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      Osteoblast-derived Laminin-332 is a novel negative regulator of osteoclastogenesis in bone microenvironments

      Author(s): , , , , ,
      Publication date Created:
      Publication date (Print):
      Journal: Laboratory Investigation
      Publisher: Springer Nature

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          c-Fos: a key regulator of osteoclast-macrophage lineage determination and bone remodeling.

          A E Grigoriadis, Z. Wang, M G Cecchini … (1994)
          Mice lacking the proto-oncogene c-fos develop the bone disease osteopetrosis. Fos mutant mice were found to have a block in the differentiation of bone-resorbing osteoclasts that was intrinsic to hematopoietic cells. Bone marrow transplantation rescued the osteopetrosis, and ectopic c-fos expression overcame this differentiation block. The lack of Fos also caused a lineage shift between osteoclasts and macrophages that resulted in increased numbers of bone marrow macrophages. These results identify Fos as a key regulator of osteoclast-macrophage lineage determination in vivo and provide insights into the molecular mechanisms underlying metabolic bone diseases.
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            The murine mutation osteopetrosis is in the coding region of the macrophage colony stimulating factor gene.

            H Yoshida, S. Hayashi, T. Kunisada … (1990)
            Mice homozygous for the recessive mutation osteopetrosis (op) on chromosome 3 have a restricted capacity for bone remodelling, and are severely deficient in mature macrophages and osteoclasts. Both cell populations originate from a common haemopoietic progenitor. As op/op mice are not cured by transplants of normal bone marrow cells, the defects in op/op mice may be associated with an abnormal haematopoietic microenvironment rather than with an intrinsic defect in haematopoietic progenitors. To investigate the molecular and biochemical basis of the defects caused by the op mutation, we established primary fibroblast cell lines from op/op mice and tested the ability of these cell lines to support the proliferation of macrophage progenitors. We show that op/op fibroblasts are defective in production of functional macrophage colony-stimulating factor (M-CSF), although its messenger RNA (Csfm mRNA) is present at normal levels. This defect in M-CSF production and the recent mapping of the Csfm structural gene near op on chromosome 3 suggest that op is a mutation within the Csfm gene itself. We have sequenced Csfm complementary DNA prepared from op/op fibroblasts and found a single base pair insertion in the coding region of the Csfm gene that generates a stop codon 21 base pairs downstream. Thus, the op mutation is within the Csfm coding region and we conclude that the pathological changes in this mutant result from the absence of M-CSF.
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              The laminin family.

              Monique Aumailley (2016)
              Laminins are large molecular weight glycoproteins constituted by the assembly of three disulfide-linked polypeptides, the α, β and γ chains. The human genome encodes 11 genetically distinct laminin chains. Structurally, laminin chains differ by the number, size and organization of a few constitutive domains, endowing the various members of the laminin family with common and unique important functions. In particular, laminins are indispensable building blocks for cellular networks physically bridging the intracellular and extracellular compartments and relaying signals critical for cellular behavior, and for extracellular polymers determining the architecture and the physiology of basement membranes.
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                Author and article information

                Journal
                Title: Laboratory Investigation
                Abbreviated Title: Lab Invest
                Publisher: Springer Nature
                ISSN (Print): 0023-6837
                ISSN (Electronic): 1530-0307
                Publication date Created: June 05 2017
                Publication date (Print): June 05 2017
                Volume:
                Issue:
                Article
                DOI: 10.1038/labinvest.2017.55
                PubMed ID: 28581488
                SO-VID: b39cd7c7-6000-4409-90e8-6194c563acef
                Copyright © © 2017
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