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The extracellular matrix of cartilage in the growth plate before and during calcification: Changes in composition and degradation of type II collagen

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Summary

Calcification occurs in the extracellular matrix of the hypertrophic zone of the growth plate when the extra-cellular matrix volume is reduced to a minimum and alkaline phosphatase content is maximal. The present study shows that significant quantitative and qualitative changes occur in the composition and structure of macromolecules in the extracellular matrix before and during calcification in the proximal tibial growth plate of the bovine fetus. These were detected in part by using microchemical and microimmuno-chemical analyses of sequential transverse frozen sections at chemical analyses of sequential transverse frozen sections at defined sites throughout the growth plate. Concentrations of matrix molecules in the extracellular matrix have not previously been determined biochemically. They were measured per unit matrix volume by using combined immunochemical/chemical-histomorphometric analyses. The concentrations within the extracellular matrix of the C-propeptide of type II collagen, aggregating proteoglycan (aggrecan), and hyaluronic acid all progressively increased in the maturing and hypertrophic zones, being maximal (or near maximal) at the time of initiation of mineralization. These results for proteoglycan are contrary to some earlier reports of a loss of proteoglycan prior to mineralization which measured the tissue content of proteoglycan rather than that present in the extracellular matrix, the volume of which is progressively reduced as the growth plate matures. The C-propeptide data provides a quantitative confirmation of previous immunohistochemical studies. Total collagen concentration (measured as hydroxyproline) in the extracellular matrix initially increased through the proliferating and maturing zones but then rapidly decreased in the hypertrophic zone. Immunohistochemical studies revealed that this is associated with the unwinding of the triple helix of type II collagen (previously shown to result from cleavage) which starts in pericellular sites in the zone of maturation (when type X collagen is first synthesized) and then extends throughout the hypertrophic zone. The significance of these matrix changes in the development and mineralization of the growth plate is discussed.

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Author notes

  1. Yasumoto Matsui

    Present address: Department of Orthopaedic Surgery, School of Medicine, Nagoya University, 65, Tsurumai-cho, Showa-ku, 466, Nagoya, Japan

  2. George R. Dodge

    Present address: Department of Pathology and Cell Biology, Jefferson Medical College, 1020 Locust Street, Alumni Hall, Room 249, 19107, Philadelphia, Pennsylvania, USA

Authors and Affiliations

  1. Joint Diseases Laboratory, Shriners Hospital for Crippled Children, 1529 Cedar Avenue, H3G 1A6, Montreal, Quebec, Canada

    Mauro Alini, Yasumoto Matsui, George R. Dodge & A. Robin Poole

  2. Division of Surgical Research, Department of Surgery, McGill University, 1529 Cedar Avenue, H3G 1A6, Montreal, Quebec, Canada

    Mauro Alini, Yasumoto Matsui, George R. Dodge & A. Robin Poole

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  1. Mauro Alini
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Alini, M., Matsui, Y., Dodge, G.R. et al. The extracellular matrix of cartilage in the growth plate before and during calcification: Changes in composition and degradation of type II collagen. Calcif Tissue Int 50, 327–335 (1992). https://doi.org/10.1007/BF00301630

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  • DOI: https://doi.org/10.1007/BF00301630

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