Regulation of in vitro and in vivo CaCO3 crystallization by fractions of oyster shell organic matrix

1988 ◽  
Vol 98 (1) ◽  
pp. 71-80 ◽  
Author(s):  
A. P. Wheeler ◽  
K. W. Rusenko ◽  
D. M. Swift ◽  
C. S. Sikes
Keyword(s):  
Oyster Shell ◽  
Organic Matrix ◽  
Shell Organic Matrix

scholarly journals Matrix Vesicles: Role in Bone Mineralization and Potential Use as Therapeutics

2021 ◽  
Vol 14 (4) ◽  
pp. 289
Author(s):  
Sana Ansari ◽  
Bregje W. M. de de Wildt ◽  
Michelle A. M. Vis ◽  
Carolina E. de de Korte ◽  
Keita Ito ◽  
...  
Keyword(s):  
Bone Formation ◽  
Bone Regeneration ◽  
Bone Cells ◽  
Bone Mineralization ◽  
Recipient Cell ◽  
Organic Matrix ◽  
Matrix Vesicles ◽  
Matrix Mineralization

Bone is a complex organ maintained by three main cell types: osteoblasts, osteoclasts, and osteocytes. During bone formation, osteoblasts deposit a mineralized organic matrix. Evidence shows that bone cells release extracellular vesicles (EVs): nano-sized bilayer vesicles, which are involved in intercellular communication by delivering their cargoes through protein–ligand interactions or fusion to the plasma membrane of the recipient cell. Osteoblasts shed a subset of EVs known as matrix vesicles (MtVs), which contain phosphatases, calcium, and inorganic phosphate. These vesicles are believed to have a major role in matrix mineralization, and they feature bone-targeting and osteo-inductive properties. Understanding their contribution in bone formation and mineralization could help to target bone pathologies or bone regeneration using novel approaches such as stimulating MtV secretion in vivo, or the administration of in vitro or biomimetically produced MtVs. This review attempts to discuss the role of MtVs in biomineralization and their potential application for bone pathologies and bone regeneration.

scholarly journals Proteomic characterization of oyster shell organic matrix proteins (OMP)

2016 ◽  
Vol 12 (05) ◽  
pp. 266-278 ◽  
Author(s):  
Abhishek Upadhyay ◽  
◽  
Vengatesen Thiyagarajan ◽  
◽  
◽  
...  
Keyword(s):  
Oyster Shell ◽  
Organic Matrix ◽  
Matrix Proteins ◽  
Shell Organic Matrix

Collagen/silica nanocomposites and hybrids for bone tissue engineering

2013 ◽  
Vol 2 (4) ◽  
pp. 427-447 ◽  
Author(s):  
Bapi Sarker ◽  
Stefan Lyer ◽  
Andreas Arkudas ◽  
Aldo R. Boccaccini
Keyword(s):  
Tissue Engineering ◽  
Bone Tissue Engineering ◽  
Bone Tissue ◽  
Self Assembly ◽  
Structural Integrity ◽  
Organic Matrix ◽  
Angiogenic Potential ◽  
Silica Nanocomposites

AbstractCollagen is increasingly attracting attention for bone tissue engineering applications. However, due to its low mechanical properties, applications including mechanical loads or requiring structural integrity are limited. To tackle this handicap, collagen can be combined with (nanoscale) silica in a variety of composite materials that are attractive for bone tissue engineering. Considering research carried out in the past 15 years, this article reviews the literature discussing the development of silica/collagen composites that have been synthesized by adding silica from different sources as inorganic bioactive material to collagen as organic matrix. Different routes for the fabrication of collagen/silica composites are presented, focusing on nanocomposites. In vitro cell bioactivity studies demonstrated the osteogenic and, in some cases, angiogenic potential of the composites. Relevant in vivo studies discussing integration of the materials in bone tissue are discussed. Due to the understanding of possible interaction between silicon species and collagen, the effect of different silica precursors on the collagen self-assembly process is also discussed. On the basis of literature results and as discussed in this review, collagen/silica nanocomposites and hybrids represent attractive biomaterials for bone regeneration applications.

scholarly journals Dentinogenic effects of extracted dentin matrix components digested with matrix metalloproteinases

2018 ◽  
Vol 8 (1) ◽  
Author(s):  
Motoki Okamoto ◽  
Yusuke Takahashi ◽  
Shungo Komichi ◽  
Paul R. Cooper ◽  
Mikako Hayashi
Keyword(s):  
Wound Healing ◽  
Matrix Metalloproteinases ◽  
Biological Effects ◽  
Organic Matrix ◽  
Bioactive Molecules ◽  
Cell Functions ◽  
Dentin Matrix ◽  
Matrix Components

