• Fisheries and Aquatic Sciences
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• 제21권4호
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• pp.7.1-7.8
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• 2018

In this study, we isolated and characterized the acid-soluble skin collagen of Pacific bluefin tuna (PBT, Thunnus orientalis). The PBT skin collagen was composed of two ${\alpha}$ chains (${\alpha}1$ and ${\alpha}2$) and one ${\beta}$ chain. The denaturation temperature of PBT collagen was low although it was rich in proline and hydroxyproline. The primary structure of PBT skin collagen was almost identical to that of calf and salmon skin collagen; however, it differed with respect to the epitope recognition of the antibody against salmon type I collagen. These results suggest that the primary structure of skin collagen was highly conserved among animal species, although partial sequences that included the epitope structure differed among collagens.

• Macromolecular Research
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• 제15권3호
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• pp.205-210
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• 2007

Collagen is the major structural protein of connective tissues. It can be used as a prosthetic biomaterial applicable to artificial skin, tendon, ligaments, and collagen implants. The objective of this study is to investigate the possibility of realizing wound dressing medical products by the synthesis of composite materials with collagen and a biodegradable polymer, PLLA, via a surface modification process. Type I collagen was obtained from pig skin by a separation process. The structural characteristics of the extracted collagen were confirmed by SDS-polyacrylamide (PAcr) gel electrophoresis (PAGE) and FTIR. Also, PLLA-g-PAcr was synthesized by the radical polymerization of acrylamide initiated by AIBN in the presence of PLLA. The surface of PLLA was modified by the presence of the acrylamide residues. The structural characteristics of the copolymer were analyzed by FTIR, $^1H-NMR$ and contact angle measurements. The water uptake and WVTR of the collagen/PLLA-g-PAcr composite tended to increase with increasing collagen concentration and with decreasing EDC concentration.

• Journal of Periodontal and Implant Science
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• 제29권2호
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• pp.355-373
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• 1999

Many researches have been reported that collagen as cellular stroma, matrix of grafting materials, mediator of agents for the purpose of promoting healing process invivo, but the responses in vivo were seen various. The goal of this experiment is to assess the effect of collagen on bony healing, through histological evaluation of implanted collagen on the calvarial defect in rats. 2-month-old Sprague-Dawley, 24 rats were used and 12 rats assigned to each group of control and test. Defect of 5mm in diameter was made on the calvarial bone with trephine bur. Following thorough saline rinse, defect of control group was left in empty and that of experimental group was filled with fibrillar collagen($COLLATAPE^{(R)}$, COLLA-TEC. INC. U.S.A.) soaked in saline. 3 rats in each group were sacrificed at 3, 7, 14, 21 days after operation respectively, and the tissue blocks were prepared for light microscope with H-E for evaluation of overall healing, with TRAP(tartrate resistant acid phosphatase) for evaluation of osteoclastic activity and with immunohistochemical staining for macrophages. The results were as follows : 1. In the control group, inflammatory responses were disappeared at day 14, but, in the experimental group inflammatory infiltrates were reduced at day 21. Thus, the experimental group showed more severe soft tissue inflammation than control group. 2. Both control and experimental group showed slight appositional growth at day 7 and gradual bony growth to 21th day. But, complete bony healing of the defect was not shown. There was no significant difference in bony healing between control and experimental group 3. Specific response of macrophages for implanted collagen was observed at day 14 in the experimental group. In conclusion, although fibrillar collagen caused inflammation of soft tissue during initial healing period, inflammatory responses by fibrillar collagen didn't inhibit bony regeneration and implanted collagen was biodegradaded by macrophages. Thus, we expect that fibrillar collagen can be used for useful mediator of graft materials or growth factors.

