Coprecipitation of Cell Adhesion Molecule with Calcium Phosphate on Hydroxyapatite Ceramic

2006 ◽  
Vol 309-311 ◽  
pp. 767-770 ◽  
Author(s):  
Yu Sogo ◽  
Yuusuke Ishikawa ◽  
Nao Kondo ◽  
Eiji Uchimura ◽  
Ayako Oyane ◽  
...  
Keyword(s):  
Calcium Phosphate ◽  
Cell Adhesion Molecule ◽  
Type I Collagen ◽  
Alveolar Bone ◽  
Composite Layer ◽  
Phosphate Solution ◽  
Type I ◽  
Hydroxyapatite Ceramic ◽  
Tooth Roots ◽  
Calcified Tissue

Fibronectin (FN) and type I collagen (Col), which are kinds of extracelluar matrices, were coprecipitated with calcium phosphate to form a composite layer on a hydroxyapatite (HAP) ceramic using a supersaturated calcium phosphate solution (CP solution). The amounts of protein immobilized in the layers were determined to be 20.97±3.04 µg·cm-2 for FN, 5.26±0.19 µg·cm-2 for Col and 21.72±2.30 µg·cm-2 for simultaneously immobilized FN and Col. When osteoblastic MC3T3-E1 cells were cultured on the HAP ceramics with the composite layer containing FN and/or Col, calcified tissue was formed through the activity of the cells. The result showed that the composite layer accelerated the differentiation of MC3T3-E1 to bone-forming cells. It is assumed that osteoblastic cells in alveolar bone migrated and differentiated on the surface of the tooth roots when the artificial tooth roots were covered with the composite layer.

scholarly journals Salivary Osteocalcin as Potential Diagnostic Marker of Periodontal Bone Destruction among Smokers

Biomolecules ◽  
2020 ◽  
Vol 10 (3) ◽  
pp. 380
Author(s):  
Betsy Joseph ◽  
Mukhatar Ahmed Javali ◽  
Mohasin Abdul Khader ◽  
Saad M. AlQahtani ◽  
Amanullah Mohammed
Keyword(s):  
Type I Collagen ◽  
Alveolar Bone ◽  
Diagnostic Marker ◽  
Bone Destruction ◽  
Alveolar Bone Loss ◽  
Youden Index ◽  
Type I ◽  
Healthy Controls ◽  
Pocket Depth ◽  
Probing Pocket Depth

The objective of the study was to assess the levels and diagnostic accuracy of salivary osteocalcin (OC), osteonectin (ON), and deoxypyridinoline-containing degradation fragment of the C-terminal telopeptide region of type I collagen (CTX) in adult smokers with periodontal bone destruction. Towards this, ninety systemically healthy patients (groups I: healthy, II: periodontitis with non-smokers, and III: periodontitis with current smokers) were included in the study. The results showed a positive correlation (weak to moderate) was observed for OC, ON, and CTX with probing pocket depth (PPD; r = 0.40, 0.32, and 0.36) and alveolar bone loss (BL; r = 0.58, 0.38, and 0.51) (p < 0.01). Smoker periodontitis was best discriminated from healthy controls using 15.25 ng/mL of OC (AUC: 0.870; 95% CI: 0.757–0.943; YI (Youden Index): 0.693; p < 0.0001). However, with a cut-off of BL at 33.33%, 19.24 ng/mL of salivary OC gave the best discrimination (AUC: 0.809; 95% CI: 0.686–0.900; Se: 80.0%; Sp: 73.47%, and YI: 0.534). A 16.45 ng/mL amount of OC gave excellent discrimination (AUC: 0.811; 95% CI: 0.688–0.901; Se: 92.31%; Sp: 65.22%, and YI: 0.575) among healthy and smoker periodontitis when PD at 6mm was considered as cut-off. Conclusion: The best discrimination between healthy controls and smoker periodontitis was obtained at 15.25 ng/mL of salivary OC.

