scholarly journals Biomineralization and Biomaterial Considerations in Dentin Remineralization

2016 ◽  
Vol 1 (1) ◽  
pp. 7-12 ◽  
Author(s):  
Xu Zhang ◽  
Zuohui Xiao ◽  
Haorong Wang ◽  
Anil Kishen
Keyword(s):  
Minimally Invasive ◽  
Type I Collagen ◽  
Organic Matrix ◽  
Type I ◽  
Hard Tissue ◽  
The Past ◽  
Organic Matrices ◽  
Caries Management ◽  
Inorganic Matrix ◽  
Demineralized Dentin

ABSTRACT Dentin is a composite hard tissue, comprising of inorganic and organic matrices, and regulated by many proteins during development. The demineralization of dentin results from the loss of inorganic matrix [mainly hydroxyapatite (HAP)], but the organic matrix (mainly type I collagen) will sustain for a period of time after demineralization. Over the past decade, there has been a growing interest on the remineralization of demineralized dentin, primarily in connection with minimally invasive caries management. More and more biomaterials and methods are currently being evaluated to achieve newer approaches for the remineralization of demineralized dentin. These strategies are mostly based on biomimetic approaches and aim to achieve the characteristics of natural hard tissue. This article will present a complete review on the basic compositions and properties of dentin, which formed the basis for the biomimetic remineralization of demineralized dentin. How to cite this article Zhang X, Xiao Z, Wang H, Kishen A. Biomineralization and Biomaterial Considerations in Dentin Remineralization. J Oper Dent Endod 2016;1(1):7-12.

scholarly journals Matrix Metalloproteinases and Other Matrix Proteinases in Relation to Cariology: The Era of ‘Dentin Degradomics'

2015 ◽  
Vol 49 (3) ◽  
pp. 193-208 ◽  
Author(s):  
Leo Tjäderhane ◽  
Marília Afonso Rabelo Buzalaf ◽  
Marcela Carrilho ◽  
Catherine Chaussain
Keyword(s):  
Mechanical Properties ◽  
Matrix Metalloproteinases ◽  
Type I Collagen ◽  
Resin Composite ◽  
Hydrolytic Degradation ◽  
Organic Matrix ◽  
Type I ◽  
Restorative Treatment ◽  
Cysteine Cathepsins ◽  
Demineralized Dentin

Dentin organic matrix, with type I collagen as the main component, is exposed after demineralization in dentinal caries, erosion or acidic conditioning during adhesive composite restorative treatment. This exposed matrix is prone to slow hydrolytic degradation by host collagenolytic enzymes, matrix metalloproteinases (MMPs) and cysteine cathepsins. Here we review the recent findings demonstrating that inhibition of salivary or dentin endogenous collagenolytic enzymes may provide preventive means against progression of caries or erosion, just as they have been shown to retain the integrity and improve the longevity of resin composite filling bonding to dentin. This paper also presents the case that the organic matrix in caries-affected dentin may not be preserved as intact as previously considered. In partially demineralized dentin, MMPs and cysteine cathepsins with the ability to cleave off the terminal non-helical ends of collagen molecules (telopeptides) may lead to the gradual loss of intramolecular gap areas. This would seriously compromise the matrix ability for intrafibrillar remineralization, which is considered essential in restoring the dentin's mechanical properties. More detailed data of the enzymes responsible and their detailed function in dentin-destructive conditions may not only help to find new and better preventive means, but better preservation of demineralized dentin collagenous matrix may also facilitate true biological remineralization for the better restoration of tooth structural and mechanical integrity and mechanical properties.

