scholarly journals Experimental investigation of temperature-dependent denaturation behavior of type-I Collagen

2019 ◽  
Author(s):  
İ. Deniz Derman ◽  
Esat C. Şenel ◽  
Onur Ferhanoğlu ◽  
İnci Çilesiz
Keyword(s):  
Tissue Repair ◽  
Type I Collagen ◽  
Wide Field ◽  
Type I ◽  
Temperature Dependent ◽  
Tissue Welding ◽  
Buffer Solutions ◽  
Collagen Denaturation ◽  
Different Temperatures ◽  
Tail Tendon

AbstractPrecise investigation of the temperature and the duration for collagen denaturation is critical for a number of applications, such as adjustment of temperature and duration during a laser-assisted tissue welding or collagen-based tissue repair products (films, implants, cross-linkers) preparation procedures. The result of such studies can serve as a guideline to mitigate potential side effects while maintaining the functionality of the collagen. Though a variety of collagen denaturation temperatures have been reported, there has not been a systematic study to report temperature-dependent denaturation rates. In this study, we perform a set of experiments on type-I collagen fiber bundles, extracted from the rat-tail tendon, and provide an Arrhenius model based on the acquired data. The tendons are introduced to buffer solutions having different temperatures, while monitoring the contrast in the crimp sights with a wide field microscope, where collagen fibers bend with respect to their original orientation. For all tested temperatures of 50°C–70 °C and tissues that were extracted from 5 rats, increasing the temperature reduced the contrast. On the average, we observed a decay of the contrast to half of its initial value at 37, 157, and 266 seconds when the collagen was introduced to 70 °C, 65 °C, and 60 °C buffer solutions, respectively. For the lower temperatures tested we only observed to be only about 20% and 2 % decay in the crimp contrast after > 2 hours at 55 °C and 50 °C, respectively. The observed denaturation behavior is also in line with Arrhenius Law, as expected. We are looking forward to expand this study to other types of collagen as a future work. Overall, with further development the data and model we present here could potentially serve as a guideline to determine limits for welding and manufacturing process of collagen-based tissue repair agents.

Type I collagen degradation during tissue repair: Comparison of mechanisms following fracture and acute coronary syndromes

Bone ◽  
2014 ◽  
Vol 69 ◽  
pp. 1-5 ◽  
Author(s):  
Rachel Stansfield ◽  
Fatma Gossiel ◽  
Allison Morton ◽  
Christopher Newman ◽  
Richard Eastell
Keyword(s):  
Acute Coronary Syndromes ◽  
Tissue Repair ◽  
Type I Collagen ◽  
Collagen Degradation ◽  
Type I ◽  
Coronary Syndromes

Influence of Decorin and Biglycan on Mechanical Properties of Multiple Tendons in Knockout Mice

2005 ◽  
Vol 127 (1) ◽  
pp. 181-185 ◽  
Author(s):  
Paul S. Robinson ◽  
Tung-Fu Huang ◽  
Elan Kazam ◽  
Renato V. Iozzo ◽  
David E. Birk ◽  
...  
Keyword(s):  
Mechanical Properties ◽  
Type I Collagen ◽  
Specific Treatment ◽  
Treatment Modalities ◽  
Type I ◽  
Tail Tendon ◽  
And Function ◽  
Flexor Digitorum ◽  
In Vivo Loading

Evaluations of tendon mechanical behavior based on biochemical and structural arrangement have implications for designing tendon specific treatment modalities or replacement strategies. In addition to the well studied type I collagen, other important constituents of tendon are the small proteoglycans (PGs). PGs have been shown to vary in concentration within differently loaded areas of tendon, implicating them in specific tendon function. This study measured the mechanical properties of multiple tendon tissues from normal mice and from mice with knock-outs of the PGs decorin or biglycan. Tail tendon fascicles, patellar tendons (PT), and flexor digitorum longus tendons (FDL), three tissues representing different in vivo loading environments, were characterized from the three groups of mice. It was hypothesized that the absence of decorin or biglycan would have individual effects on each type of tendon tissue. Surprisingly, no change in mechanical properties was observed for the tail tendon fascicles due to the PG knockouts. The loss of decorin affected the PT, causing an increase in modulus and stress relaxation, but had little effect on the FDL. Conversely, the loss of biglycan did not significantly affect the PT, but caused a reduction in both the maximum stress and modulus of the FDL. These results give mechanical support to previous biochemical data that tendons likely are uniquely tailored to their specific location and function. Variances such as those presented here need to be further characterized and taken into account when designing therapies or replacements for any one particular tendon.

