“…Similar to hDF cultures, basic cellular function analysis using hTC morphology, proliferation metabolic activity, and viability revealed no apparent differences between the skin‐ and tendon‐derived collagen scaffolds and, again, the 1 mM 4SG‐PEG did not induce any cytotoxicity. This directly aligns with previous publications, where 4SG‐PEG has shown acceptable levels of cytocompatibility (e.g., collagen type I hydrogels, 76 films 24,58 and fibers 25,77 and collagen type II hydrogels 44 and sponges 42,78 ).…”
Section: Discussionsupporting
confidence: 91%
“…Similar to hDF cultures, basic cellular function analysis using hTC morphology, proliferation metabolic activity, and viability revealed no apparent differences between the skin-and tendon-derived collagen scaffolds and, again, the 1 mM 4SG-PEG did not induce any cytotoxicity. This directly aligns with previous publications, where 4SG-PEG has shown acceptable levels of cytocompatibility (e.g., collagen type I hydrogels, 76 films 24,58 and fibers 25,77 and collagen type II hydrogels 44 and sponges 42,78 ). Immunocytochemistry analysis (the function of each molecule assessed is provided inTable S2) made apparent that at Day 14 (the longest time point assessed), the 0 mM 4SG-PEG skin-derived collagen scaffolds significantly increased (over the tendon-derived collagen scaffolds) the synthesis of collagen type IV, collagen type V, collagen type VI and fibronectin.…”
Section: Biological Response Assessment Using Htcssupporting
Recent data suggest that collagen retains the memory of the tissue that it derives from. With this in mind, collagen (from bovine skin and tendon) sponges were fabricated with different crosslinking densities, and their physicochemical and biological properties were assessed. As the crosslinking density was increased, the resistance to collagenase digestion, denaturation temperature, compressive stress, and compressive modulus was significantly increased and the free amine content, % swelling, and human dermal fibroblast cytocompatibility were significantly reduced. The tendon‐collagen‐derived scaffolds exhibited significantly higher compressive stress and compressive modulus values and induced significantly higher human tenocyte DNA concentration and metabolic activity than the skin‐collagen‐derived scaffolds. In human tenocyte cultures on day 14, the 1 mM 4‐arm polyethylene‐glycol succinimidyl glutarate tendon‐collagen‐derived collagen sponges induced significantly higher collagen type III synthesis (as expected at early stages of physiological tendon healing) and downregulated actin alpha 2 (associated with myofibroblast differentiation) and the skin‐collagen‐derived collagen sponges induced significantly higher collagen type IV synthesis (found primarily at the dermal‐epidermal junction) and upregulated prolyl 4‐hydroxylase subunit alpha‐1 (associated with collagen biosynthesis and constitutes a target for antifibrotic compounds). Our data indicate that the tissue from which collagen is extracted should be considered in the development of medical devices.
