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@ARTICLE{Scilabra:139205,
      author       = {Scilabra, Simone D and Yamamoto, Kazuhiro and Pigoni,
                      Martina and Sakamoto, Kazuma and Müller, Stephan A and
                      Papadopoulou, Alkmini and Lichtenthaler, Stefan F and
                      Troeberg, Linda and Nagase, Hideaki and Kadomatsu, Kenji},
      title        = {{D}issecting the interaction between tissue inhibitor of
                      metalloproteinases-3 ({TIMP}-3) and low density lipoprotein
                      receptor-related protein-1 ({LRP}-1): {D}evelopment of a
                      '{TRAP}' to increase levels of {TIMP}-3 in the tissue.},
      journal      = {Matrix biology},
      volume       = {59},
      issn         = {0945-053X},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier},
      reportid     = {DZNE-2020-05527},
      pages        = {69-79},
      year         = {2017},
      abstract     = {Tissue inhibitor of metalloproteinases 3 (TIMP-3) is a key
                      regulator of extracellular matrix turnover for its ability
                      to inhibit matrix metalloproteinases (MMPs), adamalysin-like
                      metalloproteinases (ADAMs) and ADAMs with thrombospondin
                      motifs (ADAMTSs). TIMP-3 is a secreted protein whose
                      extracellular levels are regulated by endocytosis via the
                      low-density-lipoprotein receptor-related protein-1 (LRP-1).
                      In this study we developed a molecule able to 'trap' TIMP-3
                      extracellularly, thereby increasing its tissue
                      bioavailability. LRP-1 contains four ligand-binding
                      clusters. In order to investigate the TIMP-3 binding site on
                      LRP-1, we generated soluble minireceptors (sLRPs) containing
                      the four distinct binding clusters or part of each cluster.
                      We used an array of biochemical methods to investigate the
                      binding of TIMP-3 to different sLRPs. We found that TIMP-3
                      binds to the ligand-binding cluster II of the receptor with
                      the highest affinity and a soluble minireceptor containing
                      the N-terminal half of cluster II specifically blocked
                      TIMP-3 internalization, without affecting the turnover of
                      metalloproteinases. Mass spectrometry-based secretome
                      analysis showed that this minireceptor, named T3TRAP,
                      selectively increased TIMP-3 levels in the extracellular
                      space and inhibited constitutive shedding of a number of
                      cell surface proteins. In conclusion, T3TRAP represents a
                      biological tool that can be used to modulate TIMP-3 levels
                      in the tissue and could be potentially developed as a
                      therapy for diseases characterized by a deficit of TIMP-3,
                      including arthritis.},
      keywords     = {Animals / Binding Sites / COS Cells / Cell Line, Tumor /
                      Chlorocebus aethiops / Endocytosis / Epithelial Cells:
                      cytology / Epithelial Cells: metabolism / Extracellular
                      Matrix: chemistry / Extracellular Matrix: metabolism / Gene
                      Expression Regulation / HEK293 Cells / Humans / Kinetics /
                      Low Density Lipoprotein Receptor-Related Protein-1: genetics
                      / Low Density Lipoprotein Receptor-Related Protein-1:
                      metabolism / Molecular Sequence Annotation / Neuroglia:
                      cytology / Neuroglia: metabolism / Protein Binding / Protein
                      Interaction Domains and Motifs / Protein Interaction Mapping
                      / Protein Transport / Receptors, Artificial: genetics /
                      Receptors, Artificial: metabolism / Recombinant Proteins:
                      genetics / Recombinant Proteins: metabolism / Signal
                      Transduction / Solubility / Tissue Inhibitor of
                      Metalloproteinase-3: genetics / Tissue Inhibitor of
                      Metalloproteinase-3: metabolism / Transfection / LRP1
                      protein, human (NLM Chemicals) / Low Density Lipoprotein
                      Receptor-Related Protein-1 (NLM Chemicals) / Receptors,
                      Artificial (NLM Chemicals) / Recombinant Proteins (NLM
                      Chemicals) / TIMP3 protein, human (NLM Chemicals) / Tissue
                      Inhibitor of Metalloproteinase-3 (NLM Chemicals)},
      cin          = {AG Lichtenthaler / Ext LMU},
      ddc          = {610},
      cid          = {I:(DE-2719)1110006 / I:(DE-2719)5000048},
      pnm          = {342 - Disease Mechanisms and Model Systems (POF3-342)},
      pid          = {G:(DE-HGF)POF3-342},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:27476612},
      doi          = {10.1016/j.matbio.2016.07.004},
      url          = {https://pub.dzne.de/record/139205},
}