• 유기물자원화
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• 제6권1호
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• pp.43-52
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• 1998

본 연구는 피혁 폐기물로부터 크롬 이온을 분리한 상태로 Collagen을 추출할 수 있는 최적 조건에 관한 것이다. Collagen 추출에 있어 온도, pH, 그리고 알칼리 용액 농도의 영향을 실험했다. 실험결과 점도측정에 의해 초기 변성온도는 $25^{\circ}C$, 완전 변성온도는 $31.5^{\circ}C$였다. Collagen 추출의 최적조건은 가용화 온도 $15^{\circ}C{\sim}20^{\circ}C$, pH 1.5, 알칼리 용액 3%였다. PH 1.5에서 크롬 이온이 거의 분리되었다. 탄닌 폐기물로부터 크롬 이온의 분리효율은 99.5% 이상이었다. 피혁 폐기물로부터 조단백질의 추출율은 89.%이었다. 추출된 조단백질내에 hydroxyprolne과 collagen의 함량은 각각 8.53%, 63.62%였다.

• Restorative Dentistry and Endodontics
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• 제29권4호
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• pp.370-377
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• 2004

The purpose of this study was to regenerate human dental pulp tissues similar to native pulp tissues. Using the mixture of type I collagen solution, primary cells collected from the different tissues (pulp, gingiva, and skin) and NIH 3T3 ($1{\;}{\times}{\;}10^5{\;}cells/ml/well$) were cultured at 12-well plate at $37^{\circ}C$ for 14 days. Standardized photographs were taken with digital camera during 14 days and the diameter of the contracted collagen gel matrix was measured and statistically analyzed with student t-test. As one of the pulp tissue engineering, normal human dental pulp tissue and collagen gel matrix cultured with dental pulp cells for 14 days were fixed and stained with Hematoxyline & Eosin. According to this study, the results were as follows: 1. The contraction of collagen gel matrix cultured with pulp cells for 14 days was significantly higher than other fibroblasts (gingiva, skin) (p < 0.05), 2. The diameter of collagen gel matrix cultured with pulp cells was reduced to 70.4% after 7 days, and 57.1% after 14 days. 3. The collagen gel without any cells did not contract, whereas the collagen gel cultured with gingiva and skin showed mild contraction after 14 days (88.1% and 87.6% respectively). 4. The contraction of the collagen gel cultured with NIH 3T3 cells after 14 days was higher than those cultured with gingival and skin fibroblasts, but it was not statistically significant (72.1%, p > 0.05). 5. The collagen gel matrix cultured with pulp cells for 14 days showed similar shape with native pulp tissue without blood vessels. This approach may provide a means of engineering a variety of other oral tissue as well and these cell behaviors may provide information needed to establish pulp tissue engineering protocols.

• Journal of Periodontal and Implant Science
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• 제49권2호
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• pp.90-104
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• 2019

Purpose: The aim of this study was to evaluate clinical and radiographic changes and the survival rate after periodontal surgery using deproteinized bovine bone mineral (DBBM) with 10% collagen or DBBM with a collagen membrane in endo-periodontal lesions. Methods: A total of 52 cases (41 patients) with at least 5 years of follow-up were included in this study. After scaling and root planing with or without endodontic treatment, periodontal regenerative procedures with DBBM with 10% collagen alone or DBBM with a collagen membrane were performed, yielding the DBBM + 10% collagen and DBBM + collagen membrane groups, respectively. Changes in clinical parameters including the plaque index, bleeding on probing, probing pocket depth, gingival recession, relative clinical attachment level, mobility, and radiographic bone gains were evaluated immediately before periodontal surgical procedures and at a 12-month follow-up. Results: At the 12-month follow-up after regenerative procedures, improvements in clinical parameters and radiographic bone gains were observed in both treatment groups. The DBBM + 10% collagen group showed greater probing pocket depth reduction ($4.52{\pm}1.06mm$) than the DBBM + collagen membrane group ($4.04{\pm}0.82mm$). However, there were no significant differences between the groups. Additionally, the radiographic bone gain in the DBBM + 10% collagen group ($5.15{\pm}1.54mm$) was comparable to that of the DBBM + collagen membrane group ($5.35{\pm}1.84mm$). The 5-year survival rate of the teeth with endo-periodontal lesions after periodontal regenerative procedures was 92.31%. Conclusions: This study showed that regenerative procedures using DBBM with 10% collagen alone improved the clinical attachment level and radiographic bone level in endo-periodontal lesions. Successful maintenance of the results after regenerative procedures in endo-periodontal lesions can be obtained by repeated oral hygiene education within strict supportive periodontal treatment.

