Stability of the Magnesium Carbonate Apatite/Anionic Collagen Scaffolds: Effect of the Cross-Link Concentration

2011 ◽  
Vol 493-494 ◽  
pp. 844-848 ◽  
Author(s):  
Marcia S. Sader ◽  
Gutemberg Alves ◽  
Racquel Z. LeGeros ◽  
Gloria Dulce de Almeida Soares
Keyword(s):  
Bone Tissue ◽  
Culture Medium ◽  
Type I Collagen ◽  
Type I ◽  
Carbonate Apatite ◽  
Reaction Products ◽  
Collagen Scaffolds ◽  
Freeze Dried ◽  
The Cross

Natural bone constitutes of an inorganic phase (a biological nanoapatite) and an organic phase (mostly type I collagen). The challenge is to develop a material that can regenerate lost bone tissue with degradation and resorption kinetics compatible with the new bone formation. The aim of this study was to prepare self-organized magnesium and carbonate substituted apatite/collagen scaffolds, cross-linked with glutaraldehyde (GA). Bovine tendon was submitted to alkaline treatment resulting in a negatively charged collagen surface. The scaffolds were prepared by precipitation: simultaneous dropwise addition of solution containing calcium (Ca) and magnesium (Mg) ions and collagen into a buffered solution containing carbonate and phosphate ions in reaction vessel maintained at 37 °C, pH=8. The reaction products were cross-linked with 0.125 and 0.25% (v/v) glutaraldehyde (GA) solution and freeze-dried. The samples were characterized by Fourier-transformed infrared spectroscopy (FTIR). In vitro cytotoxicity (based on three parameters assays) and scaffolds degradation in culture medium and osteoblastic cells culture were performed in the cross-linked materials. No cytotoxic effects were observed. The cross-linked samples with the lower GA concentration showed a lower stability when placed in contact with culture medium. Human osteoblasts attached on the scaffolds surface cross-linked with 0.25% GA, forming a continuous layer after 14 days of incubation. These results showed potential application of the designed scaffolds for bone tissue engineering.

The effects of different crossing-linking conditions of genipin on type I collagen scaffolds: an in vitro evaluation

2014 ◽  
Vol 15 (4) ◽  
pp. 531-541 ◽  
Author(s):  
Xiujie Zhang ◽  
Xueying Chen ◽  
Ting Yang ◽  
Naili Zhang ◽  
Li Dong ◽  
...  
Keyword(s):  
Type I Collagen ◽  
Type I ◽  
Collagen Scaffolds ◽  
In Vitro Evaluation

Linkage of chondroitin-sulfate to type I collagen scaffolds stimulates the bioactivity of seeded chondrocytes in vitro

Biomaterials ◽  
2001 ◽  
Vol 22 (17) ◽  
pp. 2359-2369 ◽  
Author(s):  
Job L.C van Susante ◽  
Jeroen Pieper ◽  
Pieter Buma ◽  
Toin H van Kuppevelt ◽  
Henk van Beuningen ◽  
...  
Keyword(s):  
Chondroitin Sulfate ◽  
Type I Collagen ◽  
Type I ◽  
Collagen Scaffolds

A Collagen/DBP Sponge System Designed for in Vitro Analysis of Chondroinduction

1991 ◽  
Vol 252 ◽  
Author(s):  
Shuichi Mizuno ◽  
Chris Lycette ◽  
Charlene Quinto ◽  
Julie Glowacki
Keyword(s):  
Type I Collagen ◽  
Three Dimensional ◽  
Dermal Fibroblasts ◽  
Type I ◽  
Cellular Mechanisms ◽  
Fresh Tissue ◽  
Freeze Dried ◽  
Bone Powder

ABSTRACTIn response to subcutaneous implants of demineralized bone powder (DBP), cells are attracted to the DBP, are converted to chondroblasts, and produce a cartilage matrix that is resorbed and replaced by bone. In order to define the cellular mechanisms of this induction, we developed a collagen sponge model for simulating the in vivo environment and for promoting the ingrowth and viability of cells cultured in them in vitro. Reconstituted pepsin–digested type I collagen from bovine hide was neutralized. Rat DBP (75–250 εm) was added into the collagen mixture (20 mg/ml). In order to simulate the connective tissue environment, modified chondroitin sulfate, heparan sulfate, or hyaluronic acid was added into the mixture. Aliquots (0.2 ml) were placed in 3/8 inch diameter molds and freeze-dried. Human dermal fibroblasts were cultured from minced fresh tissue and inoculated at 1.5 × 105 cells/sponge. Fifteen hours later, some sponges were transferred to medium which contained growth factors (PDGF or TGF-β). At intervals, samples were examined histologically. The inoculated cells attached to the collagen fibers and migrated into the sponge. Eventually the sponges contracted and acquired an oval shape. Cells on or near DBP were ovoid or stellate in shape. Cell morphology was modulated by glycosaminoglycan composition of the sponge. Increasing doses of PDGF or TGF-β promoted cellularity within the sponges. In conclusion, this system simulates the in vivo environment but allows accessibility for analysis. This three-dimensional matrix culture system will enable investigation of mechanisms of chondroinduction by morphogenic material.

