Biochemical characterization of fracture callus proteoglycans.
The changes in proteoglycan molecules during the initial stages of fracture healing in rats were characterized. Following extraction of callus proteoglycan components with dissociative solvents, the components were purified in a cesium chloride density gradient. The recovered proteoglycans were characterized with respect to their molecular size distribution using gel filtration chromatography and a centrifugal transport methodology. During this early healing period, a decrease was observed in the relative proportion of the aggregate and in the hydrodynamic size and sedimentation coefficients of these molecules. While some molecular degradation could have occurred during the early stages of fracture healing, the dominant change of the proteoglycan molecules seemed to be disaggregation. No significant difference was observed in the proportion of aggregates reformed when exogenous hyaluronate and link glycoproteins were allowed to interact with the two corresponding monomer preparations. The molecular changes of the proteoglycan molecules seem to parallel those occurring during endochondral calcification of rat epiphyseal cartilage.
D000818:Animals; D002146:Bony Callus / Q000032:analysis*; D002499:Centrifugation, Density Gradient; D002850:Chromatography, Gel; D006595:Hexosamines / Q000032:analysis; D008297:Male; D011509:Proteoglycans / Q000032:analysis*; D051381:Rats; D014574:Uronic Acids / Q000032:analysis; D014945:Wound Healing
D006595:Hexosamines; D011509:Proteoglycans; D014574:Uronic Acids