• 한국조리학회지
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• 제8권1호
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• pp.95-105
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• 2002

This study was conducted to present the fundamental data on physicochemical properties of chicken foot collagen by the comparison with those from pork skin, which is present used in the factories as evaluate the usability of chicken foot in the industries of collagen production. Moisture content of chicken foot skin (CFS) was higher than that of pork skin (PS), and crude protein content was higher in PS. Content of other compositions was not different in both samples. At the evaluation of the soaking processing, effective time lapsed for soaking the skin in acid solution (acetic acid of 0.1 M) was about 12 hr for efficient extract ion of collagen, when tested by the changes of pH of the soaking solution and the increase of the weight of skins. L-Hydroxyproline of PS was slightly higher than that of CFS. Collagens were loaded in a SDS-PAGE and compared. Separated pattern of collagen of CFS was very similar to that of PS. Major collagen of CFS might be clarified as type I collagen.

• 한국표면공학회:학술대회논문집
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• 한국표면공학회 2013년도 춘계학술대회 논문집
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• pp.38-38
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• 2013

The mechanical cues that adherent cells derive from the extracellular matrix (ECM) can effect dramatic changes in cell migration, proliferation, and differentiation. Using a thin film of Type I collagen fibrils comprised of 100 nm to 200 nm collagen fibrils overlaying a bed of smaller fibrils, changes in cellular response to systematically controlled changes in mechanical properties of collagen was investigated. Further, an experimental and modeling approaches to calculate the elastic modulus of individual collagen fibrils, and thereby the effective stiffness of the entire collagen thin film matrix, from atomic force microscopy force spectroscopy data was performed. These results demonstrate an approach to analysis of fundamental properties of thin, heterogeneous, organic films, and add further insights into the mechanical properties of collagen fibrils that are of relevance to cell response to the ECM.

• 생명과학회지
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• 제31권12호
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• pp.1142-1148
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• 2021

인간의 평균수명이 연장되면서 폐경 이후 여성의 삶의 질에도 많은 관심을 가지게 되었다. 한국인 여성에서 폐경이 나타나는 시기는 평균적으로 49.7세로 알려져 있으며, 폐경 이후의 삶이 일생의 1/3 이상을 차지하게 되어 주요한 사회적 문제로 대두되고 있다. L-ascorbic acid (AsA)는 생물의 에너지 대사과정에서 필수적인 조효소로 작용하고 있으며, 특히, 골 구성 단백질인 collagen의 합성 및 성숙에 관여하고 있는 것으로 알려져 있다. 따라서 본 연구에서는 폐경 여성에서의 AsA와 골 건강에 대해 소개하고자 하였다. AsA는 collagen 생합성에 중요한 인자이며, collagen은 골을 구성하는 단백질로써 골 기질의 석회화를 위해 필요한 물질이므로 골 건강에 대한 AsA의 역할은 대단히 중요하다는 것을 알 수 있다. Collagen 가교는 동물의 성장 과정에서 collagen 섬유의 안정화 및 탄력성을 위해 필요한 것이나, 과잉의 증가는 세포 간 영양소 또는 노폐물의 이동이 억제되어 더욱 노화로 연결되기 쉽다. AsA는 collagen 미숙가교 형성에 환원제로 작용하여 미숙가교를 안정화하여, 미숙가교에서 성숙가교인 pyridinoline이 생성되는 반응을 억제시킨다. 따라서, AsA는 collagen 생합성에 관여하여 골 조직의 건강에 도움을 주는 한편, collagen 가교의 지나친 성숙을 조절하여 폐경 여성에게서 나타날 수 있는 골 관련 문제에 중요한 역할을 할 것으로 추측된다. 이상의 정보는 폐경 여성의 골 건강에 대한 향후 연구에 기초자료로 이용될 수 있을 것으로 기대된다.