scholarly journals Biologically Inspired Collagen/Apatite Composite Biomaterials for Potential Use in Bone Tissue Regeneration—A Review

Materials ◽  
2020 ◽  
Vol 13 (7) ◽  
pp. 1748 ◽  
Author(s):  
Barbara Kołodziejska ◽  
Agnieszka Kaflak ◽  
Joanna Kolmas
Keyword(s):  
Bone Tissue ◽  
Orthopedic Surgery ◽  
Type I Collagen ◽  
Bone Tissue Regeneration ◽  
Type I ◽  
Biologically Inspired ◽  
Natural Composite ◽  
Potential Use

Type I collagen and nanocrystalline-substituted hydroxyapatite are the major components of a natural composite—bone tissue. Both of these materials also play a significant role in orthopedic surgery and implantology; however, their separate uses are limited; apatite is quite fragile, while collagen’s mechanical strength is very poor. Therefore, in biomaterial engineering, a combination of collagen and hydroxyapatite is used, which provides good mechanical properties with high biocompatibility and osteoinduction. In addition, the porous structure of the composites enables their use not only as bone defect fillers, but also as a drug release system providing controlled release of drugs directly to the bone. This feature makes biomimetic collagen–apatite composites a subject of research in many scientific centers. The review focuses on summarizing studies on biological activity, tested in vitro and in vivo.

scholarly journals In Vitro Characterization of Multilamellar Fibers with Uniaxially Oriented Electrospun Type I Collagen Scaffolds

2020 ◽  
Vol 2020 ◽  
pp. 1-13
Author(s):  
Alireza Hooshmand-Ardakani ◽  
Tahereh Talaei-Khozani ◽  
Mehdi Sadat-Shojai ◽  
Soghra Bahmanpour ◽  
Nehleh Zarei-fard
Keyword(s):  
Raman Spectra ◽  
Type I Collagen ◽  
Human Adipose Tissue ◽  
Type I ◽  
Fiber Morphology ◽  
Collagen Scaffolds ◽  
Fiber Layer ◽  
In Vitro Characterization ◽  
Ethylcarbodiimide Hydrochloride

Fabrication of an appropriate scaffold is critical in order to recapitulate the architecture and functionality of the native tissue. In this study, we attempted to create favorable collagen fiber alignment and multilamellar with uniaxially oriented layers, using a disc collector by turning mats 90 degrees horizontally at specific times. Different concentrations of rat tail-derived type I collagen (3, 6, 8% w/v) in 1,1,1,3,3,3-hexafluoroisopropanol (HFIP) are used for electrospinning affairs. The 6% w/v collagen at an applied voltage of 20 kV and collector rotation of 2500 rpm was selected to exhibit bead-free homogeneous nanofiber with fiber thickness of 0.14 ± 0.4 µm, maximum thickness of 0.5 ± 0.08 µm, and 60% porosity. Also, scanning electron microscope images of electrospun fibers showed 3D multilamellar scaffold with the goodness of 96.5% ± 0.8 in each aligned uniaxially oriented fiber layer. Cross-linking of collagen fibers with N-(3-dimethylaminopropyl)-N0-ethylcarbodiimide hydrochloride (EDC)/N-hydroxysuccinimide (NHS) reduced the fiber degradation rate and preserved the fiber morphology and alignment. The multilamellar mat showed significant increase in tensile strength and average breaking elongation in comparison with unilamellar mat. In vitro cell culture, using human adipose tissue-derived mesenchymal stem cells (hAT-MSCs) on cross-linked scaffold, showed improvement in cell proliferation, attachment, migration, and intercellular junction with a flattened morphology. Raman spectra revealed the preservation of collagen structure. In addition, Raman spectra of the cell containing scaffold were the same as those of an intact intervertebral disc as a sample to be used in engineering tissues. In conclusion, our results showed that the 3D multilamellar collagen nanofibrous scaffold is more appropriate for the tissues that have multilamellar structure.