Collagen-the Ultrastructural Element of the Bone Matrix

2018 ◽  
Vol 69 (7) ◽  
pp. 1706-1709
Author(s):  
Nicoleta Dumitru ◽  
Andra Cocolos ◽  
Andra Caragheorgheopol ◽  
Constantin Dumitrache ◽  
Ovidiu Gabriel Bratu ◽  
...  
Keyword(s):  
Type I Collagen ◽  
Bone Microarchitecture ◽  
Complex Structure ◽  
Bone Matrix ◽  
Organic Matrix ◽  
Bone Diseases ◽  
Bone Collagen ◽  
Type I ◽  
New Therapeutic Approaches ◽  
And Function

There is an increased interest and more studies highlight the fact that bone strength depends not only on bone tissue quantity, but also on its quality, which is characterized by the geometry and shape of bones, trabecular bone microarchitecture, mineral content, organic matrix and bone turnover. Fibrillar type I collagen is the major organic component of bone matrix, providing form and a stable template for mineralization. The biomedical importance of collagen as a biomaterial for medical and cosmetic purposes and the improvement of the molecular, cellular biology and analytical technologies, led to increasing interest in establishing the structure of this protein and in setting of the relationships between sequence, structure, and function. Bone collagen crosslinking chemistry and its molecular packing structure are considered to be distinct features. This unique post-translational modifications provide to the fibrillar collagen matrices properties such as tensile strength and viscoelasticity. Understanding the complex structure of bone type I collagen as well as the dynamic nature of bone tissues will help to manage new therapeutic approaches to bone diseases.

Zinc Inhibits Collagenolysis by Cathepsin K and Matrix Metalloproteinases in Demineralized Dentin Matrix

2017 ◽  
Vol 51 (6) ◽  
pp. 576-581 ◽  
Author(s):  
Pinar Altinci ◽  
Roda Seseogullari-Dirihan ◽  
Gulsen Can ◽  
David Pashley ◽  
Arzu Tezvergil-Mutluay
Keyword(s):  
Matrix Metalloproteinases ◽  
Mass Loss ◽  
Type I Collagen ◽  
Cathepsin K ◽  
Collagen Degradation ◽  
Type I ◽  
Level Control ◽  
Physiological Level ◽  
Cysteine Cathepsins ◽  
Demineralized Dentin

The enzymatic degradation of dentin organic matrix occurs via both the action of matrix metalloproteinases (MMPs) and cysteine cathepsins (CCs). Zinc can prevent collagen hydrolysis by MMPs. However, its effect on the activity of dentin-bound CCs is not known. The aim of this study was to investigate the effect of zinc on matrix-bound cathepsin K and MMP activity in dentin. Completely demineralized dentin beams were divided into test groups (n = 9) and incubated at 37°C in an incubation media (1 mL) containing ZnCl2 of 0.02 (physiological level, control), 0.2, 0.5, 1, 5, 10, 20, 30, or 40 mM. The dry mass changes of the beams were determined, and incubation media were analyzed for cathepsin K- and MMP-specific collagen degradation end products - CTX (C-terminal cross-linked telopeptide of type I collagen) and ICTP (cross-linked carboxy-terminal telopeptide of type I collagen) - at 1, 3, and 7 days of incubation. The mass loss of the beams decreased when the zinc level in the incubation media was ≥5 mM (p < 0.05). The release of liberated collagen degradation telopeptides decreased in accordance with the decrease in the mass loss rates of the beams. Cathepsin K-induced dentin collagen degradation can be strongly inhibited by zinc. Zinc levels of ≥5 mM can be considered as a reliable threshold for the stabilization of dentin matrices.

scholarly journals Immunohistochemical distribution of collagens types IV, V, and VI and of pro-collagens types I and III in human alveolar bone and dentine.