Gene Expression of C2C12 Cells on Calcium Phosphate Ceramic In Vitro

2005 ◽  
Vol 288-289 ◽  
pp. 265-268 ◽  
Author(s):  
Yan Fei Tan ◽  
Ling Li Zhang ◽  
Xin Lai He ◽  
Wei Qiang Xiao ◽  
Hong Song Fan ◽  
...  
Keyword(s):  
Calcium Phosphate ◽  
Type I Collagen ◽  
C2c12 Cell ◽  
C2c12 Cells ◽  
Type I ◽  
Calcium Phosphate Ceramic ◽  
Mtt Method ◽  
Difference Expression

The osteoinduction of Calcium Phosphate (CaP) had been proved and generally been investigated by in vivo implantation. However, the mechanism of the osteoinductivity was not clear and it was difficult to judge the osteoinductivity in vitro. In this study, Mouse C2C12 cell line, a kind of myoblast precursor cell, was employed to co-culture with CaP. The induction of cell differentiation by materials was tested by MTT method, fluorescence observation, especially the mRNA expression of Osteocalcin, Type I collagen and Fibronectin by RT-PCR. It was founded that C2C12 cells could be induced to expression osteocalcin when growth on the surface of the HA/TCP ceramics. At the same time, the ceramics with different composition and sintering temperature seemed to induce difference expression level of the related genes. The results proved that phase composition was one of the most important factors in the regulation of bone-related genes. This study provided a potential model to evaluate the osteoinductivity of CaP ceramics in vitro.

Sphingomyelin Phosphodiesterase 3 Enhances Cytodifferentiation of Periodontal Ligament Cells

2016 ◽  
Vol 96 (3) ◽  
pp. 339-346 ◽  
Author(s):  
S. Miyauchi ◽  
J. Kitagaki ◽  
R. Masumoto ◽  
A. Imai ◽  
K. Kobayashi ◽  
...  
Keyword(s):  
Mrna Expression ◽  
Periodontal Ligament ◽  
Type I Collagen ◽  
Alveolar Bone ◽  
Skeletal Development ◽  
Aggressive Periodontitis ◽  
Periodontal Ligament Cells ◽  
Type I ◽  
Phosphodiesterase 3 ◽  
Pdl Cells

Sphingomyelin phosphodiesterase 3 ( Smpd3), which encodes neutral sphingomyelinase 2 (nSMase2), is a key molecule for skeletal development as well as for the cytodifferentiation of odontoblasts and alveolar bone. However, the effects of nSMase2 on the cytodifferentiation of periodontal ligament (PDL) cells are still unclear. In this study, the authors analyzed the effects of Smpd3 on the cytodifferentiation of human PDL (HPDL) cells. The authors found that Smpd3 increases the mRNA expression of calcification-related genes, such as alkaline phosphatase (ALPase), type I collagen, osteopontin, Osterix (Osx), and runt-related transcription factor (Runx)-2 in HPDL cells. In contrast, GW4869, an inhibitor of nSMase2, clearly decreased the mRNA expression of ALPase, type I collagen, and osteocalcin in HPDL cells, suggesting that Smpd3 enhances HPDL cytodifferentiation. Next, the authors used exome sequencing to evaluate the genetic variants of Smpd3 in a Japanese population with aggressive periodontitis (AgP). Among 44 unrelated subjects, the authors identified a single nucleotide polymorphism (SNP), rs145616324, in Smpd3 as a putative genetic variant for AgP among Japanese people. Moreover, Smpd3 harboring this SNP did not increase the sphingomyelinase activity or mRNA expression of ALPase, type I collagen, osteopontin, Osx, or Runx2, suggesting that this SNP inhibits Smpd3 such that it has no effect on the cytodifferentiation of HPDL cells. These data suggest that Smpd3 plays a crucial role in maintaining the homeostasis of PDL tissue.