Abstract Dentin is primarily composed of hydroxyapatite crystals within a rich organic matrix. The organic matrix comprises collagenous structural components, within which a variety of bioactive molecules are sequestered. During caries progression, dentin is degraded by acids and enzymes derived from various sources, which can release bioactive molecules with potential reparative activity towards the dentin-pulp complex. While these molecules’ repair activities in other tissues are already known, their biological effects are unclear in relation to degradation events during disease in the dentin-pulp complex. This study was undertaken to investigate the effects of dentin matrix components (DMCs) that are partially digested by matrix metalloproteinases (MMPs) in vitro and in vivo during wound healing of the dentin-pulp complex. DMCs were initially isolated from healthy dentin and treated with recombinant MMPs. Subsequently, their effects on the behaviour of primary pulp cells were investigated in vitro and in vivo. Digested DMCs modulated a range of pulp cell functions in vitro. In addition, DMCs partially digested with MMP-20 stimulated tertiary dentin formation in vivo, which exhibited a more regular tubular structure than that induced by treatment with other MMPs. Our results indicate that MMP-20 may be especially effective in stimulating wound healing of the dentin-pulp complex.

scholarly journals Isolated osteoclasts resorb the organic and inorganic components of bone.

1986 ◽  
Vol 102 (4) ◽  
pp. 1164-1172 ◽  
Author(s):  
H C Blair ◽  
A J Kahn ◽  
E C Crouch ◽  
J J Jeffrey ◽  
S L Teitelbaum
Keyword(s):  
Bone Matrix ◽  
Attachment Site ◽  
Organic Matrix ◽  
Total Radioactivity ◽  
Maximum Activity ◽  
Bone Collagen ◽  
Collagenolytic Activity ◽  
Maximal Rate

Osteoclasts are the principal resorptive cells of bone, yet their capacity to degrade collagen, the major organic component of bone matrix, remains unexplored. Accordingly, we have studied the bone resorptive activity of highly enriched populations of isolated chicken osteoclasts, using as substrate devitalized rat bone which had been labeled in vivo with L-[5-3H]proline or 45Ca, and bone-like matrix produced and mineralized in vitro by osteoblast-like rat osteosarcoma cells. When co-cultured with a radiolabeled substrate, osteoclast-mediated mineral mobilization reached a maximal rate within 2 h, whereas organic matrix degradation appeared more slowly, reaching maximal rate by 12-24 h. Thereafter, the rates of organic and inorganic matrix resorption were essentially linear and parallel for at least 6 d when excess substrate was available. Osteoclast-mediated degradation of bone collagen was confirmed by amino acid analysis. 39% of the solubilized tritium was recovered as trans-4-hydroxyproline, 47% as proline. 10,000 osteoclasts solubilized 70% of the total radioactivity and 65% of the [3H]-trans-4-hydroxyproline from 100 micrograms of 25-50 micron bone fragments within 5 d. Virtually all released tritium-labeled protein was of low molecular weight, 99% with Mr less than or equal to 10,000, and 65% with Mr less than or equal to 1,000. Moreover, when the 14% of resorbed [3H]proline-labeled peptides with Mr greater than or equal to 2,000 were examined for the presence of TCA and TCB, the characteristic initial products of mammalian collagenase activity, none was detected by SDS PAGE. In addition, osteoclast-conditioned medium had no collagenolytic activity, and exogenous TCA and TCB fragments were not degraded by osteoclasts. On the other hand, osteoclast lysates have collagenolytic enzyme activity in acidic but not in neutral buffer, with maximum activity at pH 4.0. These data indicate that osteoclasts have the capacity to resorb the organic phase of bone by a process localized to the osteoclast and its attachment site. This process appears to be independent of secretion of neutral collagenase and probably reflects acid protease activity.

scholarly journals The Solubility Rate of Large Particle Oyster Shell and Limestone In vivo and In vitro,

1977 ◽  
Vol 56 (3) ◽  
pp. 810-812 ◽  
Author(s):  
H.J. KUHL ◽  
T.W. SULLIVAN
Keyword(s):  
Large Particle ◽  
Oyster Shell

scholarly journals Synthesis of a bone like composite material derived from waste pearl oyster shells for potential bone tissue bioengineering applications

2017 ◽  
Vol 5 (6) ◽  
pp. 2454 ◽  
Author(s):  
Ravi Krishna Brundavanam ◽  
Derek Fawcett ◽  
Gérrard Eddy Jai Poinern
Keyword(s):  
Composite Materials ◽  
Bone Tissue ◽  
Bone Repair ◽  
Oyster Shell ◽  
Surface Characteristics ◽  
Pearl Oyster ◽  
In Vivo Studies ◽  
Pinctada Maxima

