The extent and distribution of intratubular collagen fibrils in human dentine

Dai, Xingzhu; Cate, A. R. Ten; Limeback, Hardy

doi:10.1016/0003-9969(91)90045-v

Cited by 67 publications

(42 citation statements)

References 6 publications

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“…Mineralization within the dentinal tubule lumens similarly may require the presence of collagen to act as a structural template prior to intratubular mineralization. Collagen fibrils have been found in over 60% of coronal dentin tubules regardless of age or tooth type [Dai et al, 1991]. Collagen has been identified in transparent (sclerotic) dentin [Suppa et al, 2006].…”

Section: Discussionmentioning

confidence: 96%

Increased Matrix Metalloproteinase-2 and Bone Sialoprotein Response to Human Coronal Caries

Boushell

Nagaoka²,

Yamauchi

2011

Caries Res

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Background: It has been suggested that host matrix metalloproteinase-2 (MMP-2) present in dentin may be involved in caries progression, however, its response to caries is not known. Bone sialoprotein (BSP) has been implicated in dentin mineralization and MMP-2 modulation. Objective: To identify and compare the distribution of MMP-2 and BSP in healthy human coronal dentin and those with early caries. Methods: Freshly extracted 3rd molars and premolars with and without early caries were fixed, demineralized and subjected to immunohistochemistry using a monoclonal anti-MMP-2 antibody and monoclonal anti-BSP antibody with an avidin-biotin complex method. Immunoreactivity was visualized with 3,3′-diaminobenzidine substrate and observed under light microscopy. Results: Immunohistochemical analysis revealed that MMP-2 and BSP are not detected in the tubule lumens of healthy dentin. However, intense immunoreactivity for MMP-2 and BSP was detected in association with the full length of the caries-affected dentinal tubules. The MMP-2 and BSP at the dentino-enamel junction appeared unaltered. Conclusion: The results indicate that MMP-2 and BSP may be actively secreted by odontoblasts in response to carious insult. MMP-2 and BSP accumulation in the caries-affected dentinal tubules may indicate their potential involvement in the host defense mechanism which results in calcification of regions affected by the carious process.

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Section: Discussionmentioning

confidence: 96%

Increased Matrix Metalloproteinase-2 and Bone Sialoprotein Response to Human Coronal Caries

Boushell

Nagaoka²,

Yamauchi

2011

Caries Res

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“…We have previously provided evidence that the ability of S. gordonii or S. mutans cells to invade dentinal tubules depends upon collagen recognition by antigen I/II polypeptides (30). Although P. gingivalis cells also bind to collagen type I deposited onto hydroxylapatite surfaces (32,33), it would appear that the ability to bind type I collagen, present within dentinal tubules (9), is not sufficient to promote invasion of tubules by these bacteria in monoculture.…”

Section: Discussionmentioning

confidence: 99%

Coinvasion of Dentinal Tubules by Porphyromonas gingivalis and Streptococcus gordonii Depends upon Binding Specificity of Streptococcal Antigen I/II Adhesin

et al. 2000

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Cell wall-anchored polypeptides of the antigen I/II family are produced by many species of oral streptococci. These proteins mediate adhesion of streptococci to salivary glycoproteins and to other oral microorganisms and promote binding of cells to collagen type I and invasion of dentinal tubules. Since infections of the root canal system have a mixed anaerobic bacterial etiology, we investigated the hypothesis that coadhesion of anaerobic bacteria with streptococci may facilitate invasive endodontic disease. Porphyromonas gingivalis ATCC 33277 cells were able to invade dentinal tubules when cocultured with Streptococcus gordonii DL1 (Challis) but not when cocultured with Streptococcus mutans NG8. An isogenic noninvasive mutant of S. gordonii, with production of SspA and SspB (antigen I/II family) polypeptides abrogated, was deficient in binding to collagen and had a 40% reduced ability to support adhesion of P. gingivalis. Heterologous expression of the S. mutans SpaP (antigen I/II) protein in this mutant restored collagen binding and tubule invasion but not adhesion to P. gingivalis or the ability to promote P. gingivalis coinvasion of dentin. An isogenic afimbrial mutant of P. gingivalis had 50% reduced binding to S. gordonii cells but was unaffected in the ability to coinvade dentinal tubules with S. gordonii wild-type cells. Expression of the S. gordonii SspA or SspB polypeptide on the surface of Lactococcus lactis cells endowed these bacteria with the abilities to bind P. gingivalis, penetrate dentinal tubules, and promote P. gingivalis coinvasion of dentin. The results demonstrate that collagen-binding and P. gingivalis-binding properties of antigen I/II polypeptides are discrete functions. Specificity of antigen I/II polypeptide recognition accounts for the ability of P. gingivalis to coinvade dentinal tubules with S. gordonii but not with S. mutans. This provides evidence that the specificity of interbacterial coadhesion may influence directly the etiology of pulpal and periapical diseases.

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“…In human, PTD mineral content by volume is approximately 90% [3], but if PTD contains any collagen remains controversial [11][12][13][14][15][16][17][18]. The bulk of the dentin comprises intertubular dentin (ITD), whose organic content is approximately three times higher than in PTD [14].…”

Section: Introductionmentioning

confidence: 99%

Animal and human dentin microstructure and elemental composition

et al. 2014

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AbstractAnimal teeth are a common model in studies on dentin adhesive materials. The aim of this study was to compare microstructural parameters (density and diameter of dentinal tubules (DT), peritubular dentin (PTD) thickness, PTD and intertubular dentin (ITD) surface area) and chemical characteristics of canine, porcine, equine, and human root dentin. The middle layers of dentin were harvested just below a cemento-enamel junction from incisors and investigated by means of scanning electron microscopy (SEM) and energy dispersive X-ray spectroscopy (EDXS). SEM evaluation of the specimens revealed, that porcine dentin shared most similarities with human dentin. When comparing the density of DTs, canine dentin was also found to be similar to human dentin. Elemental composition of the root dentin did not differ significantly in porcine, equine and human dentin, but in canine dentin higher magnesium value in PTD compared to ITD was found. It is known that microstructural and chemical characteristics affect the strength of the adhesive bonds created among restorative materials and dentin. According to the results of this study, porcine dentin seems to be the most appropriate model to study dental materials to be used in human restorative dentistry.

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The extent and distribution of intratubular collagen fibrils in human dentine

Cited by 67 publications

References 6 publications

Increased Matrix Metalloproteinase-2 and Bone Sialoprotein Response to Human Coronal Caries

Increased Matrix Metalloproteinase-2 and Bone Sialoprotein Response to Human Coronal Caries

Coinvasion of Dentinal Tubules by Porphyromonas gingivalis and Streptococcus gordonii Depends upon Binding Specificity of Streptococcal Antigen I/II Adhesin

Animal and human dentin microstructure and elemental composition

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