• 한국축산식품학회지
• /
• 제37권3호
• /
• pp.392-401
• /
• 2017

Variations in physical toughness between muscles and animals are a function of growth rate and extend of collagen type I and III. The current study was designed to investigate the ability of growth rate, collagen concentration, collagen synthesizing and degrading genes on two different fibroblast cells derived from Hanwoo m. longissimus dorsi (LD) and semimembranosus (SM) muscles. Fibroblast cell survival time was determined for understanding about the characteristics of proliferation rate between the two fibroblasts. We examined the collagen concentration and protein expression of collagen type I and III between the two fibroblasts. The mRNA expression of collagen synthesis and collagen degrading genes to elucidate the molecular mechanisms on toughness and tenderness through collagen production between the two fibroblast cells. From our results the growth rate, collagen content and protein expression of collagen type I and III were significantly higher in SM than LD muscle fibroblast. The mRNA expressions of collagen synthesized genes were increased whereas the collagen degrading genes were decreased in SM than LD muscle. Results from confocal microscopical investigation showed increased fluorescence of collagen type I and III appearing stronger in SM than LD muscle fibroblast. These results implied that the locomotion muscle had higher fibroblast growth rate, leads to produce more collagen, and cause tougher than positional muscle. This in vitro study mirrored that background toughness of various muscles in live animal is likely associated with fibroblast growth pattern, collagen synthesis and its gene expression.

• 한국식품영양과학회지
• /
• 제24권3호
• /
• pp.446-453
• /
• 1995

The improtant components of extracellular matrix(ECM) are collagen and chondroitin sulfate. The hydrophobic surface of collagen is one of the determining factors of diameter of collagen fiber and also is closely related to the aging phenomena. The controlling mechanism of the diameter of collagen fiber influenced by the interaction with chondroitin sulfate was evaluated using bis-ANS as a hydrophobic probe. Hydrophobic surface area of collagen molecule shielded by chondroitin sulfate was evaluated. Relative fluorescence intensity of collagen in thepresence of chondroitin sulfate was measured using bis-ANS as a hydrophobic probe. The fluorescence intensity decreased with the increase in chondroitin sulfate up to 3.8 chondroitin sulfate/collagen(mole/mole). Further increase in the ratio of chondroitin sulfate to collagen did not change the fluorescence intensity. Similar changes in the relative fluorescence intensity were observed for both rat tail and lathyrific rat skin collagen. The fluorescence intensity indicated by the binding between bis-ANS and hydrophobic sites of collagen was pH dependent, and the shielding effect of collagen-chondroitin sulfate interaction could not be detected at pH above 6.0. This is probably due to the charge repulsions caused by negative charged collagen molecules at higher pH.

• 한국축산식품학회지
• /
• 제39권2호
• /
• pp.345-353
• /
• 2019

Various commercial collagen mixtures aimed at improving the quality of meat products are available, but the optimal composition is unclear. This study aimed to compare the functional properties, including physicochemical characteristics and lipid oxidative stability, of loin ham marinated with three commercial collagen mixtures sold as food additives. The addition of collagen mixtures led to significant increases in the moisture content, water holding capacity (WHC), cooking yield, and instrumental tenderness, regardless of the type of collagen mixture. In particular, meat samples containing collagen mixture C showed the highest (p<0.05) WHC and tenderness among all groups. Furthermore, collagen mixture B induced increases (p<0.05) in pH values in both raw and cooked samples. The $a^*$ values of samples with collagen mixtures were lower (p<0.05) than those of samples without collagen mixtures. All collagen mixtures effectively improved oxidative stability during 7 days of storage at $4^{\circ}C$. The samples containing collagen mixture B had the lowest lipid oxidation (p<0.05) among groups. These results indicated that collagen mixture C could be used in injection brine to enhance the quality characteristics of meat products, particularly the WHC and tenderness. Collagen mixture A could be used for meat products with high fat contents based on its ability to improve lipid oxidative stability during long-term storage.

