Use of Shark Collagen for Cell Culture and Zymography

Nomura, Yasuya; Kitazume, Nobuhide

doi:10.1271/bbb.66.2673

Cited by 11 publications

(5 citation statements)

References 11 publications

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“…It has also been reported that shark collagen gel could be used as a cell-culture matrix, but cell culture was conducted at 30°C. The shark collagen gel melted at 37°C although its melting temperature was 39-41°C [15]. Therefore, this is the first report to show successful cell culture at 37°C on fish collagen gel to which no reagents were added to improve the thermal stability.…”

Section: Discussionmentioning

confidence: 88%

Characteristics of a self-assembled fibrillar gel prepared from red stingray collagen

et al. 2009

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A translucent collagen gel was formed from a transparent acidic solution of red stingray collagen by adjusting to physiological ionic strength and pH in phosphate buffer and then incubating at 25-37°C. During fibril formation from red stingray collagen, the turbidity increased when the NaCl concentration was increased at constant pH and the rate of fibril formation was accelerated by higher pH or lower NaCl concentration. The T m of red stingray collagen fibrillar gel was estimated as 44.3 ± 3.5°C, which was higher than that of the collagen solution, 33.2°C. In addition, red stingray collagen gel maintained its shape without melting and was suitable for culture of mouse stromal cells at 37°C.

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Section: Discussionmentioning

confidence: 88%

Characteristics of a self-assembled fibrillar gel prepared from red stingray collagen

et al. 2009

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“…Shark type I collagen forms fibrils under different conditions compared to bovine and porcine collagen [31]. For example, shark type I collagen gels and membranes have stronger rigidity and higher affinity to water vapour than those of porcine collagen, thus indicating the potential for utilising shark collagen as a new type I collagen material for various uses such as cell culture and medical technology [32].…”

Section: Collagen From Fishmentioning

confidence: 99%

Collagen: From Waste to Gold

Noorzai¹,

Verbeek²

2021

Biotechnological Applications of Biomass

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Industrial processing of bovine hides into leather results in many unusable hide off-cuttings, shavings and trimmings. This waste raw material is under-utilised and presents a waste valorisation opportunity to derive a high-value product such as collagen. Collagen is a highly sought-after protein which consists of three polypeptide chains, comprising 30% of the mammalian body’s protein, being the main component of skin, connective tissue and cartilage. The demand for collagen is rising at approximately 20% annually and global collagen-based biomaterials market is predicted to reach US$5 billion by 2025. This chapter presents a waste valorisation opportunity to extract collagen from waste bovine hide off-cuttings. Further, it discusses collagen extraction method optimization and methods used to investigate physicochemical properties of collagen are reviewed.

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“…To a sample of 3-5 mg of the cross-linked scaffold, 1 ml of 4% (w/v) NaHCO 3 solution (pH 8.5) and 1 ml of freshly prepared 0.5% (w/v) TNBS solution in distilled water was 9 added. After allowing the reaction to take place for 2 h at 40 ℃, 2 ml of 6 N HCl was added, and the temperature was raised to 60 ℃.…”

Section: Determination Of the Degree Of Cross-linkingmentioning

confidence: 99%

“…The structure and physicochemical characteristics of fish collagen have already been investigated (6, 7), but there had been very few studies on the potential for using fish collagen as biomaterials (9). In the present study, we used fish collagen from chum salmon skin, which was discarded as industrial waste, so as to make effective use of natural sources.…”

Section: Introductionmentioning

confidence: 99%

Application of cross-linked salmon atelocollagen to the scaffold of human periodontal ligament cells

Nagai

Yunoki

Suzuki

et al. 2004

Journal of Bioscience and Bioengineering

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The purpose of this study was to investigate the application of salmon atelocollagen (SAC) to a scaffold. SAC has a low denaturation temperature and needs to be cross-linked before being used as a scaffold. In the present study, SAC was cross-linked respectively. The proliferation rate of HPDL cells cultured in EDC-SAC was equivalent to that in EDC-BAC, and the ALP activity in EDC-SAC was found to be significantly higher than that in EDC-BAC. In the cross-linking by DHT, the cell proliferation rate and the ALP activity in DHT-SAC were lower than those in DHT-BAC. DHT seemed to provide insufficient cross-linking, and DHT-SAC was found to be breakable and 2 contractile, resulting in less cell activity. In contrast, there was no difference in the thermal stability, porous structure, and cell proliferation rate between EDC-SAC and EDC-BAC. In addition, the collagen helix of EDC-SAC was found to be partially denatured, and this structure resulted in the enhancement of ALP activity of HPDL cells compared with that using EDC-BAC. In conclusion, our results indicate that EDC-SAC could be used as a scaffold for in vitro culture.3

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Use of Shark Collagen for Cell Culture and Zymography

Cited by 11 publications

References 11 publications

Characteristics of a self-assembled fibrillar gel prepared from red stingray collagen

Characteristics of a self-assembled fibrillar gel prepared from red stingray collagen

Collagen: From Waste to Gold

Application of cross-linked salmon atelocollagen to the scaffold of human periodontal ligament cells

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