Background/purpose: Root dentin is vulnerable to acid attack, suggesting a higher risk of demineralization than coronal enamel. This study aimed to evaluate the inhibitory effect of Miswak extract on collagen degradation of demineralized dentin lesion.
Materials And Methods: Demineralized bovine root dentin specimens were treated for 1 h by 20% Miswak extract and 0.12% Chlorehexidine (CHX) as a positive control group, and then subjected to collagenolytic attack (clostridium histolyticum 0.5 CDU/mL, 16 h). These cyclic treatments were repeated for 3 days. After the cyclic treatment, the images of the specimens were captured with a light microscope and the lesion depth of degraded collagen layer of all specimens was measured. The mean lesion depth was calculated and compared between the groups using descriptive and One-way ANOVA followed by Post hoc Tukey's tests. Significant level was set at p < 0.05.
Results: The mean lesion depth of CHX (28.6 ± 3.37 μm) had the least value, followed by Miswak (37.5 ± 4.01 μm) then the control (78.4 ± 18.43 μm) group. There was a significant difference in the mean lesion depth among the three groups (p = 0.000).
Conclusion: Miswak aqueous extract from was found to preserve the dentin collagen matrix from collagenase enzyme. This could be due to the organic compounds like flavonoids, saponins, alkaloids, tannins, and others which have been reported in literature. Present finding suggests that Miswak might play a positive effect in dentin caries prevention.
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http://dx.doi.org/10.1016/j.jds.2020.05.025 | DOI Listing |
F1000Res
January 2025
Immunology, University of Toronto, Toronto, Ontario, Canada.
Fibroblasts, non-hematopoietic cells of mesenchymal origin, are tissue architects which regulate the topography of tissues, dictate tissue resident cell types, and drive fibrotic disease. Fibroblasts regulate the composition of the extracellular matrix (ECM), a 3-dimensional network of macromolecules that comprise the acellular milieu of tissues. Fibroblasts can directly and indirectly regulate immune responses by secreting ECM and ECM-bound molecules to shape tissue structure and influence organ function.
View Article and Find Full Text PDFJ Invest Dermatol
January 2025
Dept. of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, Connecticut, USA; Dept. of Dermatology, Yale School of Medicine, New Haven, Connecticut, USA. Electronic address:
During skin fibrosis, extracellular matrix (ECM) proteins are overproduced, and resident lipid-filled, mature dermal adipocytes are depleted in both human disease and mouse models. However, the mechanisms by which the reduction in lipid-filled adipocytes occurs during fibrosis are not well understood. Here, we identify that adipocyte lipolysis via the rate limiting enzyme, adipocyte triglyceride lipase (Atgl), is required for loss of adipose tissue during skin fibrosis in mice.
View Article and Find Full Text PDFJ Appl Physiol (1985)
January 2025
Department Physical Therapy.
The purpose of this study was to investigate the ability of mechanotherapy to enhance recovery or prevent loss of muscle size with atrophy, in female rats. Female F344/BN rats were assigned to weight bearing (WB), hindlimb suspended (HS) for 14 days with reambulation for 7 days without (RA) or with (RAM) mechanotherapy (study 1), or to WB, HS for 7 days, with (HSM) or without mechanotherapy (study 2) to gastrocnemius. Muscle fiber cross sectional area (CSA) and type, collagen, satellite cell number, and protein synthesis (K) and degradation (K) were assessed.
View Article and Find Full Text PDFJ Med Chem
January 2025
Ma̅tai Ha̅ora - Centre for Redox Biology and Medicine, Department of Biomedical Science and Pathology, University of Otago, Christchurch, Christchurch 8140, New Zealand.
In humans, the 2-oxoglutarate-dependent dioxygenases (2-OGDDs) catalyze hydroxylation reactions involved in cell metabolism, the biosynthesis of small molecules, DNA and RNA demethylation, the hypoxic response and the formation of collagen. The reaction is catalyzed by a highly oxidizing ferryl-oxo species produced when the active site non-heme iron engages molecular oxygen. Enzyme activity is specifically stimulated by l-ascorbic acid (ascorbate, vitamin C), an effect not well mimicked by other reducing agents.
View Article and Find Full Text PDFInvest Ophthalmol Vis Sci
January 2025
University Eye Clinic Maastricht, Maastricht University Medical Center, Maastricht, the Netherlands.
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