Affiliation:
1. The Second Department of Oro-Maxillo-Facial Surgery
2. Department of Biochemistry, School of Dentistry, Aichi-Gakuin University, Nagoya 464, Japan
Abstract
Three α chains of type V collagen - α1(V), α2(V), and α3(V)- were initially demonstrated together with the expected collagen types I and III in the pepsin-soluble fraction of both normal mandibular bone and tooth extraction wound tissues of rabbits, as analyzed by sodium dodecyl sulfate-gel electrophoresis. The total collagen content of each extraction wound, as determined by the hydroxyproline assay, was observed to increase continuously from day 5 through day 17 and then leveled off or decreased. The ratio of type V to type I collagen was significantly higher in the initial stage of wound healing and decreased sharply down to the level of mandibular bone by day 5. The ratio of type III to type I collagen in the pepsin-soluble fraction increased and reached a maximum on day 5, whereas it was maximal on day 7 in the cyanogen bromide-soluble fraction, and thereafter decreased gradually in both fractions. The ratio for the pepsin-soluble fraction was, however, significantly higher than that for the cyanogen bromide-soluble fraction in the early stage of wound healing.
Cited by
37 articles.
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