ISSN:
1600-0714
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Medicine
Notes:
Abstract. Of a total of 80 allogenic demineralized guinea pig dentin samples, 60 were treated with collagenase or trypsin, leaving a group of 20 controls. The dentin was then either subjected to amino acid analysis and transmission electron microscopy, or implanted in the abdominal muscles of 12 male guinea pigs for four weeks. Amino acid analyses of the CH3COOH extracts of dentin matrix proteins revealed a marked difference between the collagenase- and trypsin-treated samples, suggesting the extraction by trypsin of a non-collagenous protein or of peptides derived from such a protein. Both collagenase and trypsin reduced the ability of demineralized dentin to induce bone formation, but whereas the former resulted in enhanced resorption of the dentin implants, the trypsin-treated dentin did not. If the host mesenchymal cells need to be exposed to the inducing factor for a certain minimal length of time for induction of bone formation, enhanced resorption would hinder the induction process. While electron microscopy of control specimens exhibited collagen fibrils with distinct cross-striations, the samples exposed to collagenase treatment displayed disarranged and swollen fibrils with loss of cross-striation. Many of the collagen fibrils of the trypsin-treated dentin had, however, retained their cross-striation. The present results indicate that (he bone-inducing capacity of dentin matrix may be caused by a non-collagenous protein.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1600-0714.1972.tb01660.x
