title: The extracellular matrix of cartilage in the growth plate before and during calcification: changes in composition and degradation of type II collagen.
abstract: Calcification occurs in the extracellular matrix of the hypertrophic zone of the growth plate when the extracellular 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 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 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.(ABSTRACT TRUNCATED AT 250 WORDS)
authors.affiliation: Joint Diseases Laboratory, Shriners Hospital for Crippled Children, Montreal, Quebec, Canada.
authors.forename: M
authors.initials: M
authors.lastname: Alini
authors.forename: Y
authors.initials: Y
authors.lastname: Matsui
authors.forename: G R
authors.initials: GR
authors.lastname: Dodge
authors.forename: A R
authors.initials: AR
authors.lastname: Poole
mesh_terms: D000135:Acid Phosphatase / Q000378:metabolism; D000818:Animals; D002113:Calcification, Physiologic; D002135:Calcium-Binding Proteins / Q000032:analysis; D002417:Cattle; D003094:Collagen / Q000032:analysis / Q000378:metabolism*; D024043:Collagen Type II; D005109:Extracellular Matrix / Q000378:metabolism; D005333:Fetus / Q000378:metabolism; D006132:Growth Plate / Q000737:chemistry / Q000378:metabolism*; D006820:Hyaluronic Acid / Q000378:metabolism; D006909:Hydroxyproline / Q000378:metabolism; D007150:Immunohistochemistry; D011509:Proteoglycans / Q000378:metabolism; D013977:Tibia / Q000737:chemistry / Q000378:metabolism
chemical_list: D002135:Calcium-Binding Proteins; D024043:Collagen Type II; D011509:Proteoglycans; C040072:chondrocalcin; D006820:Hyaluronic Acid; D003094:Collagen; D000135:Acid Phosphatase; D006909:Hydroxyproline