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@ARTICLE{Linz:127020,
      author       = {A. Linz and Y. Knieper and T. Gronau and U. Hansen and A.
                      Aszodi and N. Garbi and G. Hämmerling$^*$ and T. Pap and P.
                      Bruckner and R. Dreier},
      title        = {{ER} {S}tress {D}uring the {P}ubertal {G}rowth {S}purt
                      {R}esults in {I}mpaired {L}ong-{B}one {G}rowth in
                      {C}hondrocyte-{S}pecific {ER}p57 {K}nockout {M}ice.},
      journal      = {Journal of bone and mineral research},
      volume       = {30},
      number       = {8},
      issn         = {0884-0431},
      address      = {Hoboken, NJ [u.a.]},
      publisher    = {Wiley},
      reportid     = {DKFZ-2017-03046},
      pages        = {1481 - 1493},
      year         = {2015},
      abstract     = {Long-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.},
      keywords     = {Pdia3 protein, mouse (NLM Chemicals) / Protein
                      Disulfide-Isomerases (NLM Chemicals)},
      cin          = {D050},
      ddc          = {610},
      cid          = {I:(DE-He78)D050-20160331},
      pnm          = {314 - Tumor immunology (POF3-314)},
      pid          = {G:(DE-HGF)POF3-314},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:25704664},
      doi          = {10.1002/jbmr.2484},
      url          = {https://inrepo02.dkfz.de/record/127020},
}