Identification of Genes Differentially Regulated in Rat Alveolar Bone Wound Healing by Subtractive Hybridization

2004 ◽  
Vol 83 (7) ◽  
pp. 546-551 ◽  
Author(s):  
T. Ohira ◽  
F. Myokai ◽  
N. Shiomi ◽  
K. Yamashiro ◽  
T. Yamamoto ◽  
...  
Keyword(s):  
Wound Healing ◽  
Connective Tissue ◽  
Type I Collagen ◽  
Alveolar Bone ◽  
Subtractive Hybridization ◽  
Tissue Structure ◽  
Type I ◽  
Expression Of Genes ◽  
Periodontal Healing ◽  
Connective Tissue Structure

Periodontal healing requires the participation of regulatory molecules, cells, and scaffold or matrix. Here, we hypothesized that a certain set of genes is expressed in alveolar bone wound healing. Reciprocal subtraction gave 400 clones from the injured alveolar bone of Wistar rats. Identification of 34 genes and analysis of their expression in injured tissue revealed several clusters of unique gene regulation patterns, including the up-regulation at 1 wk of cytochrome c oxidase regulating electron transfer and energy metabolism, presumably occurring at the site of inflammation; up-regulation at 2.5 wks of pro-α-2 type I collagen involving the formation of a connective tissue structure; and up-regulation at 1 and 2 wks and down-regulation at 2.5 and 4 wks of ubiquitin carboxyl-terminal hydrolase l3 involving cell cycle, DNA repair, and stress response. The differential expression of genes may be associated with the processes of inflammation, wound contraction, and formation of a connective tissue structure.

EFFECT OF COLLAGEN ON THE MORPHOLOGY AND STRUCTURE OF CALCIUM PHOSPHATE NANOPARTICLES

2014 ◽  
Vol 26 (05) ◽  
pp. 1450061
Author(s):  
Hoda Salemi ◽  
Aliasghar Behnamghader ◽  
Mohamadreza Baghaban Eslaminejad ◽  
Mohammad Ataei
Keyword(s):  
Calcium Phosphate ◽  
Electrostatic Interactions ◽  
Type I Collagen ◽  
Bone Matrix ◽  
Control Sample ◽  
Molar Ratio ◽  
Type I ◽  
Sem Images ◽  
Collagen Concentration ◽  
Calcium Phosphate Nanoparticles

Collagen and noncollagenous proteins have an important role in the formation of mineral constituent of bone matrix. In this research, the morphology and phase characteristics of calcium phosphate nanoparticles in presence of collagen were investigated. The synthesis reaction was initiated by mixing H 3 PO 4 as phosphorous source and CaCl 2 as calcium source and type I collagen. Collagen concentration in suspension and Ca to P ratio was 1% and 1.67, respectively. The samples (with collagen and without collagen), were heat treated at 600°C and characterized by X-Ray diffraction (XRD), Fourier transformation infrared (FTIR) and scanning electron microscopy (SEM). More smaller and flake-like shape particles were observed in the SEM images of sample synthesized in the presence of collagen compared to the control sample which was constituted of larger granular particles. The XRD results revealed that the synthesized mineral powders with collagen were composed of hydroxyapatite and octacalcium phosphate. P – O and OH characteristic peaks were identified in FTIR spectra. In hybrid sample, the shift of amides band, revealed the electrostatic interactions between calcium phosphate ions and carboxyl or amino groups of collagen fibrils. The Ca to P molar ratio for sample with collagen was 1.9. It was found that the sample synthesized in the presence of collagen has a similar microstructure to natural bone.

scholarly journals Cobalt-containing Calcium Phosphate Induces Resorption of Biomineralized Collagen by Human Osteoclasts

2020 ◽  
Author(s):  
Daniel de Melo Pereira ◽  
Matthias Schumacher ◽  
Pamela Habibović
Keyword(s):  
Cell Culture ◽  
Calcium Phosphate ◽  
Calcium Release ◽  
Type I Collagen ◽  
Cell Culture Supernatant ◽  
Type I ◽  
Cobalt Ions ◽  
Collagen Membranes ◽  
Human Osteoclasts ◽  
Osteoclast Resorption

