Home » APJ Receptor » [PubMed] [Google Scholar]Tj?derhane L, Larjava H, Sorsa T, Uitto VJ, Larmas M, Salo T

[PubMed] [Google Scholar]Tj?derhane L, Larjava H, Sorsa T, Uitto VJ, Larmas M, Salo T

[PubMed] [Google Scholar]Tj?derhane L, Larjava H, Sorsa T, Uitto VJ, Larmas M, Salo T. raise concern about the potential of intrafibrillar remineralization. 11-220 kDa) carbohydrate-containing polyanions consisting of a polypeptide core with lateral glycosaminoglycan chains. Glycosaminoglycans regulate the biophysical properties of dentin by filling spaces, binding and organizing water molecules, and repelling negatively charged molecules (Bourdon (Okuda studies (Arends sclerotic dentin (Breschi (1977) shown the presence of intermolecular Mibampator cross-linking from collagen fibrils in the transparent zone. The authors suggested that caries-affected dentin is definitely remineralizable and is a suitable substrate for dentin adhesion. The antigenicity of a single protein, as exposed by its specific binding to a monoclonal antibody, provides definitive evidence of an ideal conservation of the epitope structure (Hall and Embery, 1997). Since monoclonal antibodies are highly sensitive (Willingham, 1999), the protocol for this study can be considered highly selective in identifying alterations in the protein epitopes. Relating to Lynn (2004), epitopes for collagen type I monoclonal antibodies can be divided into helical, central, and terminal, depending on their ability to interact with the collagen peptides. The antibody anti-helical portion (such as the one used in this study) recognizes the substrate based on three-dimensional conformation that is related to the presence of an intact triple helix. Since the antibody recognizes the native form of collagen type I and does not react with the denatured molecule, we have to reject the null hypothesis that there are no variations in the distribution of antigenically intact collagen fibrils and proteoglycans between normal hard and sclerotic dentin under caries lesions. Indeed, the caries process induces modifications to both type I collagen fibrils and proteoglycans, as shown from the decreased labeling indices when sclerotic dentin was compared with sound dentin. The decreased labeling indices associated with the sclerotic dentin under caries lesions may be caused either from the masking of the protein epitopes from the apatite mineral phase present in the hypermineralized peritubular areas of the transparent zone, or from the denaturing of the protein parts (Breschi (2001) shown that intertubular dentin in the transparent zone is not hypermineralized compared with normal sound dentin. Therefore, alteration in the antigenicity of the collagen fibrils and proteoglycans in sclerotic dentin under caries lesions appears to be the more logical explanation for the decreased labeling indices of the gold-conjugated antibodies. To day, evidence of remineralization of enamel and dentinal caries is largely based upon the results acquired with densitometry (Arends secondary caries using confocal laser scanning microscope and x-ray analytical microscope. Am J Dent. 2003;16:191C196. [PubMed] [Google Scholar]Pashley DH, Tay FR, Yiu C, Hashimoto M, Breschi L, Carvalho RM, et al. Collagen degradation by host-derived enzymes during ageing. J Dent Res. 2004;83:216C221. [PubMed] [Google Scholar]Scott JE. Proteoglycan-fibrillar collagen relationships. Biochem J. 1988;252:313C323. [PMC free article] [PubMed] [Google Scholar]Septier D, Hall RC, Lloyd D, Embery G, Goldberg M. Quantitative immunohistochemical evidence of a functional gradient of chondroitin 4-sulphate/dermatan sulphate, developmentally controlled in the predentine of rat incisor. Histochem J. 1998;30:275C284. [PubMed] [Google Scholar]ten Cate JM. Remineralization of caries lesions extending into dentin. J Dent Res. 2001;80:1407C1411. [PubMed] [Google Scholar]Tj?derhane L, Larjava H, Sorsa T, Uitto VJ, Larmas M, Salo T. The activation and function of sponsor matrix metalloproteinases in dentin matrix breakdown in caries lesions. Mibampator J Dent Res. 1998;77:1622C1629. [PubMed] [Google Scholar]Vehicle Strijp AJ, Jansen DC, DeGroot J, ten Cate JM, Everts V. Host-derived proteinases and degradation of dentine collagen in situ. Caries Res. 2003;37:58C65. [PubMed] [Google Scholar]Willingham MC. Conditional epitopes. Is definitely your antibody usually specific? J Histochem Cytochem. 1999;47:1233C1236. Mibampator [PubMed] [Google Scholar]Yoshiyama M, Tay FR, Torii Y, Nishitani Y, Doi J, Itou K, et al. DKFZp686G052 Resin adhesion to carious dentin. Am J Dent. 2003;16:47C52. [PubMed] [Google Scholar]Zheng L, Hilton JF, Habelitz S, Marshall SJ, Marshall GW. Dentin caries activity status related to hardness and elasticity. Eur J Dental Sci. 2003;111:243C252. [PubMed] [Google Scholar].