The assembly and remodeling of the extracellular matrix in the growth plate in relationship to mineral deposition and cellular hypertrophy: an in situ study of collagens II and IX and proteoglycan.

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  • Author(s): Mwale F;Mwale F; Tchetina E; Wu CW; Poole AR
  • Source:
    Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research [J Bone Miner Res] 2002 Feb; Vol. 17 (2), pp. 275-83.
  • Publication Type:
    Journal Article; Research Support, Non-U.S. Gov't
  • Language:
    English
  • Additional Information
    • Source:
      Publisher: American Society for Bone and Mineral Research Country of Publication: United States NLM ID: 8610640 Publication Model: Print Cited Medium: Print ISSN: 0884-0431 (Print) Linking ISSN: 08840431 NLM ISO Abbreviation: J Bone Miner Res Subsets: MEDLINE
    • Publication Information:
      Publication: 2000- : Washington, DC : American Society for Bone and Mineral Research
      Original Publication: New York : Mary Ann Liebert, Inc., c1986-
    • Subject Terms:
      Collagen Type I/*metabolism ; Collagen Type IX/*metabolism ; Extracellular Matrix/*physiology ; Growth Plate/*metabolism ; Proteoglycans/*metabolism; Animals ; Calcium/analysis ; Cattle ; Collagen Type IX/genetics ; Collagenases/genetics ; Collagenases/metabolism ; Gene Expression Regulation, Developmental ; Immunoassay/methods ; Matrix Metalloproteinase 13 ; Phosphates/analysis ; Tibia/embryology
    • Abstract:
      The recent development of new specific immunoassays has provided an opportunity to study the assembly and resorption of type II and IX collagens of the extracellular matrix in relationship to endochondral calcification in situ. Here, we describe how in the bovine fetal physis prehypertrophic chondrocytes deposit an extensive extracellular matrix that, initially, is rich in both type II and type IX collagens and proteoglycan (PG; principally, aggrecan). The majority of the alpha1(IX)-chains lack the NC4 domain consistent with our previous studies with cultured chondrocytes. During assembly, the molar ratio of type II/COL2 domain of the alpha1(IX)-chain varied from 8:1 to 25:1. An increase in the content of Ca2+ and inorganic phosphate (Pi) was initiated in the prehypertrophic zone when the NC4 domain was removed selectively from the alpha1(IX)-chain. This was followed by the progressive loss of the alpha1(IX) COL2 domain and type II collagen. In the hypertrophic zone, the Ca2+/Pi molar ratio ranged from 1.56 to a maximum of 1.74, closely corresponding to that of mature hydroxyapatite (1.67). The prehypertrophic zone had an average ratio Ca2+/Pi ranging from 0.25 to 1, suggesting a phase transformation. At hypertrophy, when mineral content was maximal, type II collagen was reduced maximally in content coincident with a peak of cleavage of this molecule by collagenase when matrix metalloproteinase 13 (MMP-13) expression was maximal. In contrast, PG (principally aggrecan) was retained when hydroxyapatite was formed consistent with the view that this PG does not inhibit and might promote calcification in vivo. Taken together with earlier studies, these findings show that matrix remodeling after assembly is linked closely to initial changes in Ca2+ and Pi to subsequent cellular hypertrophy and mineralization. These changes involve a progressive and selective removal of types II and IX collagens with the retention of the PG aggrecan.
    • Accession Number:
      0 (Collagen Type I)
      0 (Collagen Type IX)
      0 (Phosphates)
      0 (Proteoglycans)
      EC 3.4.24.- (Collagenases)
      EC 3.4.24.- (Matrix Metalloproteinase 13)
      SY7Q814VUP (Calcium)
    • Publication Date:
      Date Created: 20020129 Date Completed: 20020802 Latest Revision: 20131121
    • Publication Date:
      20231215
    • Accession Number:
      10.1359/jbmr.2002.17.2.275
    • Accession Number:
      11811558