Renaturation of α1 Chains from Shark Skin Collagen Type 1

Nomura, Yasuya; Yamano, Masaya; Shirai, Kunio

doi:10.1111/j.1365-2621.1995.tb04563.x

Cited by 31 publications

(16 citation statements)

References 11 publications

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“…The Td of shark collagen solution is approximately 30°C [37], which results in the dissolution of the fibrillar gel of this collagen at 37°C [35]. Such features indicate that the gel cannot be used at the actual physical temperature required for human medical application.…”

Section: Characteristics Of Fish Collagenmentioning

confidence: 99%

Potency of Fish Collagen as a Scaffold for Regenerative Medicine

Yamada

Yamamoto

Ikeda

et al. 2014

BioMed Research International

165

114

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Cells, growth factors, and scaffold are the crucial factors for tissue engineering. Recently, scaffolds consisting of natural polymers, such as collagen and gelatin, bioabsorbable synthetic polymers, such as polylactic acid and polyglycolic acid, and inorganic materials, such as hydroxyapatite, as well as composite materials have been rapidly developed. In particular, collagen is the most promising material for tissue engineering due to its biocompatibility and biodegradability. Collagen contains specific cell adhesion domains, including the arginine-glycine-aspartic acid (RGD) motif. After the integrin receptor on the cell surface binds to the RGD motif on the collagen molecule, cell adhesion is actively induced. This interaction contributes to the promotion of cell growth and differentiation and the regulation of various cell functions. However, it is difficult to use a pure collagen scaffold as a tissue engineering material due to its low mechanical strength. In order to make up for this disadvantage, collagen scaffolds are often modified using a cross-linker, such as gamma irradiation and carbodiimide. Taking into account the possibility of zoonosis, a variety of recent reports have been documented using fish collagen scaffolds. We herein review the potency of fish collagen scaffolds as well as associated problems to be addressed for use in regenerative medicine.

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Section: Characteristics Of Fish Collagenmentioning

confidence: 99%

Potency of Fish Collagen as a Scaffold for Regenerative Medicine

Yamada

Yamamoto

Ikeda

et al. 2014

BioMed Research International

165

114

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“…9,21,22 Type I collagen has been found as the major collagen in the skin, bone and fins of various fish species. 2,3,9,23,24 Recently, collagen subunits from shark skin and sea cucumber 25,26 have been characterized. Nevertheless, collagen from different species and habitats might be different in terms of molecular composition and properties.…”

Section: Introductionmentioning

confidence: 99%

Isolation and characterization of collagen from bigeye snapper (Priacanthus macracanthus) skin

et al. 2005

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Acid-solubilized collagen (ASC) and pepsin-solubilized collagen (PSC) were isolated from the skin of bigeye snapper (Priacanthus macracanthus) with yields of 64 and 11 g kg −1 wet weight, respectively. Both ASC and PSC were characterized as type I collagens with no disulfide bonds. Peptide maps of ASC and PSC digested by V8 protease and lysyl endopeptidase showed some differences in peptide patterns and were totally different from those of calf skin collagen. The maximum solubility was observed at pH 4 and 5 for ASC and PSC, respectively. A sharp decrease in solubility of both collagens in acetic acid was found with NaCl concentration above 30 g l −1 . Thermal transitions of ASC and PSC in deionized water were observed with T max of 30.37 and 30.87 • C, respectively, and were lowered in the presence of acetic acid (0.05 mol kg −1 solution). Therefore, ASC was a major fraction in bigeye snapper skin and it exhibited some different characteristics to PSC.

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“…However the shark skin collagen is also potentially an important biomaterial as suggested by the earlier reports. 13) Type I collagen is characteristic in its fibril forming ability. In vitro, the self-assembly of type I collagen molecules takes place when the collagen solution is adjusted to physiological pI-I.…”

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confidence: 99%