Fibrillogenesis in Dense Collagen Solutions: A Physicochemical Study

Gobeaux, Frédéric; Mosser, Gervaise; Anglo, Anny; Panine, Pierre; Davidson, Patrick; Giraud‐Guille, Marie‐Madeleine; Belamie, Emmanuel

doi:10.1016/j.jmb.2007.12.047

Cited by 169 publications

(203 citation statements)

References 64 publications

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“…The presence of GAG however, particularly CS, seems to play an important role in regulating Col I fibril formation as it happened even at pH 4. Also, the concentration of Col I affects strongly fibril formation as found previously [40,41]. Presumably CS binds to collagen molecules and facilitates the organization of mature fibrils by increasing collagen concentration as it was found in the presence of 4,6-disulfated disaccharides structures, previously [38].…”

Section: Physicochemical Characterization Of Polyelectrolyte Multilaysupporting

confidence: 58%

Molecular composition of GAG-collagen I multilayers affects remodeling of terminal layers and osteogenic differentiation of adipose-derived stem cells

et al. 2016

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T. (2016) Molecular composition of GAG-collagen I multilayers affects remodeling of terminal layers and osteogenic differentiation of adipose-derived stem cells. Acta Biomaterialia, 41, pp. 86-99. (doi:10.1016Biomaterialia, 41, pp. 86-99. (doi:10. /j.actbio.2016 This is the author's final accepted version.There may be differences between this version and the published version. You are advised to consult the publisher's version if you wish to cite from it.http://eprints.gla.ac.uk/119626/ AbstractThe effect of molecular composition of multilayers, by pairing type I collagen (Col I) with either hyaluronic acid (HA) or chondroitin sulfate (CS) was studied regarding the osteogenic differentiation of adhering human adipose-derived stem cells (hADSCs). Multilayer (PEM)formation was based primarily on ion pairing and on additional intrinsic cross-linking through imine bond formation replacing native by oxidized HA (oHA) or CS (oCS) with Col I.Significant amounts of Col I fibrils were found on both native and oxidized CS-based PEMs, resulting in higher water contact angles and surface potential under physiological condition, while much less organized Col I was detected in either HA-based multilayers, which were more hydrophilic and negatively charged. An important finding was that hADSCs remodeled Col I at the terminal layers of PEMs by mechanical reorganization and pericellular proteolytic degradation, being more pronounced on CS-based PEMs. This was in accordance with the higher quantity of Col I deposition in this system, accompanied by more cell spreading, focal adhesions (FA) formation and significant α2β1 integrin recruitment compared to HA-based PEMs. Both CS-based PEMs caused also an increased fibronectin (FN) secretion and cell growth. Furthermore, significant calcium phosphate deposition, enhanced ALP, Col I and Runx2 expression were observed in hADSCs on CS-based PEMs, particularly on oCS-containing one. Overall, multilayer composition can be used to direct cell-matrix interactions, and hence stem cell fates showing for the first time that PEMs made of biogenic polyelectrolytes undergo significant remodeling of terminal protein layers, which enables cells to form a more adequate extracellular matrix-like environment.

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Section: Physicochemical Characterization Of Polyelectrolyte Multilaysupporting

confidence: 58%

Molecular composition of GAG-collagen I multilayers affects remodeling of terminal layers and osteogenic differentiation of adipose-derived stem cells

et al. 2016

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“…29 Scanning and transmission electron microscopy ͑SEM/TEM͒ can be used to probe the collagen microstructure, but only in thin samples and following extensive preprocessing. 30 Other techniques such as polarization microscopy exploit the unique birefringence properties of collagen fibers, but yield quantitative results only in thin samples as well. 31 Noninvasive imaging approaches to visualize the fibrillar types of collagen in thick specimens are being developed as more suitable alternatives for in vivo applications.…”

Section: Discussionmentioning

confidence: 99%

Fully automated, quantitative, noninvasive assessment of collagen fiber content and organization in thick collagen gels