Background: Hydroxyapatite is generally considered a viable substitute for bone in a number of medical procedures such as bone repair, bone augmentation and coating metal implants. Unfortunately, hydroxyapatite has poor mechanical properties that make it unsuitable for many load bearing applications.Methods: In the present work various grades of finely crushed Pinctada maxima (pearl oyster shell) were combined with a nanometer scale hydroxyapatite powder to form novel composite materials. A comparative study was made between the various powder based composites synthesized. The crystalline structure and morphology of the various powder based composites were investigated using X-ray diffraction and field emission scanning electron microscopy. The composite materials were also evaluated and characterized.Results: Manufactured hydroxyapatite powders were composed of crystalline spherical/granular particles with a mean size of 30 nm. Also produced were hydroxyapatite and finely crushed calcium carbonate from Pinctada maxima (pearl oyster shell) powder mixtures. Hydroxyapatite coatings produced on Pinctada maxima nacre substrates were investigated and their surface characteristics reported.Conclusions: Pinctada maxima nacre pre-treated with sodium hypo chlorate before hydroxyapatite deposition produced a superior coating and could be used for bone tissue engineering. But further in vitro and in vivo studies are needed to validate the biocompatibility and long term stability of this composite coating.

Targeting and Immobilization of Bioactive Peptides on Dentin Matrix

2007 ◽  
Vol 86 (10) ◽  
pp. 968-973 ◽  
Author(s):  
J.S. Song ◽  
A. Wlodarska ◽  
H.J. Ko ◽  
W.J. Grzesik
Keyword(s):  
Bioactive Peptides ◽  
Covalent Binding ◽  
Periodontal Regeneration ◽  
Organic Matrix ◽  
Biologically Active ◽  
Binding Motif ◽  
Rich Domain ◽  
Dentin Matrix

The regeneration of structurally/functionally competent tooth root cementum is a critical step for the successful restoration of periodontal attachment. In this study, we tested whether a poly-glutamic acid-rich domain and glutamine-containing transglutaminase substrate can be used to target biologically active peptides to the mineralized root matrix and to bind such peptides covalently to the organic matrix. As a biologically active model molecule, the integrin-binding motif, RGD, was used. The effects of immobilization of such synthetic peptides to the dentin matrix on cementoblastic adhesion in vitro and cementogenesis in vivo were studied. In vitro, cementoblastic adhesion improved significantly when the dentin surface contained covalently bound peptides. In vivo, this bound peptide significantly increased cementum formation compared with that attained in control conditions. Transglutaminase-catalyzed covalent binding of bioactive peptides targeted to mineralized collagenous dentin matrix via the poly-glutamate domain can be readily achieved. This approach offers potential for clinical use in periodontal regeneration.

scholarly journals The inhibitory effect of carboxyl-terminated polyamidoamine dendrimers on dentine host-derived matrix metalloproteinases in vitro in an etch-and-rinse adhesive system

2019 ◽  
Vol 6 (10) ◽  
pp. 182104
Author(s):  
Qian Wu ◽  
Tiantian Shan ◽  
Manduo Zhao ◽  
Sui Mai ◽  
Lisha Gu
Keyword(s):  
Matrix Metalloproteinases ◽  
Organic Matrix ◽  
Adhesive System ◽  
Collagen Fibrils ◽  
Fourth Generation ◽  
Etch And Rinse ◽  
Polyamidoamine Dendrimers ◽  
Pre Treatment

The biomimetic remineralization of collagen fibrils has increased interest in restoring the demineralized dentine generated by dental caries. Carboxyl-terminated polyamidoamine dendrimers (PAMAM-COOH), hyperbranched polymeric macromolecules, can act as non-collagenous proteins to induce biomimetic remineralization on a dentine organic matrix. However, in vivo remineralization is an extremely time-consuming process; before complete remineralization, demineralized dentine collagen fibrils are susceptible to degradation by host-derived matrix metalloproteinases (MMPs). Therefore, we examined the effect of fourth-generation PAMAM-COOH (G4-PAMAM-COOH) on the collagenolytic activities of endogenous MMPs, the interaction between G4-PAMAM-COOH and demineralized dentine collagen and the influence of G4-PAMAM-COOH pre-treatment on resin–dentine bonding. G4-PAMAN-COOH not only inhibited exogenous soluble rhMMP9 but also hampered the proteolytic activities of dentine collagen-bound MMPs. Cooperated with the results of G4-PAMAM-COOH absorption and desorption, FTIR spectroscopy provided evidence for the exclusive electrostatic interaction rather than hydrogen or covalent bonding between G4-PAMAM-COOH and dentine collagen. Furthermore, G4-PAMAM-COOH pre-treatment showed no damage to resin–dentine bonding because it did not significantly decrease the elastic modulus of the demineralized dentine, degree of conversion, penetration of the adhesive into the dentinal tubules or ultimate tensile strength. Thus, G4-PAMAM-COOH can effectively inactivate MMPs, retard the enzymolysis of collagen by MMPs and scarcely influence the application of resin–dentine bonding.

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