From Tendon Injury to Collagen-based Tendon Regeneration: Overview and Recent Advances

Rieu, Clément; Picaut, Lise; Mosser, Gervaise; Trichet, Léa

doi:10.2174/1381612823666170516130515

Cited by 23 publications

(17 citation statements)

References 182 publications

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“…This source has high resemblance to human collagen. There are no allergenic limitations to its usage because it has been widely used as a tendon reinforcement [22,23], hernia repairment [24], and for skin and wound healing as a plastic and reconstructive surgery material [25].…”

Section: Introductionmentioning

confidence: 99%

Hydrolyzed Collagen—Sources and Applications

et al. 2019

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Hydrolyzed collagen (HC) is a group of peptides with low molecular weight (3–6 KDa) that can be obtained by enzymatic action in acid or alkaline media at a specific incubation temperature. HC can be extracted from different sources such as bovine or porcine. These sources have presented health limitations in the last years. Recently research has shown good properties of the HC found in skin, scale, and bones from marine sources. Type and source of extraction are the main factors that affect HC properties, such as molecular weight of the peptide chain, solubility, and functional activity. HC is widely used in several industries including food, pharmaceutical, cosmetic, biomedical, and leather industries. The present review presents the different types of HC, sources of extraction, and their applications as a biomaterial.

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Section: Introductionmentioning

confidence: 99%

Hydrolyzed Collagen—Sources and Applications

et al. 2019

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“…1,2 In a recent review by Rieu et al, a plethora of studies are highlighted for demonstrating that COL can be independently guided (i.e., in the absence of other biological molecules) into highly organized structures in vitro. 3 However, many of these approaches achieve fibrillar, anisotropic constructs by operating in a parameter space which largely deviates from the physiological environment. [4][5][6][7][8] We suspect that the need for extreme processing conditions stems from the absence of the associated molecular milieu (e.g., proteoglycans, proteins, glycoproteins, and enzymes) that is normally present during development.…”

Section: Introductionmentioning

confidence: 99%

Molecular Interactions between Collagen and Fibronectin: A Reciprocal Relationship that Regulates De Novo Fibrillogenesis

Paten

Martin

Wanis

et al. 2019

Chem

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Determining the fundamental mechanisms underlying tissue formation and wound healing allows for bio-inspired approaches that leverage the best practices of biology, as decided upon by millions of years of evolution. To gain insight into how tissue is built, we have studied the interactions between two of the principal proteins found in connective tissues: collagen and fibronectin. We have confirmed a binding affinity in solution, which supports a reciprocal relationship whereby the assembly pathway of one catalyzes the other. The molecular synergy enables complex extracellular matrix formation with a range of mechanical properties.

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“…In sharp contrast, collagen, another gold standard material in tissue engineering, has been extensively studied 24 . The simplicity of collagen self-assembly, induced by neutralization or 37°C heat activation, makes it favorable for multiple shaping techniques, such as molding or extrusion 25 . To investigate if similar processes could be used to trigger fibrin polymerization and thus widen the possibilities in fibrin shaping, we thus focused on fibrinogen and fibrin solutions at acidic pH.…”

Section: Introductionmentioning

confidence: 99%

Thrombin-free polymerization leads to pure fibrin(ogen) materials with extended processing capacity

Rieu¹,

Mosser²,

Haye³

et al. 2020

Preprint

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Fibrin is a key protein for various clinical applications such as tissue reconstruction. However, in contrast to type I collagen, fibrin shaping has so far faced major limitations related to the necessity to add thrombin enzyme to fibrinogen precursors to induce fibrin self-assembly. Here we report a thrombin-free gelation pathway of fibrinogen solutions by incubation at 37°C in mild acidic conditions. We unravel the biochemical mechanisms underlying the gelation process and draw comparison between fibrinogen and fibrin at both molecular and supramolecular levels in these conditions. The protocol enables to control the viscosity of fibrin(ogen) solutions, and to induce fibrin(ogen) gel formation by simple 37°C incubation, with a reinforcement effect at neutralization. It facilitates processing of fibrin(ogen) materials, for coating, molding and extrusion, and offers new possibilities such as 3D printing. This approach is further compatible with type I collagen processing and can provide advanced tissue engineering scaffolds with high bioactivity.

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From Tendon Injury to Collagen-based Tendon Regeneration: Overview and Recent Advances

Cited by 23 publications

References 182 publications

Hydrolyzed Collagen—Sources and Applications

Hydrolyzed Collagen—Sources and Applications

Molecular Interactions between Collagen and Fibronectin: A Reciprocal Relationship that Regulates De Novo Fibrillogenesis

Thrombin-free polymerization leads to pure fibrin(ogen) materials with extended processing capacity

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