“…Similar to hDF cultures, basic cellular function analysis using hTC morphology, proliferation metabolic activity, and viability revealed no apparent differences between the skin‐ and tendon‐derived collagen scaffolds and, again, the 1 mM 4SG‐PEG did not induce any cytotoxicity. This directly aligns with previous publications, where 4SG‐PEG has shown acceptable levels of cytocompatibility (e.g., collagen type I hydrogels, 76 films 24,58 and fibers 25,77 and collagen type II hydrogels 44 and sponges 42,78 ).…”
Section: Discussionsupporting
confidence: 91%
“…Similar to hDF cultures, basic cellular function analysis using hTC morphology, proliferation metabolic activity, and viability revealed no apparent differences between the skin-and tendon-derived collagen scaffolds and, again, the 1 mM 4SG-PEG did not induce any cytotoxicity. This directly aligns with previous publications, where 4SG-PEG has shown acceptable levels of cytocompatibility (e.g., collagen type I hydrogels, 76 films 24,58 and fibers 25,77 and collagen type II hydrogels 44 and sponges 42,78 ). Immunocytochemistry analysis (the function of each molecule assessed is provided inTable S2) made apparent that at Day 14 (the longest time point assessed), the 0 mM 4SG-PEG skin-derived collagen scaffolds significantly increased (over the tendon-derived collagen scaffolds) the synthesis of collagen type IV, collagen type V, collagen type VI and fibronectin.…”
Section: Biological Response Assessment Using Htcssupporting
Recent data suggest that collagen retains the memory of the tissue that it derives from. With this in mind, collagen (from bovine skin and tendon) sponges were fabricated with different crosslinking densities, and their physicochemical and biological properties were assessed. As the crosslinking density was increased, the resistance to collagenase digestion, denaturation temperature, compressive stress, and compressive modulus was significantly increased and the free amine content, % swelling, and human dermal fibroblast cytocompatibility were significantly reduced. The tendon‐collagen‐derived scaffolds exhibited significantly higher compressive stress and compressive modulus values and induced significantly higher human tenocyte DNA concentration and metabolic activity than the skin‐collagen‐derived scaffolds. In human tenocyte cultures on day 14, the 1 mM 4‐arm polyethylene‐glycol succinimidyl glutarate tendon‐collagen‐derived collagen sponges induced significantly higher collagen type III synthesis (as expected at early stages of physiological tendon healing) and downregulated actin alpha 2 (associated with myofibroblast differentiation) and the skin‐collagen‐derived collagen sponges induced significantly higher collagen type IV synthesis (found primarily at the dermal‐epidermal junction) and upregulated prolyl 4‐hydroxylase subunit alpha‐1 (associated with collagen biosynthesis and constitutes a target for antifibrotic compounds). Our data indicate that the tissue from which collagen is extracted should be considered in the development of medical devices.
“…Thus, the application of articular cartilage tissue engineering to repair, regenerate, and improve injured articular cartilage needs to be studied further [ 54 ]. Cartilage is primarily composed of collagen type II; thus, the use of collagen type II scaffolds has been advocated in cartilage engineering approaches [ 183 ].…”
Section: Tissue Engineering and Regenerative Medicinesmentioning
Aquatic-based collagens have attracted much interest due to their great potential application for biomedical sectors, including the tissue engineering sector, as a major component of the extracellular matrix in humans. Their physical and biochemical characteristics offer advantages over mammalian-based collagen; for example, they have excellent biocompatibility and biodegradability, are easy to extract, and pose a relatively low immunological risk to mammalian products. The utilization of aquatic-based collagen also has fewer religious restrictions and lower production costs. Aquatic-based collagen also creates high-added value and good environmental sustainability by aquatic waste utilization. Thus, this study aims to overview aquatic collagen’s characteristics, extraction, and fabrication. It also highlights its potential application for tissue engineering and the regeneration of bone, cartilage, dental, skin, and vascular tissue. Moreover, this review highlights the recent research in aquatic collagen, future prospects, and challenges for it as an alternative biomaterial for tissue engineering and regenerative medicines.
“…With respect to marine species, squid [134] , jellyfish [ 135 , 136 ], amur sturgeon [137] , hoki [138] and chondrichthyes (e.g. sharks [139] , [140] , [141] , skates [142] , rays [143] ), a diverse group of cartilaginous fish that lack true bone and exhibit a skeleton solely comprised of unmineralized cartilage, have been used for collagen type II extraction. In general, high yield, pure collagen type II preparations are produced by acid solubilisation, pepsin digestion and repeated salt precipitation / acid solubilisation and finally dialysis methods ( Fig.…”
Section: Collagen Type II Biosynthesis Extraction and Synthesis Via R...mentioning
confidence: 99%
“… Fig. 2 Collagen type II extraction flow chart from cartilage tissues (the detailed protocol can be found here [ 131 , 143 ]) and electrophoretic mobility of collagen type I and collagen type II (the detailed protocol can be found here [223] ). Notes: As the same protocol is used to extract collagen type I [224] , [225] , [226] , attention should be paid during dissection to remove all not cartilaginous tissues.…”
Section: Collagen Type II Biosynthesis Extraction and Synthesis Via R...mentioning
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