Endodontically treated teeth restored with posts are susceptible to coronal leakage after long-term function. We hypothesize that demineralized collagen matrices (DCMs) created in dentin by acidic zinc phosphate cement within the dowel spaces degrade with time. Forty-two post-restored teeth were extracted after three periods of clinical service and were examined, by means of scanning and transmission electron microscopy, for the status of the DCMs. SEM revealed a progressive degradation of the DCMs, becoming less dense after 3 to 5 years, losing structural integrity after 6 to 9 years, and partially disappearing after 10 to 12 years. TEM revealed evidence of collagenolytic activity within the DCMs, with loss of cross-banding and unraveling into microfibrils, and gelatinolytic activity that resulted in disintegration of the microfibrils. Bacterial colonization and the release of bacterial enzymes and of host-derived matrix metalloproteinases may contribute to the degradation of collagen fibrils in root dentin after clinical function.
Ferrari, M., Mason, P.N., Goracci, C., Pashley, D., Tay, F. (2004). Collagen degradation in endodontically treated teeth after clinical function. JOURNAL OF DENTAL RESEARCH, 83(5), 414-419 [10.1177/154405910408300512].
Collagen degradation in endodontically treated teeth after clinical function
FERRARI M.;GORACCI C.;
2004-01-01
Abstract
Endodontically treated teeth restored with posts are susceptible to coronal leakage after long-term function. We hypothesize that demineralized collagen matrices (DCMs) created in dentin by acidic zinc phosphate cement within the dowel spaces degrade with time. Forty-two post-restored teeth were extracted after three periods of clinical service and were examined, by means of scanning and transmission electron microscopy, for the status of the DCMs. SEM revealed a progressive degradation of the DCMs, becoming less dense after 3 to 5 years, losing structural integrity after 6 to 9 years, and partially disappearing after 10 to 12 years. TEM revealed evidence of collagenolytic activity within the DCMs, with loss of cross-banding and unraveling into microfibrils, and gelatinolytic activity that resulted in disintegration of the microfibrils. Bacterial colonization and the release of bacterial enzymes and of host-derived matrix metalloproteinases may contribute to the degradation of collagen fibrils in root dentin after clinical function.File | Dimensione | Formato | |
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https://hdl.handle.net/11365/25970
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