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Deficiency of the DSPP-cleaving enzymes meprin α and meprin ß does not result in dentin malformation in mice.
Arnold, Philipp; Koopmann, Lara; Peters, Florian; Birkenfeld, Falk; Goff, Sandrine Vadon-Le; Damm, Timo; Qin, Chunlin; Moali, Catherine; Lucius, Ralph; Becker-Pauly, Christoph.
Affiliation
  • Arnold P; Anatomical Institute, Kiel University, Otto-Hahn-Platz 8, 24118, Kiel, Germany. p.arnold@anat.uni-kiel.de.
  • Koopmann L; Anatomical Institute, Kiel University, Otto-Hahn-Platz 8, 24118, Kiel, Germany.
  • Peters F; Biochemical Institute, Kiel University, Otto-Hahn-Platz 9, 24118, Kiel, Germany.
  • Birkenfeld F; Department of Oral and Maxillofacial Surgery, University Hospital Schleswig-Holstein, Arnold-Heller-Str. 16, 24105, Kiel, Germany.
  • Goff SV; Department of Tissue Biology and Therapeutic Engineering, Unité Mixte de Recherche 5305, Centre National de la Recherche Scientifique/University of Lyon, 69367, Lyon Cedex 7, France.
  • Damm T; Section Biomedical Imaging, Department of Radiology and Neurology, University Hospital Schleswig-Holstein, Am Botanischen Garten 18, 24118, Kiel, Germany.
  • Qin C; Department of Biomedical Sciences, Texas A&M University Baylor College of Dentistry, 3302 Gaston Avenue, 75246, Dallas, TX, USA.
  • Moali C; Department of Tissue Biology and Therapeutic Engineering, Unité Mixte de Recherche 5305, Centre National de la Recherche Scientifique/University of Lyon, 69367, Lyon Cedex 7, France.
  • Lucius R; Anatomical Institute, Kiel University, Otto-Hahn-Platz 8, 24118, Kiel, Germany.
  • Becker-Pauly C; Biochemical Institute, Kiel University, Otto-Hahn-Platz 9, 24118, Kiel, Germany.
Cell Tissue Res ; 367(2): 351-358, 2017 02.
Article in En | MEDLINE | ID: mdl-27628095
ABSTRACT
Formation of dentin requires the maturation of procollagen I and the proteolytic processing of the dentin sialophosphoprotein (DSPP). These cleavage events can be facilitated by the metalloproteinases meprin α and meprin ß as well as by bone morphogenetic protein 1 (BMP-1). All three enzymes have been shown to play important roles during collagen I maturation in vivo and their potential in cleaving DSPP was demonstrated in vitro. Hence, it has been discussed whether meprin α, meprin ß, BMP-1 or all three are crucial factors in the onset and progression of dentin-related diseases and this issue is addressed here. In this study, we compare the incisors and molars of meprin α (Mep1a -/-)- and meprin ß (Mep1b -/-)-deficient mice with wild-type (WT) controls on the macroscopic and microscopic level. The dentin was evaluated towards the bone mineral density, dentin volume, calcification and collagen matrix integrity. Using immunohistochemistry, we could identify meprin ß, BMP-1 and DSPP/DSP in the pre-dentin of WT mice. Nevertheless, no significant dentin malformation was observed in Mep1b -/- or Mep1a -/- deficient mice.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Phosphoproteins / Sialoglycoproteins / Metalloendopeptidases / Extracellular Matrix Proteins / Dentin Type of study: Prognostic_studies Limits: Animals / Humans Language: En Journal: Cell Tissue Res Year: 2017 Document type: Article Affiliation country: Germany

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Phosphoproteins / Sialoglycoproteins / Metalloendopeptidases / Extracellular Matrix Proteins / Dentin Type of study: Prognostic_studies Limits: Animals / Humans Language: En Journal: Cell Tissue Res Year: 2017 Document type: Article Affiliation country: Germany
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