1986 ◽  
Vol 34 (11) ◽  
pp. 1417-1429 ◽  
Author(s):  
J Becker ◽  
D Schuppan ◽  
H Benzian ◽  
T Bals ◽  
E G Hahn ◽  
...  
Keyword(s):  
Type I Collagen ◽  
Collagen Type ◽  
Alveolar Bone ◽  
Organic Matrix ◽  
Collagen Type I ◽  
Basement Membranes ◽  
Type I ◽  
Collagen Type Iii ◽  
Type Iii ◽  
Hard Tissues

The aim of the present study was to characterize the composition of the organic matrix in alveolar jaw bone and dentine using antibodies against pro-collagens Types I and III and collagens Types IV, V, and VI. After demineralization of oral hard tissues in 0.2 N HCl, antigenicity was well preserved and the distribution of the pro-collagens and collagens could be demonstrated. Staining for pro-collagen Type I was prominent around osteoblasts and in pre-dentine, indicating active de novo synthesis of Type I pro-collagen. Pro-collagen Type I was ubiquitous but was less abundant in bone and dentine, whereas pro-collagen Type III was seen only in areas of bone remodeling, in peritubular spaces, and in pre-dentine. Type IV collagen was limited to the basement membranes of vessels in osteons and bone marrow. Type V collagen was detected neither in pre-dentine nor in bone. In contrast, Type VI collagen was found in dentine and bone, showing a faint but homogeneous staining which, similarly to pro-collagen Type III, was pronounced around osteoblasts and in pre-dentine, areas of active bone and dentine formation. This study showed that the organic matrix of dentine and bone contains Type VI as well as Type I collagen. Pro-collagen Type III (and to a lesser extent collagen Type VI) is transiently produced during new formation and remodeling of oral hard tissues, and disappears once the matrix calcifies. Type I pro-collagen qualifies as a general marker protein for increased osteoblastic activity. We conclude that immunostaining for the different collagen/pro-collagen types can be used to assess normal or abnormal stages of bone/dentine formation.

scholarly journals Reduced Antigenicity of Type I Collagen and Proteoglycans in Sclerotic Dentin

2006 ◽  
Vol 85 (2) ◽  
pp. 133-137 ◽  
Author(s):  
P. Suppa ◽  
A. Ruggeri ◽  
F.R. Tay ◽  
C. Prati ◽  
M. Biasotto ◽  
...  
Keyword(s):  
High Resolution ◽  
Type I Collagen ◽  
Organic Matrix ◽  
Collagen Fibrils ◽  
Type I ◽  
Secondary Antibodies ◽  
Caries Lesions ◽  
Carious Teeth ◽  
Double Immunolabeling

Antigenic alterations to the dentin organic matrix may be detected by an immunohistochemical approach. We hypothesized that alterations in the antigenicity of type I collagen and proteoglycans occur in sclerotic dentin under caries lesions. Transverse sections were prepared from carious teeth in the sclerotic zone and normal hard dentin. A double-immunolabeling technique was performed on these sections, with anti-type I collagen and anti-chondroitin 4/6 sulfate monoclonal primary antibodies. We used gold-conjugated secondary antibodies to visualize the distribution of intact collagen fibrils and proteoglycans by high-resolution SEM. For sclerotic dentin, labeling densities were 19.57 ± 3.01/μm2 for collagen and 9.84 ± 2.62/μm2 for proteoglycans. For normal hard dentin, values were 35.20 ± 2.73/μm2 and 17.03 ± 1.98/μm2, respectively. Distribution of intact collagen fibrils and proteoglycans in sclerotic dentin was significantly lower than in normal hard dentin. Reductions in antigenicity from the organic matrix of sclerotic dentin under caries lesions raise concern about the potential of intrafibrillar remineralization.

Effects of fluoride on the ultrastructure and expression of Type I collagen in rat hard tissue

Chemosphere ◽  
2015 ◽  
Vol 128 ◽  
pp. 36-41 ◽  
Author(s):  
Xiaoyan Yan ◽  
Xianhui Hao ◽  
Qingli Nie ◽  
Cuiping Feng ◽  
Hongwei Wang ◽  
...  
Keyword(s):  
Type I Collagen ◽  
Type I ◽  
Hard Tissue

scholarly journals Cytotoxicity test and characteristics of demineralized dentin matrix scaffolds in adipose-derived mesenchymal stem cells of rats

