:(DE-HGF)POF3-314$$a314 - Tumor immunology (POF3-314)$$cPOF3-314$$fPOF III$$x0
000127020 588__ $$aDataset connected to CrossRef, PubMed,
000127020 650_7 $$0EC 5.3.4.1$$2NLM Chemicals$$aPdia3 protein, mouse
000127020 650_7 $$0EC 5.3.4.1$$2NLM Chemicals$$aProtein Disulfide-Isomerases
000127020 7001_ $$aKnieper, Yvonne$$b1
000127020 7001_ $$aGronau, Tobias$$b2
000127020 7001_ $$aHansen, Uwe$$b3
000127020 7001_ $$aAszodi, Attila$$b4
000127020 7001_ $$aGarbi, Natalio$$b5
000127020 7001_ $$0P:(DE-He78)5f9901fc60b769b523d0dd8e79b3fe08$$aHämmerling, Günter$$b6$$udkfz
000127020 7001_ $$aPap, Thomas$$b7
000127020 7001_ $$aBruckner, Peter$$b8
000127020 7001_ $$aDreier, Rita$$b9
000127020 773__ $$0PERI:(DE-600)2008867-X$$a10.1002/jbmr.2484$$gVol. 30, no. 8, p. 1481 - 1493$$n8$$p1481 - 1493$$tJournal of bone and mineral research$$v30$$x0884-0431$$y2015
000127020 909CO $$ooai:inrepo02.dkfz.de:127020$$pVDB
000127020 9101_ $$0I:(DE-588b)2036810-0$$6P:(DE-He78)5f9901fc60b769b523d0dd8e79b3fe08$$aDeutsches Krebsforschungszentrum$$b6$$kDKFZ
000127020 9131_ $$0G:(DE-HGF)POF3-314$$1G:(DE-HGF)POF3-310$$2G:(DE-HGF)POF3-300$$3G:(DE-HGF)POF3$$4G:(DE-HGF)POF$$aDE-HGF$$bGesundheit$$lKrebsforschung$$vTumor immunology$$x0
000127020 9141_ $$y2015
000127020 915__ $$0StatID:(DE-HGF)0300$$2StatID$$aDBCoverage$$bMedline
000127020 915__ $$0StatID:(DE-HGF)0310$$2StatID$$aDBCoverage$$bNCBI Molecular Biology Database
000127020 915__ $$0StatID:(DE-HGF)0100$$2StatID$$aJCR$$bJ BONE MINER RES : 2015
000127020 915__ $$0StatID:(DE-HGF)0200$$2StatID$$aDBCoverage$$bSCOPUS
000127020 915__ $$0StatID:(DE-HGF)0199$$2StatID$$aDBCoverage$$bThomson Reuters Master Journal List
000127020 915__ $$0StatID:(DE-HGF)0110$$2StatID$$aWoS$$bScience Citation Index
000127020 915__ $$0StatID:(DE-HGF)0150$$2StatID$$aDBCoverage$$bWeb of Science Core Collection
000127020 915__ $$0StatID:(DE-HGF)0111$$2StatID$$aWoS$$bScience Citation Index Expanded
000127020 915__ $$0StatID:(DE-HGF)1030$$2StatID$$aDBCoverage$$bCurrent Contents - Life Sciences
000127020 915__ $$0StatID:(DE-HGF)1050$$2StatID$$aDBCoverage$$bBIOSIS Previews
000127020 915__ $$0StatID:(DE-HGF)9905$$2StatID$$aIF >= 5$$bJ BONE MINER RES : 2015
000127020 9201_ $$0I:(DE-He78)D050-20160331$$kD050$$lMolekulare Immunologie$$x0
000127020 980__ $$ajournal
000127020 980__ $$aVDB
000127020 980__ $$aI:(DE-He78)D050-20160331
000127020 980__ $$aUNRESTRICTED