Glutaraldehyde crosslinking of collagen: Effects of time, temperature, concentration and presoaking as measured by shrinkage temperature

Ruijgrok, J.M.; Wijn, J.R. de; Boon, Mathilde E.

doi:10.1016/0267-6605(94)90044-2

Cited by 27 publications

(19 citation statements)

References 7 publications

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“…15,21,22 Despite the widespread use of crosslinking treatments on collagen films, fibers, and scaffolds, a detailed analysis has not been carried out to determine how the process variables affect CG scaffold properties. Previous studies have concentrated on optimizing the effectiveness of individual crosslinking treatments, 15,17,21,23 but a study directly comparing the effectiveness of several grades of different treatments has yet to be carried out. Additionally, many studies have investigated crosslinking of collagen fibers or films that may not be directly comparably to the crosslinking of a CG scaffold.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Crosslinking and Mechanical Properties Significantly Influence Cell Attachment, Proliferation, and Migration Within Collagen Glycosaminoglycan Scaffolds

Haugh

Murphy

McKiernan

et al. 2011

Tissue Engineering Part A

280

269

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Crosslinking and the resultant changes in mechanical properties have been shown to influence cellular activity within collagen biomaterials. With this in mind, we sought to determine the effects of crosslinking on both the compressive modulus of collagen-glycosaminoglycan scaffolds and the activity of osteoblasts seeded within them. Dehydrothermal, 1-ethyl-3-3-dimethyl aminopropyl carbodiimide and glutaraldehyde crosslinking treatments were first investigated for their effect on the compressive modulus of the scaffolds. After this, the most promising treatments were used to study the effects of crosslinking on cellular attachment, proliferation, and infiltration. Our experiments have demonstrated that a wide range of scaffold compressive moduli can be attained by varying the parameters of the crosslinking treatments. 1-Ethyl-3-3-dimethyl aminopropyl carbodiimide and glutaraldehyde treatments produced the stiffest scaffolds (fourfold increase when compared to dehydrothermal crosslinking). When cells were seeded onto the scaffolds, the stiffest scaffolds also showed increased cell number and enhanced cellular distribution when compared to the other groups. Taken together, these results indicate that crosslinking can be used to produce collagen-glycosaminoglycan scaffolds with a range of compressive moduli, and that increased stiffness enhances cellular activity within the scaffolds.

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Section: Introductionmentioning

confidence: 99%

“…Additionally, many studies have investigated crosslinking of collagen fibers or films that may not be directly comparably to the crosslinking of a CG scaffold. 13,[23][24][25] Likewise, knowledge of the effect of crosslinking on the activity of cells seeded onto collagen scaffolds is incomplete.…”

Section: Introductionmentioning

confidence: 99%

Crosslinking and Mechanical Properties Significantly Influence Cell Attachment, Proliferation, and Migration Within Collagen Glycosaminoglycan Scaffolds

Haugh

Murphy

McKiernan

et al. 2011

Tissue Engineering Part A

280

269

View full text Add to dashboard Cite

show abstract

“…In the human sclera, homogeneous glyceraldehyde concentration in the sclera should be reached also, because it is significantly thinner than porcine sclera [25,26]. Interestingly, using a multilayer model of collagenous sheets Ruijgrok et al were able to demonstrate insufficient soaking with glutaraldehyde after 5 minutes exposure, leading to a shrinkage temperature profile within the multilayer sandwich and a difference in shrinkage temperature between inner and outer sheets of about 14°C [27].…”

Section: Discussionmentioning

confidence: 96%

Thermomechanical stability of sclera after glyceraldehyde crosslinking

Wollensak¹

2010

Graefes Arch Clin Exp Ophthalmol

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Scleral collagen crosslinking by glyceraldehyde proved very efficient in increasing the scleral thermomechanical stability by at least 10°C in Ts, stabilizing the eye shape and preventing the shrinkage of the eye in all dimensions. There is hope that, in a similar manner, glyceraldehyde crosslinking can stabilize the scleral collagen crosslinks and eye shape in myopia, stopping progression of scleral thinning and stretching.

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“…[8][9][10] Toward this end, various hydrogels with interfibrillar networks, such as fibrin and collagen gel, are being designed with controllable stiffness to examine cellular activities. [10][11][12][13] The stiffness of collagen hydrogels is typically controlled using short cross-linkers with bivalent or multivalent aldehyde groups; however, these methods are toxic to cells. [10][11] Therefore, it is common to first induce interconnected micropores into the hydrogel via lyophilization or porogen leaching, and subsequently incorporate cells into the pores.…”

Section: Introductionmentioning

confidence: 99%

“…[10][11][12][13] The stiffness of collagen hydrogels is typically controlled using short cross-linkers with bivalent or multivalent aldehyde groups; however, these methods are toxic to cells. [10][11] Therefore, it is common to first induce interconnected micropores into the hydrogel via lyophilization or porogen leaching, and subsequently incorporate cells into the pores. However, this approach may not precisely reflect the 3D microenvironment of cells in the original tissue.…”

Section: Introductionmentioning

confidence: 99%

Stiffness-Modulated Water Retention and Neovascularization of Dermal Fibroblast-Encapsulating Collagen Gel

Jeong

Jang

Cha

et al. 2013

Tissue Engineering Part A

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There is increasing evidence that matrix stiffness modulates various phenotypic activities of cells surrounded by a three-dimensional (3D) matrix. These findings suggest that matrix stiffness can also regulate dermal fibroblasts activities to remodel, repair, and recreate skin dermis, but this has not yet been systematically demonstrated to date. This study examines the effects of matrix rigidity on the morphology, growth rates, and glycosaminoglycan (GAG) production of dermal fibroblasts cultured in collagen-based hydrogels with controlled elastic moduli. The elastic moduli (E) of collagen hydrogels were increased from 0.7 to 1.6 and 2.2 kPa by chemically cross-linking collagen fibrils with poly(ethylene glycol) disuccinimidylester. Increasing E of the hydrogel led to decreases in cellular spreading, nuclear aspect ratio, and growth rate. In contrast, the cellular GAG production level was elevated by increasing E from 0.7 to 1.6 kPa. The larger accumulation of GAG in the stiffer hydrogel led to increased water retention during exposure to air, as confirmed with magnetic resonance imaging. Additionally, in a chicken chorioallantoic membrane, a cell-encapsulating hydrogel with E of 1.6 kPa created dermis-like tissue with larger amount of GAG and density of blood vessels, while a cell-hydrogel construct with E of 0.7 kPa generated scar-like tissue. Overall, the results of this study will be highly useful for designing advanced tissue engineering scaffolds that can enhance the quality of a wide array of regenerated tissues including skin.

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Glutaraldehyde crosslinking of collagen: Effects of time, temperature, concentration and presoaking as measured by shrinkage temperature

Cited by 27 publications

References 7 publications

Crosslinking and Mechanical Properties Significantly Influence Cell Attachment, Proliferation, and Migration Within Collagen Glycosaminoglycan Scaffolds

Crosslinking and Mechanical Properties Significantly Influence Cell Attachment, Proliferation, and Migration Within Collagen Glycosaminoglycan Scaffolds

Thermomechanical stability of sclera after glyceraldehyde crosslinking

Stiffness-Modulated Water Retention and Neovascularization of Dermal Fibroblast-Encapsulating Collagen Gel

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