2018 ◽  
Vol 51 (4) ◽  
pp. 194
Author(s):  
Desi Sandra Sari ◽  
Ernie Maduratna ◽  
F. Ferdiansyah ◽  
I Ketut Sudiana ◽  
Fedik Abdul Rantam
Keyword(s):  
Stem Cells ◽  
Mesenchymal Stem Cells ◽  
Cell Viability ◽  
Type I Collagen ◽  
Type I ◽  
Cytotoxicity Test ◽  
Human Teeth ◽  
Dentin Matrix ◽  
Demineralized Dentin Matrix ◽  
Demineralized Dentin

Background: Demineralized dentin matrix (DDM) scaffold is a substitute material for the bone contained in human teeth. DDM is a scaffold-derived tooth dentine containing type I collagen and bone morphogenetic protein (BMP). While DDM possesses the ability to perform osteoinductive and osteoconductive roles, a cytotoxicity test of DDM scaffold remains extremely important in evaluating the level of toxicity of a material if cultured in cells. Adipose-derived mesenchymal stem cells (ADMSCs) are multipotent in nature because they contain progenitor cells and have the potential for differentiation via adipogenic, osteogenic and chondrogenic pathways. ADMSCs are also known to have high biocompatibility and the ability to combine with other bone material. Purpose: The purpose of this study was to determine the cytotoxicity and characteristics of DDM scaffolds derived from bovine teeth in the ADMSCs of rats cultured in vitro. Methods: This research constituted an experimental study. ADMSCs were isolated from the inguinal fat of rats. Thereafter, DDM was extracted from bovine teeth and formed 355-710 μm-sized particles. DDM scaffolds were assessed using SEM and the effects of DDM scaffolds on the cell viability of ADMSCs at concentrations of 10%, 50%, and 100% analyzed by means of 3-4,5’dimethylihiazol-2-yl,2.5-di-phenyl-tetrazolium bromide (MTT) assay. The results obtained were then analyzed by an ANOVA to establish the difference between the groups. Results: SEM results showed the diameter sizes of the dental tubulis DDM scaffolds to be approximately 4.429 μm and 7.519 μm. The highest cell viability (97.08%) was found by means of an MTT test to be in ADMSCs at a concentration of 10% compared to those at concentrations of 50% and 100%. Conclusion: In conclusion, DDM scaffold derived from bovine teeth with a particle size of 355-710 μm produces a low cytotoxicity effect on ADMSCs.

Role of Host-Derived Proteinases in Dentine Caries and Erosion

2015 ◽  
Vol 49 (Suppl. 1) ◽  
pp. 30-37 ◽  
Author(s):  
Marília Afonso Rabelo Buzalaf ◽  
Senda Charone ◽  
Leo Tjäderhane
Keyword(s):  
Structural Changes ◽  
Type I Collagen ◽  
Organic Matrix ◽  
Collagen Matrix ◽  
Type I ◽  
Cysteine Cathepsins ◽  
Gradual Loss ◽  
Collagen Molecules ◽  
And Function

Demineralization in dentinal caries and erosion exposes dentine organic matrix. This exposed matrix, containing type I collagen and non-collagenous proteins, is then degraded by host collagenolytic enzymes, matrix metalloproteinases (MMPs) and cysteine cathepsins. The knowledge of the identities and function of these enzymes in dentine has accumulated only within the last 15 years, but has already formed a field of research called ‘dentine degradomics'. This research has demonstrated the role of endogenous collagenolytic enzymes in caries and erosion development. In demineralized dentine, the enzymes degrade triple-helical collagen molecules, leading to the gradual loss of collagen matrix. Even before that, they can cleave off the terminal non-helical ends of collagen molecules called telopeptides, leading to the structural changes at the intramolecular gap areas, which may affect or even prevent intrafibrillar remineralization, which is considered essential in restoring the dentine's mechanical properties. They may also cause the loss of non-collagenous proteins that could serve as nucleation sites for remineralization. Here we review the findings demonstrating that inhibition of salivary or dentine endogenous MMPs and cysteine cathepsins may provide preventive means against the progression of caries or erosion. Furthermore, we also suggest the future directions for the new experimental preventive research to gain more knowledge of the enzymes and their function during and after dentine demineralization, and the pathways to find the clinically acceptable means to prevent the functional activity of these enzymes.