Bayan

Levitt

Miller

et al. 2009

Journal of Applied Physics

109

124

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Collagen is the most prominent protein of human tissues. Its content and organization define to a large extent the mechanical properties of tissue as well as its function. Methods that have been used traditionally to visualize and analyze collagen are invasive, provide only qualitative or indirect information, and have limited use in studies that aim to understand the dynamic nature of collagen remodeling and its interactions with the surrounding cells and other matrix components. Second harmonic generation ͑SHG͒ imaging emerged as a promising noninvasive modality for providing high-resolution images of collagen fibers within thick specimens, such as tissues. In this article, we present a fully automated procedure to acquire quantitative information on the content, orientation, and organization of collagen fibers. We use this procedure to monitor the dynamic remodeling of collagen gels in the absence or presence of fibroblasts over periods of 12 or 14 days. We find that an adaptive thresholding and stretching approach provides great insight to the content of collagen fibers within SHG images without the need for user input. An additional feature-erosion and feature-dilation step is useful for preserving structure and noise removal in images with low signal. To quantitatively assess the orientation of collagen fibers, we extract the orientation index ͑OI͒, a parameter based on the power distribution of the spatial-frequency-averaged, two-dimensional Fourier transform of the SHG images. To measure the local organization of the collagen fibers, we access the Hough transform of small tiles of the image and compute the entropy distribution, which represents the probability of finding the direction of fibers along a dominant direction. Using these methods we observed that the presence and number of fibroblasts within the collagen gel significantly affects the remodeling of the collagen matrix. In the absence of fibroblasts, gels contract, especially during the first few days, in a manner that allows the fibers to remain mostly disoriented, as indicated by small OI values. Subtle changes in the local organization of fibers may be taking place as the corresponding entropy values of these gels show a small decrease. The presence of fibroblasts affects the collagen matrix in a manner that is highly dependent on their number. A low density of fibroblasts enhances the rate of initial gel contraction, but ultimately leads to degradation of collagen fibers, which start to organize in localized clumps. This degradation and reorganization is seen within the first days of incubation with fibroblasts at a high density and is followed by de novo collagen fiber deposition by the fibroblasts. These collagen fibers are more highly oriented and organized than the fibers of the original collagen gel. These initial studies demonstrate that SHG imaging in combination with automated image analysis approaches offer a noninvasive and easily implementable method for characterizing important features of the content and organization of collage...

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“…As discussed in the previous section, several authors have studied the effects of parameters like pH, ionic strength and temperature on fibrillogenesis [11,[22][23][24]37]. Some of them already pointed out that, regarding the process of self-assembly, the modulation of these parameters can determine modifications at the micro-structural level in terms of the fibril size and the electrostatic interactions between neighboring fibrils [20,21,23,[33][34][35]38].…”

Section: (Kpa)mentioning

confidence: 99%

“…Ionization and electrostatic interactions between amino acid residues are regulated by factors such as pH and ionic strength. The formation of net charges between collagen molecules of neighboring fibrils may determine electrostatic attractions that can stabilize the matrix as well as affect the size of the fibrils and consequently the structure of the matrix [20][21][22][23]. Moreover, temperature affects the hydrophobic interactions and therefore the kinetics of collagen fibrillogenesis as well as pH and ionic strength [20,23,24].…”

Section: Introductionmentioning

confidence: 99%

Tailoring Mechanical Properties of Collagen-Based Scaffolds for Vascular Tissue Engineering: The Effects of pH, Temperature and Ionic Strength on Gelation

2010

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Collagen gels have been widely studied for applications in tissue engineering because of their biological implications. Considering their use as scaffolds for vascular tissue engineering, the main limitation has always been related to their low mechanical properties. During the process of in vitro self-assembly, which leads to collagen gelation, the size of the fibrils, their chemical interactions, as well as the resulting microstructure are regulated by three main experimental conditions: pH, ionic strength and temperature. In this work, these three parameters were modulated in order to increase the mechanical properties of collagen gels. The effects on the gelation process were assessed by turbidimetric and scanning electron microscopy analyses. Turbidity measurements showed that gelation was affected by all three factors and scanning electron images confirmed that major changes occurred at the microstructural level. Mechanical tests showed that the compressive and tensile moduli increased by four-and three-fold, respectively, compared to the control. Finally, viability tests confirmed that these gels are suitable as scaffolds for cellular adhesion and proliferation.

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Fibrillogenesis in Dense Collagen Solutions: A Physicochemical Study

Cited by 169 publications

References 64 publications

Molecular composition of GAG-collagen I multilayers affects remodeling of terminal layers and osteogenic differentiation of adipose-derived stem cells

Molecular composition of GAG-collagen I multilayers affects remodeling of terminal layers and osteogenic differentiation of adipose-derived stem cells

Fully automated, quantitative, noninvasive assessment of collagen fiber content and organization in thick collagen gels

Tailoring Mechanical Properties of Collagen-Based Scaffolds for Vascular Tissue Engineering: The Effects of pH, Temperature and Ionic Strength on Gelation

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