In Vitro Evaluation of Type I Collagen-Based Scaffolds After Applying Different Sterilization Techniques

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.

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

Journal of Clinical Medicine ◽

10.3390/jcm10143141 ◽

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

Journal of Applied Biomaterials & Functional Materials ◽

10.1177/2280800021989698 ◽

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.

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In vitro phosphorylation of type I collagen by cyclic AMP-dependent protein kinase.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)57267-2 ◽

1986 ◽

Vol 261 (12) ◽

pp. 5674-5679

Author(s):

D B Glass ◽

J M McPherson

Keyword(s):

Protein Kinase ◽

Cyclic Amp ◽

Type I Collagen ◽

Type I ◽

Dependent Protein Kinase ◽

Dependent Protein

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

Biochemical Journal ◽

10.1042/bj2740615 ◽

1991 ◽

Vol 274 (2) ◽

pp. 615-617 ◽

Cited By ~ 32

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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Characterization of hydrogen sulphide reaction with rat-tail tendon Type I collagen in vitro

Journal of Periodontal Research ◽

10.1111/j.1600-0765.1985.tb00452.x ◽

1985 ◽

Vol 20 (4) ◽

pp. 403-410 ◽

Cited By ~ 6

Author(s):

P. W. Johnson ◽

J. Tonzetich ◽

R. H. Pearce

Keyword(s):

Hydrogen Sulphide ◽

Type I Collagen ◽

Type I ◽

Tail Tendon ◽

Rat Tail

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Development of Multilayered Chlorogenate-Peptide Based Biocomposite Scaffolds for Potential Applications in Ligament Tissue Engineering - An In Vitro Study

Journal of Biomimetics Biomaterials and Biomedical Engineering ◽

10.4028/www.scientific.net/jbbbe.34.37 ◽

2017 ◽

Vol 34 ◽

pp. 37-56 ◽

Cited By ~ 1

Author(s):

Harrison T. Pajovich ◽

Alexandra M. Brown ◽

Andrew M. Smith ◽

Sara K. Hurley ◽

Jessica R. Dorilio ◽

...

Keyword(s):

Tissue Regeneration ◽

Type I Collagen ◽

Phase Changes ◽

Peptide Sequence ◽

Proteoglycan Synthesis ◽

Type I ◽

Average Roughness ◽

Potential Applications ◽

Self Assembled

In this work, for the first time, chlorogenic acid, a natural phytochemical, was conjugated to a lactoferrin derived antimicrobial peptide sequence RRWQWRMKKLG to develop a self-assembled template. To mimic the components of extracellular matrix, we then incorporated Type I Collagen, followed by a sequence of aggrecan peptide (ATEGQVRVNSIYQDKVSL) onto the self-assembled templates for potential applications in ligament tissue regeneration. Mechanical properties and surface roughness were studied and the scaffolds displayed a Young’s Modulus of 169 MP and an average roughness of 72 nm respectively. Thermal phase changes were studied by DSC analysis. Results showed short endothermic peaks due to water loss and an exothermic peak due to crystallization of the scaffold caused by rearrangement of the components. Biodegradability studies indicated a percent weight loss of 27.5 % over a period of 37 days. Furthermore, the scaffolds were found to adhere to fibroblasts, the main cellular component of ligament tissue. The scaffolds promoted cell proliferation and displayed actin stress fibers indicative of cell motility and attachment. Collagen and proteoglycan synthesis were also promoted, demonstrating increased expression and deposition of collagen and proteoglycans. Additionally, the scaffolds exhibited antimicrobial activity against Staphylococcus epidermis bacteria, which is beneficial for minimizing biofilm formation if potentially used as implants. Thus, we have developed a novel biocomposite that may open new avenues to enhance ligament tissue regeneration.

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