Structural Property and<i>in Vitro</i>Self-assembly of Shark Type I Collagen

Nomura, Yasuya; Yamano, Masaya; Hayakawa, Chikayuki; Ishii, Yasuhiro; Shirai, Kunio

doi:10.1271/bbb.61.1919

Cited by 41 publications

(34 citation statements)

References 5 publications

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“…Meli et al 31 monitored collagen I under physiological conditions in vitro during an 8-week incubation period and reported changes in solubility and glycoxidated products. Nomura et al 32 demonstrated differences between shark and porcine collagen for the optimum temperature and pH to form self-assembly aggregates. However, we found data about the pH curves in collagen I/III for neither DMEM nor MesenCult ™ or 0.9% NaCl in the literature.…”

Section: Tricalcium Phosphates (Vitossmentioning

confidence: 99%

Extensive H⁺release by bone substitutes affects biocompatibilityin vitrotesting

Jäger

Fischer

Schultheis

et al. 2005

J Biomedical Materials Res

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Bone substitutes are widespread in orthopedic and trauma surgery to restore critical bony defects and/or promote local bone healing. Cell culture systems have been used for many years to screen biomaterials for their toxicity and biocompatibility. This study applies a human bone marrow cell culture system to evaluate the toxic in vitro effects of soluble components of different bone substitutes, which are already in clinical use. Different specimens of tricalcium phosphates (TCP) (Vitoss, Cerasorb), nondecalcified bovine bone (Lubboc), demineralized human bone matrices (DBM) (Grafton Flex/Putty), and collagen I/III matrix (ACI-Maix) were tested in Dulbecco's modified Eagle's medium (DMEM) and MesenCult culture solution and compared with a biomaterial-free cell culture. Biocompatibility parameters were cell viability evaluated by phase-contrast microscopy and laser flow cytometry, morphology, and the local H(+) release by bone substitutes. There were significant differences (p < 0.05) between the tested biomaterials and culture solutions. Collagen I/III, non-demineralized bovine bone, and TCP materials showed advantages for cell survival over other tested biomaterials (average values of vital cells/mL MesenCult/DMEM: Collagen I/III: 1090/1083; Vitoss: 893/483; Cerasorb: 471/523; Lubboc: 815/410; Grafton Putty: 61/44; Grafton Flex: 149/57). Especially the DBM materials lead to a significant decrease of pH, which is considered to be a major factor for cell death. DMEM culture solution supports cell survival for those bone substitutes that induce an alkaline reaction, whereas MesenCult media promotes cell vitality in biomaterials, which leads to an acidification of culture solution.

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Section: Tricalcium Phosphates (Vitossmentioning

confidence: 99%

Extensive H⁺release by bone substitutes affects biocompatibilityin vitrotesting

Jäger

Fischer

Schultheis

et al. 2005

J Biomedical Materials Res

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“…Among the Chondrichthyes-which includes sharks, skates, and rays-there are some studies reporting data on properties of type I collagen (Yoshimura et al, 2000;Nomura et al, 1997). As far as we know, this is the first study about skin collagen from these species, such as rabbit fish (Chimera monstrosa) or small-spotted catshark (S. canicula).…”

Section: Introductionmentioning

confidence: 96%

Characterization of Collagen from Different Discarded Fish Species of the West Coast of the Iberian Peninsula

Sotelo

Comesaña

Ariza

et al. 2015

Journal of Aquatic Food Product Technology

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Skin collagen of six discarded fish species was analyzed and compared. Acid soluble collagen (ASC) was extracted; a characteristic sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) profile for type I collagen was obtained, except for Chimaera mostrosa. Contents of collagen calculated from HPro (31.85% average) were higher than those determined from ASC extracts (17.75% average), with Galeus spp. being the species with the higher percentage. Amino acid analysis revealed the typical composition of collagen, with very few differences among species. Specific profiles were obtained after protease digestion. Denaturation temperature of ASC correlated well with imino and hydroxyproline contents.Results demonstrate the feasibility of using the obtained collagens in different industrial applications.

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“…However, there are likely to be some diŠerences in the detailed molecular structure between the collagen from both origins; especially since shark type I collagen formsˆbrils under diŠerent conditions from those of pig type I collagen. 7) Such a diŠerence inˆbrilogenesis is likely to in‰uence the physicochemical properties of collagen gel and membrane. Shark collagen gel and membrane are more rigid and have a higher a‹nity for water vapor than those of pig collagen, and these results have suggested that shark collagen could be a new type I collagen material for various uses.…”

mentioning

confidence: 99%

“…7) Fibroblasts were prepared from fetal rat back skin, and cultured according to the method of Ham. 14) Thê broblasts were grown and maintained in Dulbecco's modiˆed Eagle's medium (DMEM from Gibco BRL) containing 10z fetal calf serum (FBS from EquitechBio), 10 mM NaHCO3, 20 mM HEPES, 50 units W ml penicillin, 50 mg W ml streptomycin, and 100 mg W ml neomycin in a moist atmosphere composed of 5z CO2 W 95z air at 379 C. The population doubling level of the cells used in this study was withinˆve passages.…”

mentioning

confidence: 99%

“…7) To prepare the matrix for cell culture, collagen was dissolved in 5 mM acetic acid at 49 C. After centrifuging at 100,000×g for 1 h and adjustment of the collagen concentration to 0.3z, the collagen solution was mixed with DMEM at twice this concentration containing 20z FCS in culture dishes (48 wells), and then warmed to 309 C to form a gel matrix. This temperature was used as the upper limit to avoid gelatinization of the shark collagen.…”

mentioning

confidence: 99%

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Use of Shark Collagen for Cell Culture and Zymography

Nomura

Kitazume

2002

Bioscience, Biotechnology, and Biochemistry

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The uses of shark collagen as a matrix for cell culture and as a substrate for zymography were investigated. Fibroblasts were cultured on a gel matrix of shark type I collagen at 309 C. The collagen gel had contracted by 4 days of incubation. Individualˆbroblasts were visible against the transparent background of the contracted collagen as long, lean star-shaped cells. The matrix metalloproteinases (MMPs) fromˆbroblasts secreted from the medium more easily digested shark gelatin than pig gelatin. MMP-2, -9, and that of potential form were recognizable in the zymographic gel of shark gelatin.

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Structural Property andin VitroSelf-assembly of Shark Type I Collagen

Cited by 41 publications

References 5 publications

Extensive H⁺release by bone substitutes affects biocompatibilityin vitrotesting

Extensive H⁺release by bone substitutes affects biocompatibilityin vitrotesting

Characterization of Collagen from Different Discarded Fish Species of the West Coast of the Iberian Peninsula

Use of Shark Collagen for Cell Culture and Zymography

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Structural Property andin VitroSelf-assembly of Shark Type I Collagen

Cited by 41 publications

References 5 publications

Extensive H+release by bone substitutes affects biocompatibilityin vitrotesting

Extensive H+release by bone substitutes affects biocompatibilityin vitrotesting

Characterization of Collagen from Different Discarded Fish Species of the West Coast of the Iberian Peninsula

Use of Shark Collagen for Cell Culture and Zymography

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Extensive H⁺release by bone substitutes affects biocompatibilityin vitrotesting

Extensive H⁺release by bone substitutes affects biocompatibilityin vitrotesting