scholarly journals LINC00312/YBX1 Axis Regulates Myofibroblast Activities in Oral Submucous Fibrosis

2020 ◽  
Vol 21 (8) ◽  
pp. 2979 ◽  
Author(s):  
Chuan-Hang Yu ◽  
Chih-Yuan Fang ◽  
Cheng-Chia Yu ◽  
Pei-Ling Hsieh ◽  
Yi-Wen Liao ◽  
...  
Keyword(s):  
Gene Expression ◽  
Noncoding Rna ◽  
Type I Collagen ◽  
Oral Submucous Fibrosis ◽  
Collagen Gel ◽  
Great Effort ◽  
Type I ◽  
The Past ◽  
Submucous Fibrosis

Oral submucous fibrosis (OSF) has been recognized as a precancerous disorder in the oral cavity. Great effort has been made to inhibit the malignant progression of OSF over the past decades, but the cure of this fibrosis disease has not been discovered. In the present study, we found that a long noncoding RNA, LINC00312, was upregulated in OSF tissues, and positively associated with several fibrosis factors, such as α-SMA, type I collagen, and fibronectin. As such, we sought to investigate the role of LINC00312 in OSF progression and identify its interacting factor that mediated oral fibrogenesis. Our results showed that the inhibition of LINC00312 downregulated the myofibroblast activities, including collagen gel contractility, transwell migration, and wound healing, as well as the gene expression of myofibroblast markers. We verified that YBX1 was a downstream factor of LINC00312 and revealed that the downregulation of YBX1 repressed the gene expression of α-SMA and p-Smad2 along with the reduced myofibroblast phenotypes. Most importantly, we demonstrated that the LINC00312-induced myofibroblast activities were reverted by the knockdown of YBX1, suggesting that the LINC00312-mediated myofibroblast transdifferentiation was through YBX1. Collectively, our findings revealed that the LINC00312/ YBX1 axis may serve as a target for the development of therapies against OSF.

scholarly journals Chitosan Based Biocomposites for Hard Tissue Engineering

2021 ◽  
Author(s):  
Fouad Dabbarh ◽  
Noureddin Elbakali-Kassimi ◽  
Mohammed Berrada
Keyword(s):  
Type I Collagen ◽  
Soft Tissues ◽  
Calcium Phosphates ◽  
Low Cost ◽  
Type I ◽  
Hard Tissue ◽  
Structural Support ◽  
Bone Substitute Materials ◽  
Autologous Bone ◽  
Hard Tissue Engineering

Bone is the second most transplanted organ, just after blood. It provides structural support, protection for organs and soft tissues. It holds some critical biological processes such as the bone marrow blood forming system. It is responsible for storing and supplying minerals such calcium and phosphate. Bone is a connective tissue formed by two predominant phases: an inorganic phase containing mainly apatitic calcium and phosphate and an organic phase made of fibrous type I collagen. This natural biocomposite has many biological features such osteoconductivity, osteoinductivity, osteogenicity and is subject to a continuous remodeling process through osteoclastic and osteoblastic activities. In biomedical engineering, the restoration of damaged hard tissue with autologous bone is not always possible or even the best option. The development of some safe and low-cost alternatives such as biocomposites that mimic organic and calcified bone materials have shown very good results and offer an alternative to autologous bone implants. However, the mechanical properties of biocomposites still present a big challenge as a hard tissue substitute. This chapter reviews the properties of bone substitute materials chitosan and calcium phosphates, discusses strategies used in the treatment of calcified hard tissues as well as new approaches developed in this field.

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