• 한국식품과학회지
• /
• 제27권4호
• /
• pp.576-581
• /
• 1995

피부조직에서 추출한 콜라겐의 유동특성을 검토하여 콜라겐을 효율적으로 활용할 수 있는 기초자료를 얻고자 하였다. 콜라겐의 점도는 동물의 나이와 성(sex), 콜라겐 종류에 따라 차이를 보였다. 즉, 주령에 따라서는 콜라겐의 종류에 관계없이 $6{\sim}12$주령의 것이 비교적 높게 나타났으며, 동일 주령에서는 수컷의 점도보다 암컷의 점도가, 그리고 불용성 콜라겐의 점도보다 산가용성 콜라겐의 점도가 높게 나타났다. 콜라겐 용액은 Bingham plastic 및 thixotropic 유체의 특성을 나타냈으며, 온도, pH, 에탄올 농도 및 콜라겐 농도에 따라 점도 변화가 뚜렷하게 나타났다. 즉, 콜라겐 농도를 6%까지 높일 경우 콜라겐 용액의 점조도는 직선적으로 증가하는 경향(산가용성 콜라겐 r=0.972, 불용성 콜라겐 r=0.957)을 나타냈는데, 산가용성 콜라겐의 증가속도가 불용성 콜라겐의 경우보다 높게 나타났다. 온도 증가에 따라 콜라겐 용액의 점조도는 감소하였으며 특히, 산가용성 콜라겐에서는 $30{\sim}40^{\circ}C$ 온도구간에서 점조도가 급격히 감소하였다. pH에 따라 산가용성 콜라겐의 점조도는 pH 6에서 최대치를 보였고, pH 10 부근에서 다시 증가하는 biphasic 현상을 나타냈으나, 불용성 콜라겐의 경우는 pH에 큰 영향을 받지 않았다. 에탄올 농도에 따른 산가용성 콜라겐과 불용성 콜라겐의 점조도는 에탄올 농도 $40{\sim}60%$ 수준에서 높게 나타났다.

• 한국정보기술학회 영문논문지
• /
• 제9권1호
• /
• pp.89-102
• /
• 2019

Collagen can be used in building artificial skin replacements for treatment of burns and towards the reconstruction of bone as well as researching cell behavior and cellular interaction. The strength of collagen in connective tissue rests on the characteristics of collagen fibers. 3D confocal imaging of collagen fibers enables the characterization of their spatial distribution as related to their function. However, the image stacks acquired with confocal laser-scanning microscope does not clearly show the collagen architecture in 3D. Therefore, we developed a new method to reconstruct, visualize and characterize collagen fibers from fluorescence confocal images. First, we exploit the tensor voting framework to extract sparse reliable information about collagen structure in a 3D image and therefore denoise and filter the acquired image stack. We then propose to segment the collagen fibers by defining an energy term based on the Hessian matrix. This energy term is minimized by a min cut-max flow algorithm that allows adaptive regularization. We demonstrate the efficacy of our methods by visualizing reconstructed collagen from specific 3D image stack.

• Archives of Plastic Surgery
• /
• 제35권1호
• /
• pp.7-12
• /
• 2008

Purpose: Since the report of artificial dermis manufacturing method using collagen by Yannas in 1980, collagen has been effectively used as dermal substitute with its merits such as, lower antigeneicity, controllable biodegradation rate, and minimal inflammatory cytotoxic properties in the dermal tissue engineering field. However, weak mechanical durability was the main drawback of collagen dermal substitute. To improve its stability, mechanical or chemical cross-linking was used. Despite of such process, its clinical use was restricted due to weak durability. To improve the durability of collagen matrix, we designed elastin-incorporated collagen matrix and compared its durability with conventional collagen matrix. Methods: 15mm diameter with 4mm thick collagen dermal matrix was made according to Yannas protocol by mixing 0.5% bovine collagen and chondroitin-6-sulfate followed by degassing, freeze drying, dehydrodermal cross-linking and chemical cross-linking procedure. In elastin incorporated collagen matrix, same procedure was performed by mixing elastin to previous collagen matrix in 4:1 ratio(collagen 80% elastin 20%). In comparison of the two dermal matrix in vitro tests, matrix contracture rate, strain, tensile strength, was measured and stiffness was calculated from comparative analysis. Results: In terms of matrix contracture, the elastin-incorperated added collagen dermis matrix showed 1.2 times more contraction compared to conventional collagen matrix. However, tensile strength showed 1.6 times and stiffness showed 1.6 times increase in elastin-incorporated matrix. Conclusion: Elastin incorperated collagen matrix manufactured by our team showed increased durability due to improvement in tensile strength and stiffness compared to previous collagen matrix($Integra^{(R)}$).

• Tissue Engineering and Regenerative Medicine
• /
• 제15권6호
• /
• pp.673-697
• /
• 2018

