BMP Signaling Mediated by BMPR1A in Osteoclasts Negatively Regulates Osteoblast Mineralization Through Suppression of Cx43.

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  • Author(s): Shi C;Shi C;Shi C; Zhang H; Zhang H; Louie K; Louie K; Mishina Y; Mishina Y; Sun H; Sun H
  • Source:
    Journal of cellular biochemistry [J Cell Biochem] 2017 Mar; Vol. 118 (3), pp. 605-614. Date of Electronic Publication: 2016 Sep 30.
  • Publication Type:
    Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
  • Language:
    English
  • Additional Information
    • Source:
      Publisher: Wiley-Liss Country of Publication: United States NLM ID: 8205768 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1097-4644 (Electronic) Linking ISSN: 07302312 NLM ISO Abbreviation: J Cell Biochem Subsets: MEDLINE
    • Publication Information:
      Publication: <2004>- : Hoboken, NJ : Wiley-Liss
      Original Publication: New York : Liss, c1982-
    • Subject Terms:
      Bone Morphogenetic Protein Receptors, Type I/*metabolism ; Bone Morphogenetic Proteins/*metabolism ; Calcification, Physiologic/*physiology ; Connexin 43/*metabolism ; Osteoblasts/*metabolism ; Osteoclasts/*metabolism ; Signal Transduction/*physiology; Animals ; Bone Morphogenetic Protein Receptors, Type I/genetics ; Bone Morphogenetic Proteins/genetics ; Cell Communication/physiology ; Connexin 43/genetics ; Mice ; Mice, Knockout ; Osteoblasts/cytology
    • Abstract:
      Osteoblasts and osteoclasts are well orchestrated through different mechanisms of communication during bone remodeling. Previously, we found that osteoclast-specific disruption of one of the BMP receptors, Bmpr1a, results in increased osteoblastic bone formation in mice. We hypothesized that BMPR1A signaling in osteoclasts regulates production of either membrane bound proteins or secreted molecules that regulated osteoblast differentiation. In our current study, we co-cultured wild-type osteoblasts with either control osteoclasts or osteoclasts lacking BMPR1A signaling activity. We found that loss of Bmpr1a in osteoclasts promoted osteoblast mineralization in vitro. Further, we found that the expression of Cx43/Gja1 in the mutant osteoclasts was increased, which encoded for one of the gap junction proteins connexin 43/gap junction alpha 1. Knockdown of Gja1 in the mutant osteoclasts for Bmpr1a reduced osteoblastic mineralization when co-cultured. Our findings suggest that GJA1 may be one of the downstream targets of BMPR1A signaling in osteoclasts that mediates osteoclast-osteoblast communication during bone remodeling. J. Cell. Biochem. 118: 605-614, 2017. © 2016 Wiley Periodicals, Inc.
      (© 2016 Wiley Periodicals, Inc.)
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    • Grant Information:
      R01 DE020843 United States DE NIDCR NIH HHS; T32 DE007057 United States DE NIDCR NIH HHS
    • Contributed Indexing:
      Keywords: BMPR1A; CONNEXIN 43/GJA1; GAP JUNCTION; OSTEOBLAST; OSTEOCLAST
    • Accession Number:
      0 (Bone Morphogenetic Proteins)
      0 (Connexin 43)
      0 (GJA1 protein, mouse)
      EC 2.7.11.30 (Bmpr1a protein, mouse)
      EC 2.7.11.30 (Bone Morphogenetic Protein Receptors, Type I)
    • Publication Date:
      Date Created: 20160921 Date Completed: 20171030 Latest Revision: 20181113
    • Publication Date:
      20231215
    • Accession Number:
      PMC5813677
    • Accession Number:
      10.1002/jcb.25746
    • Accession Number:
      27649478