Abstract Background: Biomineralized collagen, consisting of fibrillary type-I collagen with embedded hydroxyapatite mineral, is a bone-mimicking material with potential application as a bone graft substitute. Despite the chemical and structural similarity with bone extracellular matrix, no evidence exists so far that biomineralized collagen can be resorbed by osteoclasts. The aim of the current study was to induce resorption of biomineralized collagen by osteoclasts by a two-fold modification: increasing the calcium phosphate content and introducing cobalt ions (Co2+), which have been previous shown to stimulate resorptive activity of osteoclasts.Methods: To this end, we produced biomineralized collagen membranes and coated them with a cobalt-containing calcium phosphate (CoCaP). Human osteoclasts, derived from CD14+ monocytes from peripheral blood, were differentiated directly on the membranes. Their morphology was assessed by laser confocal microscopy and their capacity for resorption observed by scanning electron microscopy (SEM), as well as indirectly quantified by calcium release into cell culture supernatant. Results: The CoCaP coating increased the mineral content of the membranes by 4 wt.% and their elastic modulus from 1 to 10 MPa. The coated membranes showed a sustained Co2+ release of about 7 nM per 2 days. In contrast to uncoated membranes, on CoCaP-coated biomineralized collagen membranes, osteoclasts sporadically formed actin rings, and caused resorption lacunae to form, as observed by SEM and confirmed by increase in Ca2+ concentration in cell culture medium. The effect of the CoCaP layer on osteoclast function is thought to be mainly caused by the increase of membrane stiffness, although the effect of Co2+, which was released in very low amounts, cannot be fully excluded.Conclusions: This work shows the potential of this relatively simple approach to induce osteoclast resorption of biomineralized collagen, despite the fact that the extent of osteoclast resorption was limited, and the method needs further optimization,. Moreover, the coating method is suitable for incorporating bioactive ions of interest into biomineralized collagen, which is typically not possible using the common biomineralization methods, such as polymer-induced liquid precursor method.

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 On the synthesis and characterization of β-tricalcium phosphate scaffolds coated with collagen or poly (D, L-lactic acid) for alveolar bone augmentation

2017 ◽  
Vol 11 (04) ◽  
pp. 496-502 ◽  
Author(s):  
Isadora S. Deschamps ◽  
Gabriel L. Magrin ◽  
Ricardo S. Magini ◽  
Márcio C. Fredel ◽  
Cesar A.M. Benfatti ◽  
...  
Keyword(s):  
Lactic Acid ◽  
Tricalcium Phosphate ◽  
Type I Collagen ◽  
Alveolar Bone ◽  
Porous Ceramic ◽  
Polyurethane Foams ◽  
Type I ◽  
X Ray ◽  
Collagen Group ◽  
Coating Method

ABSTRACT Objectives: After tooth loss, dimensional alterations on the alveolar bone ridge can occur that can negatively affect the placement of dental implants. The purpose of this study was to evaluate the synthesis, and mechanical properties of β-tricalcium phosphate (β-TCP) scaffolds coated with bioabsorbable polymers, namely, collagen and poly (D, L-lactic acid) (PDLLA). Materials and Methods: β-TCP powder was obtained by reactive milling and then characterized by X-ray diffraction and scanning electron microscopy/energy dispersive X-ray spectroscopy (SEM/EDS). β-TCP scaffolds were obtained by replica method, in which polyurethane foams are immersed in β-TCP suspension and thereafter submitted to a thermal treatment to remove the polyurethane and sinter the ceramic. Type-I collagen or PDLLA were used to coat the β-TCP scaffolds by dip-coating method. Scaffolds were separated in four groups depending on the coating material: noncoated (Group A), double immersion in collagen (Group B), double immersion in PDLLA (Group C), and ten immersions in PDLLA (Group D). Samples were characterized by compressive tests and SEM/EDS. Data were statistically analyzed through two-way ANOVA (p = 0.05). Results: Chemical and microscopic analyses revealed proper morphology and chemical composition of powder particles and scaffolds with or without polymeric coatings. Scaffolds coated with PDLLA showed higher compressive strength (0.11 ± 0.054 MPa) than those of collagen (0.022 ± 0.012 MPa) or noncoated groups (0.024 ± 0.012 MPa). Conclusions: The coating method of β-TCP with PDLLA revealed a potential strategy to increase the mechanical strength of porous ceramic materials while collagen can enhance cell migration.

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