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.

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

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.

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

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.

scholarly journals Effects of chitosan-collagen dressing on wound healing in vitro and in vivo assays

2021 ◽  
Vol 19 ◽  
pp. 228080002198969
Author(s):  
Min-Xia Zhang ◽  
Wan-Yi Zhao ◽  
Qing-Qing Fang ◽  
Xiao-Feng Wang ◽  
Chun-Ye Chen ◽  
...  
Keyword(s):  
Wound Healing ◽  
Wound Dressing ◽  
Type I Collagen ◽  
Inhibition Zone ◽  
Negative Control ◽  
Type I ◽  
Nih3t3 Cells ◽  
Post Operation

The present study was designed to fabricate a new chitosan-collagen sponge (CCS) for potential wound dressing applications. CCS was fabricated by a 3.0% chitosan mixture with a 1.0% type I collagen (7:3(w/w)) through freeze-drying. Then the dressing was prepared to evaluate its properties through a series of tests. The new-made dressing demonstrated its safety toward NIH3T3 cells. Furthermore, the CCS showed the significant surround inhibition zone than empty controls inoculated by E. coli and S. aureus. Moreover, the moisture rates of CCS were increased more rapidly than the collagen and blank sponge groups. The results revealed that the CCS had the characteristics of nontoxicity, biocompatibility, good antibacterial activity, and water retention. We used a full-thickness excisional wound healing model to evaluate the in vivo efficacy of the new dressing. The results showed remarkable healing at 14th day post-operation compared with injuries treated with collagen only as a negative control in addition to chitosan only. Our results suggest that the chitosan-collagen wound dressing were identified as a new promising candidate for further wound application.

scholarly journals Relative rates of biosynthesis of collagen type I, type V and type VI in calf cornea

1991 ◽  
Vol 274 (2) ◽  
pp. 615-617 ◽  
Author(s):  
P Kern ◽  
M Menasche ◽  
L Robert
Keyword(s):  
Type I Collagen ◽  
Collagen Type ◽  
Corneal Stroma ◽  
Collagen Type I ◽  
Type I ◽  
Type Vi Collagen ◽  
Sds Page ◽  
Proline Incorporation ◽  
Type V

The biosynthesis of type I, type V and type VI collagens was studied by incubation of calf corneas in vitro with [3H]proline as a marker. Pepsin-solubilized collagen types were isolated by salt fractionation and quantified by SDS/PAGE. Expressed as proportions of the total hydroxyproline solubilized, corneal stroma comprised 75% type I, 8% type V and 17% type VI collagen. The rates of [3H]proline incorporation, linear up to 24 h for each collagen type, were highest for type VI collagen and lowest for type I collagen. From pulse-chase experiments, the calculated apparent half-lives for types I, V and VI collagens were 36 h, 10 h and 6 h respectively.

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