Effects of Hydration on Nanoscale Structural Morphology and Mechanics of Individual Type I Collagen Fibrils

2012 ◽  
Vol 1465 ◽  
Author(s):  
Joseph M. Wallace ◽  
Chad Harding ◽  
Arika Kemp
Keyword(s):  
Type I Collagen ◽  
Type I ◽  
Mechanical Function ◽  
Structural Morphology ◽  
Force Microscopy ◽  
Atomic Force ◽  
Individual Type ◽  
Nanoscale Structure ◽  
Tail Tendon ◽  
Morphology And Mechanical Properties

ABSTRACTType I collagen is one of the most vital proteins in our bodies and serves a number of structural roles. Despite collagen’s importance, little is known about its nanoscale morphology in tissues and how morphology relates to mechanical function. This study directly probes nanoscale structure and mechanics in collagen as a function of hydration utilizing atomic force microscopy investigations of the mouse tail tendon. We demonstrate that collagen morphology and mechanical properties at the nanoscale change with dehydration, indicating that hydration is a factor which must be considered when performing studies at any length scale in collagen-based tissues. Studies are underway to further investigate this phenomenon and to determine how these properties change with disease in tendon and other Type I collagen-based tissues.

scholarly journals Methacrylation Induces Rapid, Temperature-Dependent, Reversible Self-Assembly of Type-I Collagen

Langmuir ◽  
2014 ◽  
Vol 30 (37) ◽  
pp. 11204-11211 ◽  
Author(s):  
Kathryn E. Drzewiecki ◽  
Avanish S. Parmar ◽  
Ian D. Gaudet ◽  
Jonathan R. Branch ◽  
Douglas H. Pike ◽  
...  
Keyword(s):  
Self Assembly ◽  
Type I Collagen ◽  
Type I ◽  
Temperature Dependent ◽  
Rapid Temperature

scholarly journals Ozonized solutions favor the repair of experimentally induced skin wounds in rats

2020 ◽  
Vol 40 (11) ◽  
pp. 914-921
Author(s):  
Rafael C. Sanguanini ◽  
Mariana F. Bento ◽  
Evelyn de Oliveira ◽  
Emmanuel Arnhold ◽  
Mariana B.R. Faleiro ◽  
...  
Keyword(s):  
Sodium Chloride ◽  
Tissue Repair ◽  
Wound Repair ◽  
Type I Collagen ◽  
Type I ◽  
Skin Wounds ◽  
The Third ◽  
Picrosirius Red ◽  
Morphometric Evaluation ◽  
Experimentally Induced

ABSTRACT: This study aimed to evaluate and compare the effects of ozonized solutions on tissue wound repair in rats. Treatments consisted of ozonized water (GA), 0.9% sodium chloride (GCL), ozonized oil (GO), and 0.2% allantoin cream (GAL). The morphometric evaluation showed that wounds of the GA group presented a higher degree of retraction (p<0.05) at three and eight days of treatment (37.96 and 84.81%, respectively). Picrosirius red staining showed that groups GA and GO presented higher deposition (p<0.05) of type I collagen at 15 and 22 days of treatment, respectively. The neovascularization was higher in wounds of group GO on days 3, 8, and 15 (p<0.05), with higher VEGF immunostaining. (p<0.05). Thus, ozonized water enhances wound retraction and assists in the maturation and remodeling phase, while ozonized oil promotes higher neovascularization during tissue repair and higher deposition of type I collagen from the third week of treatment.