BACKGROUND: Cartilage tissue engineering (CTE) aims to obtain a structure mimicking native cartilage tissue through the combination of relevant cells, three-dimensional scaffolds, and extraneous signals. Implantation of 'matured' constructs is thus expected to provide solution for treating large injury of articular cartilage. Type I collagen is widely used as scaffolds for CTE products undergoing clinical trial, owing to its ubiquitous biocompatibility and vast clinical approval. However, the long-term performance of pure type I collagen scaffolds would suffer from its limited chondrogenic capacity and inferior mechanical properties. This paper aims to provide insights necessary for advancing type I collagen scaffolds in the CTE applications. METHODS: Initially, the interactions of type I/II collagen with CTE-relevant cells [i.e., articular chondrocytes (ACs) and mesenchymal stem cells (MSCs)] are discussed. Next, the physical features and chemical composition of the scaffolds crucial to support chondrogenic activities of AC and MSC are highlighted. Attempts to optimize the collagen scaffolds by blending with natural/synthetic polymers are described. Hybrid strategy in which collagen and structural polymers are combined in non-blending manner is detailed. RESULTS: Type I collagen is sufficient to support cellular activities of ACs and MSCs; however it shows limited chondrogenic performance than type II collagen. Nonetheless, type I collagen is the clinically feasible option since type II collagen shows arthritogenic potency. Physical features of scaffolds such as internal structure, pore size, stiffness, etc. are shown to be crucial in influencing the differentiation fate and secreting extracellular matrixes from ACs and MSCs. Collagen can be blended with native or synthetic polymer to improve the mechanical and bioactivities of final composites. However, the versatility of blending strategy is limited due to denaturation of type I collagen at harsh processing condition. Hybrid strategy is successful in maximizing bioactivity of collagen scaffolds and mechanical robustness of structural polymer. CONCLUSION: Considering the previous improvements of physical and compositional properties of collagen scaffolds and recent manufacturing developments of structural polymer, it is concluded that hybrid strategy is a promising approach to advance further collagen-based scaffolds in CTE.

• 대한지역사회영양학회지
• /
• 제13권6호
• /
• pp.912-921
• /
• 2008

This study was performed to examine if the effects of collagen supplementation from pork skin could improve the sex steroid hormone, serum lipid and skin crack in Korean middle-aged women. Middle-aged women (40-55 years) who were not diagnosed with any type of disease were included in this study and thirty subjects were randomly assigned to a control group (n = 15) or a collagen supplemented group (n = 15). The collagen supplemented group ingested collagen flour 2 g, 3 times a day for 12 weeks. We measured serum collagen, estrogen, estradiol, estriol, progesterone, total cholesterol, triglyceride, HDL-cholesterol and LDL-cholesterol concentration. The collagen supplementation group had significantly increased serum collagen (p < 0.05) compared with the control group. In addition, skin crack was improved. But, there were no differences for sex steroid hormone and lipid profile in control and collagen supplemented groups. The result of the present study demonstrated that supplementation of 6 g collagen per day for 12 weeks can give beneficial effects on skin crack reduction and serum collagen concentration.

• 대한화장품학회지
• /
• 제30권1호
• /
• pp.135-140
• /
• 2004

피부 노화를 예방할 수 있는 기능성 화장품은 지질과산화를 초래하는 활성산소종(ROS)의 생성 억제와 제거 또는 collagen과 elastin의 사슬 절단 및 교차결합의 변형을 억제하는 효능이 있어야 한다. 본 연구에서는 피부 조직 중 malonedialdehydt (MDA)와 collagen이 항노화 작용이 있는 기능성 화장품의 검색 지표로서의 사용 가능성을 알아보고자 10, 25 주령 랫드의 정상 피부와 창상을 유도한 피부를 7일간 관찰하였다. 육안적인 관찰에서는 10 주령군의 11마리 랫드 중 10마리에서, 노령 랫드군의 11마리 중 8마리에서 창상이 폐쇄되었다. 10 주령 랫드와 비교했을 때 노령 랫드에서 흉터의 길이는 긴 반면에 외피의 폐쇄, collagen 밀도, 외피의 두께, 총 hydroxyproline (hyp)과 MDA 농도가 유의적으로 낮게 나타났다( p〈0.05 ∼ p 〈 0.005). 10 주령에서 진피의 규칙적으로 배열된 collagen 섬유다발과 많은 섬유아세포의 관찰과는 반대로 25 주령 이상 랫드에서는 collagen 섬유다발 사이에 많은 낭포, 소와 및 섬유아세포 수의 감소, 느슨한 외피와 진피의 결합과 얇은 외피가 관찰됨으로서 25 주령 이상의 랫드에서 감소된 hyp 양은 감소된 collagen 밀도 및 형태학적 변화와 일치하였다. 따라서 collagen 합성과 축적의 지표인 hyp의 측정은 항 피부노화 예방 및 개선제의 모니터링 연구에서 매우 유용하며 또한 피부 노화의 검객 지표로 사용이 가능하다고 사료된다.

• 한국응용과학기술학회지
• /
• 제26권4호
• /
• pp.457-466
• /
• 2009

This study is manufacturing method and analysis of feasibility about collagen peptide from fish scale. This is processed by enzyme hydrolysis, isolating and refining etc. The results of analysis of nutritional composition showed protein content of collagen peptide. In the analysis of constitutive amino acids, the ratio of contents of hydroxyproline and glycine, the characteristics of collagen peptides appeared similar and the contents of glutamic acid and aspartic acid which are involved in protein metabolism. As a result of measurement of total polyphenol content and total flavonoid, it showed that collagen peptide had more contents generally, and the effect of bioactivity of pig-skin collagen peptide appeared higher although different kinds of scale collagen peptide showed a little DPPH radical scavenging ability, total antioxidant capacity by ABTS, ACE inhibitory.