Abstract
Comparison of the rates of synthesis, conversion, and maturation of type I and type III collagens in rat periodontal tissues.
Highlights
Procollagen synthesis, procollagen conversion, and collagen maturation in functional rat periodontal tissues were compared for type I and III collagens using a combination of sodium dodecyl sulfate-polyacrylamide gel electrophoresis and fluorography to separate and quantitate radiolabeled collagen molecules
The high specific radioactivities of insoluble collagens obtained in these tissues shortly after the administration of radiolabeled precursors has permitted the use of sodium dodecyl sulfatepolyacrylamide slab gel electrophoresis in combination with fluorography for the analysis of the labeled collagens in the same manner as the collagens produced by cell cultures
The migration of the slowest band was sensitive to treatment with mercaptoethanol and in the absence of reducing agent migrated with type I y-chains. This material was judged to consist of type III collagen a-chains since its behavior on electrophoresis was indistinguishable from the type III colIagen produced by monkey periodontal ligament fibroblasts which has been characterized by CNBr-peptide patterns [5]
Summary
Procollagen synthesis, procollagen conversion, and collagen maturation in functional rat periodontal tissues were compared for type I and III collagens using a combination of sodium dodecyl sulfate-polyacrylamide gel electrophoresis and fluorography to separate and quantitate radiolabeled collagen molecules. Similar values for the corresponding tissues were obtained when the a-chains from pepsin-solubilized insoluble collagen were analyzed, both calorimetrically and fluorographically These results demonstrate that despite differences in procollagen processing, types I and III collagen are metabolized at similar rates during the rapid turnover of collagen in periodontal tissues. In the only other in uiuo study, the high rate of remodeling of collagen in the skin of rapidly growing rats has been shown to involve both type I and III collagens [17]. The unusually high turnover of collagen in the rat periodontal tissues [18,19,20] provides a unique opportunity for studying both the relative turnover rates of type I and type III collagen and the rates of conversion of their precursors. Aorta was included in this study for comparative purposes, since it contains a high proportion of type III collagen [21] and is remodeled quite rapidly [22]
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