scholarly journals Assessment of carvacrol paste as endodontic medication associated with laser photobiomodulation in tissue repair: an experimental study in rats

2020 ◽  
Vol 36 (5) ◽  
Author(s):  
Ismário Silva Meneses ◽  
Ricardo Luiz Cavalcanti de Albuquerque Júnior ◽  
Felipe de Souza Matos ◽  
Aline Aragão Pereira Macedo ◽  
Adriano Antunes de Souza Araújo ◽  
...  
Keyword(s):  
Tissue Repair ◽  
Wistar Rats ◽  
Type I Collagen ◽  
Subcutaneous Tissue ◽  
Fibrous Tissue ◽  
Tissue Reaction ◽  
Type Iii Collagen ◽  
Type I ◽  
Subcutaneous Implantation ◽  
Inflammatory Infiltration

This study aimed to analyze the tissue reaction caused by carvacrol paste associated or not with laser photobiomodulation (LPBM) at λ660 nm in the subcutaneous tissue of rats. Sixty Wistar rats were divided into four groups and they received the following interventions: subcutaneous implantation of empty polyethylene tubes (CTR), implantation of tubes containing carvacrol paste (CVC), implantation of empty tubes and LPBM (LLLT), and implantation of tubes containing carvacrol paste and LPBM (CVCLT). The animals were euthanized at three, eight, and 15 days after surgery. The inflammatory reaction and fibroplasia were analyzed histomorphometrically. Significant differences among the groups were determined by ANOVA and Tukey's test (p<0.05). In the 3-day period, the CVCLT group had low inflammatory infiltration (p<0.01). In the 8- and 15-day periods, the LLLT and CVCLT groups presented a low amount of lymphocytic inflammatory infiltrate (p<0.01 and p<0.05). Regarding the formation of fibrous tissue, the CVC group had the highest formation of type III collagen in the 8-day period (p<0.001). In the 15-day period, the CVCLT group had a lower formation of type I collagen than the CTR and LLLT groups (p<0.05). The use of the carvacrol paste associated with photobiomodulation optimizes the inflammatory period and tissue repair.

scholarly journals Collagen Scaffolds in Bone Sialoprotein-Mediated Bone Regeneration

2013 ◽  
Vol 2013 ◽  
pp. 1-6 ◽  
Author(s):  
Thomas E. Kruger ◽  
Andrew H. Miller ◽  
Jinxi Wang
Keyword(s):  
Bone Regeneration ◽  
Tissue Repair ◽  
Type I Collagen ◽  
Structural Integrity ◽  
Natural Fibers ◽  
Bone Sialoprotein ◽  
Type I ◽  
Collagen Scaffolds ◽  
Mineral Deposition ◽  
Mediate Cell

Decades of research in bioengineering have resulted in the development of many types of 3-dimentional (3D) scaffolds for use as drug delivery systems (DDS) and for tissue regeneration. Scaffolds may be comprised of different natural fibers and synthetic polymers as well as ceramics in order to exert the most beneficial attributes including biocompatibility, biodegradability, structural integrity, cell infiltration and attachment, and neovascularization. Type I collagen scaffolds meet most of these criteria. In addition, type I collagen binds integrins through RGD and non-RGD sites which facilitates cell migration, attachment, and proliferation. Type I collagen scaffolds can be used for bone tissue repair when they are coated with osteogenic proteins such as bone morphogenic protein (BMP) and bone sialoprotein (BSP). BSP, a small integrin-binding ligand N-linked glycoprotein (SIBLING), has osteogenic properties and plays an essential role in bone formation. BSP also mediates mineral deposition, binds type I collagen with high affinity, and bindsαvβ3andαvβ5integrins which mediate cell signaling. This paper reviews the emerging evidence demonstrating the efficacy of BSP-collagen scaffolds in bone regeneration.

Sign in / Sign up

Export Citation Format

Share Document