• Clinical Nutrition Research
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• 제12권4호
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• pp.245-256
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• 2023

A randomized, double-blind, placebo-controlled trial was conducted to confirm whether collagen peptide supplementation for 12 week has a beneficial effect on body fat control in older adults at a daily physical activity level. Participants were assigned to either the collagen group (15 g/day of collagen peptide) or the placebo group (placebo drink). Body composition was measured by bioelectrical impedance analysis (BIA) and dual-energy X-ray absorptiometry (DEXA). In total, 74 participants (collagen group, n = 37; placebo group, n = 37) were included in the final analysis. The collagen group showed a significant reduction in total body fat mass compared with the placebo group, as evidenced by both BIA (p = 0.021) and DEXA (p = 0.041) measurements. Body fat mass and percent body fat of the whole body and trunk reduced at 12 weeks compared with baseline only in the collagen group (whole body: body fat mass, p = 0.002; percent body fat, p = 0.002; trunk: body fat mass, p = 0.001; percent body fat, p = 0.000). Total fat mass change (%) (collagen group, -0.49 ± 3.39; placebo group, 2.23 ± 4.20) showed a significant difference between the two groups (p = 0.041). Physical activity, dietary intake, and biochemical parameters showed no significant difference between the groups. The results confirmed that collagen peptide supplementation had a beneficial effect on body fat reduction in older adults aged ≥ 50 years with daily physical activity level. Thus, collagen peptide supplementation has a positive effect on age-related changes.

• KSBB Journal
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• 제7권4호
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• pp.271-277
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• 1992

쥐 간세포를collagenase perfusion method에 의해 분리한 뒤 collagen coated dish와floating collagen membrane에서 일차배양하여 간세포의 분화기능을 조사하였다. 두 경우 모두 간세포의 생존율은 5일 이후부터 점차 감소하였거나 간세포에 의한 암모니아 처리기능과 albumin생성기능은 약 7일간 유지되었다. 또 이러한 분화기능에 유지는 ollagen coated dish보다floating collagen membrane이 유리한 것으로 나타났다.

• Asian-Australasian Journal of Animal Sciences
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• 제4권4호
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• pp.407-410
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• 1991

The relationship between the possible structural change due to chemical modifications and functionality changes was studied in pigskin collagen. Amino groups in collagen were modified by succinylation and reductive alkylation. Carboxyl groups were modified using carbodiimide. Thermal denaturation temperature of collagen increased remarkably by carboxyl groups modification whereas decreased by succinylation and reductive alkylation. Emulsifying capacity was improved by reductive alkylation and carboxyl groups modification while emulsion stability was improved by succinylation. Chemical modifications increased solubility whereas decreased the foaming capacity of collagen. Viscosity of collagen at various pH varied with methods of modification.

• 한국식품위생안전성학회지
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• 제14권1호
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• pp.45-54
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• 1999

The purpose of this study was to examine the increased bone loss caused by ovariectomy through monitoring the concentrations of the collagen and the pyridinoline crosslinks of collagen. The ovariectomized rats treated for 8 weeks, were divided at random into two or three groups of 10. Ovariectomies were carried out from the saline-treated group (Ovx), the estrogentreated group (Ovx+ES) and chondroitin sulfate-treated group (Ovx+CS). Sham operations were performed on the sham-operated group (Sham). Ovx+ES and Ovx+CS groups showed the remarkably increased collagen and pyridinoline amount in the bone and cartilage compared to Ovx group. And as the result of the measurement of SOD, Catalase and GPx which are antioxidant enzyme, SOD and Catalase activities in Ovx group were much higher than in Sham group. But they were significantly decreased in Ovx+CS group. Based on these results, it is supposed that estrogen and condroitin sulfate can enhance collagen synthesis and affect the pyridinoline formation in collagen fibrils through stimulating lysyl oxidase activity. And it is also thought that chondroitin sulfate can inhibit aging by reducing antioxidant enzyme.