Biomimetic Fabrication and Characterization of BG/COL/HCA Scaffolds for Bone Tissue Engineering

2007 ◽  
Vol 336-338 ◽  
pp. 1574-1576
Author(s):  
Xiao Feng Chen ◽  
Ying Jun Wang ◽  
Chun Rong Yang ◽  
Na Ru Zhao
Keyword(s):  
Tissue Engineering ◽  
Calcium Phosphate ◽  
Bioactive Glass ◽  
Bone Tissue Engineering ◽  
Bone Tissue ◽  
Type I Collagen ◽  
Porous Scaffold ◽  
Sol Gel ◽  
Type I ◽  
Carbonate Apatite

The bone tissue engineering scaffold was developed by compounded the type I collagen with the porous scaffold of the sol-gel derived bioactive glass (BG) in the system CaO-P2O5-SiO2. The resultant porous scaffold was treated in supersaturated calcification solution (SCS) to form the surface layer of hydroxyl-carbonate-apatite (HCA) since the type I collagen possessed good biocompatibility and bio-absorbability, and also, the ability of inducting calcium phosphates to precipitated inside and outside the collagen fibers where the collagen fibers acted as bio-macromolecules template for formation of bone-like inorganic minerals in nature bone such as: octo-calcium phosphate (OCP), tri-calcium phosphate (TCP) and hydroxyl-carbonate-apatite (HCA). On the other hand, the sol-gel derived bioactive glass also played an important role in formation of the above bio-minerals owing to its serial chemical reactions with the body fluid. The in vitro study in supersaturated calcification solution SCS indicated that the surface of the porous scaffold was able to induce formation of bone-like HCA crystals on the pore walls of the scaffold which possessed satisfactory cells biocompatibility.

Collagen fibrillogenesis in vitro: interaction of types I and V collagen

1986 ◽  
Vol 44 ◽  
pp. 210-211
Author(s):  
Arthur J. Wasserman ◽  
Kathy C. Kloos ◽  
David E. Birk
Keyword(s):  
Type I Collagen ◽  
Corneal Stroma ◽  
Minor Component ◽  
Homogeneous Distribution ◽  
Type I ◽  
Type V Collagen ◽  
Fibril Morphology ◽  
Type V ◽  
In Vitro Interaction

Type I collagen is the predominant collagen in the cornea with type V collagen being a quantitatively minor component. However, the content of type V collagen (10-20%) in the cornea is high when compared to other tissues containing predominantly type I collagen. The corneal stroma has a homogeneous distribution of these two collagens, however, immunochemical localization of type V collagen requires the disruption of type I collagen structure. This indicates that these collagens may be arranged as heterpolymeric fibrils. This arrangement may be responsible for the control of fibril diameter necessary for corneal transparency. The purpose of this work is to study the in vitro assembly of collagen type V and to determine whether the interactions of these collagens influence fibril morphology.

scholarly journals Restoration of Osteogenesis by CRISPR/Cas9 Genome Editing of the Mutated COL1A1 Gene in Osteogenesis Imperfecta

2021 ◽  
Vol 10 (14) ◽  
pp. 3141
Author(s):  
Hyerin Jung ◽  
Yeri Alice Rim ◽  
Narae Park ◽  
Yoojun Nam ◽  
Ji Hyeon Ju
Keyword(s):  
Osteogenesis Imperfecta ◽  
Type I Collagen ◽  
Disease Modeling ◽  
Bone Fragility ◽  
Osteogenic Potential ◽  
Type I ◽  
Gene Correction ◽  
Col1a1 Gene ◽  
Collagen Formation

Osteogenesis imperfecta (OI) is a genetic disease characterized by bone fragility and repeated fractures. The bone fragility associated with OI is caused by a defect in collagen formation due to mutation of COL1A1 or COL1A2. Current strategies for treating OI are not curative. In this study, we generated induced pluripotent stem cells (iPSCs) from OI patient-derived blood cells harboring a mutation in the COL1A1 gene. Osteoblast (OB) differentiated from OI-iPSCs showed abnormally decreased levels of type I collagen and osteogenic differentiation ability. Gene correction of the COL1A1 gene using CRISPR/Cas9 recovered the decreased type I collagen expression in OBs differentiated from OI-iPSCs. The osteogenic potential of OI-iPSCs was also recovered by the gene correction. This study suggests a new possibility of treatment and in vitro disease modeling using patient-derived iPSCs and gene editing with CRISPR/Cas9.

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