• BMB Reports
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• 제53권10호
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• pp.539-544
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• 2020

Skin aging appears to be the result of overlapping intrinsic (including genetic and hormonal factors) and extrinsic (external environment including chronic light exposure, chemicals, and toxins) processes. These factors cause decreases in the synthesis of collagen type I and elastin in fibroblasts and increases in the melanin in melanocytes. Collagen Type I is the most abundant type of collagen and is a major structural protein in human body tissues. In previous studies, many products containing collagen derived from land and marine animals as well as other sources have been used for a wide range of purposes in cosmetics and food. However, to our knowledge, the effects of human collagen-derived peptides on improvements in skin condition have not been investigated. Here we isolate and identify the domain of a human COL1A2-derived protein which promotes fibroblast cell proliferation and collagen type I synthesis. This human COL 1A2-derived peptide enhances wound healing and elastin production. Finally, the human collagen alpha-2 type I-derived peptide (SMM) ameliorates collagen type I synthesis, cell proliferation, cell migration, and elastin synthesis, supporting a significant anti-wrinkle effect. Collectively, these results demonstrate that human collagen alpha-2 type I-derived peptides is practically accessible in both cosmetics and food, with the goal of improving skin condition.

• Fisheries and Aquatic Sciences
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• 제24권12호
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• pp.406-414
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• 2021

The objective of this study was to investigate the yield and characteristics of collagen protein extracted from the muscle of four different species of mantis shrimp: Miyakella nepa, Harpiosquilla harpax, Erugosquilla woodmasoni, and Odontodactylus cultrifer. Mantis shrimp muscle was extracted by using a pepsin-solubilization technique, with 0.5 M acetic acid and 5% pepsin enzyme. The highest collagen yield was from M. nepa muscle (0.478 ± 0.06%), which was significantly greater (p < 0.05) than that from H. harpax, O. cultrifer, and E. woodmasoni (0.313 ± 0.03%, 0.123 ± 0.02%, and 0.015 ± 0.00%, respectively). The freeze-dried collagen appeared as thin fibers, and formed an opaque film. The pepsin-soluble collagen (PSC) from four mantis shrimp species was analyzed by gel electrophoresis. The results showed that all species of mantis shrimp contained type I collagen, consisting of β, α1, and α2 subunits with average molecular weights of 250, 145, and 118 kDa, respectively. The study of the solubility of collagen showed that, for NaCl, collagen had the highest relative solubility in 2% NaCl (80.20 ± 4.95%). In contrast, the solubility decreased at higher NaCl concentrations. However, in terms of pH, collagen had the highest relative solubility at pH 3 (91.32 ± 5.14%), and its solubility decreased at higher pH. FT-IR spectroscopy was used to compare the collagen with a model compound. Five wavenumbers in the spectrum for model collagen were identified: Amide A (3,406-3,421 cm^-1), amide B (2,916-2,940 cm^-1), amide I (1,639-1,640 cm^-1), amide II (1,539-1,570 cm^-1), and amide III (1,234-1,250 cm^-1).

• 대한치과교정학회지
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• 제25권6호
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• pp.723-731
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• 1995

Type I and type II collagens are considered the major collagens of bone and cartilage respectively. Monitoring the patterns of those gene and protein expressions during development will provide a basis for the understanding of the normal and abnormal growths. This study was undertaken to investigate the expression of collagen genes and proteins involved in the developing human mandible. Fifty embryos and fetuses were studied with Alcian blue-PAS, Masson's Trichrome, reverse transcription polymerase chain reaction (RT-PCR), Western blot analysis, and Southern blot analysis. Our results showed that $pro-{\alpha}1(II)$ collagen gene expression begins in the 5th week. Type II collagen is synthesized in mesenchymal cells in advance: of overt chondrogenesis. The gene expression for type II collagen was highest during the appearance of Meckel's cartilage. There was a switch in collagen protein expression from type I to type II during the appearance stage of Meckel's cartilage. The distribution of the mRNA for type II collagen corresponded well with the pattern of type II collagen protein. The endochondral ossification was observed where there was direct replacement of cartilage by bone.

• 대한의용생체공학회:의공학회지
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• 제35권6호
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• pp.192-196
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• 2014

Collagen scaffolds were synthesized by cross linking into a solution mixture of 1-ethyl-3-[3-dimethylaminopropyl] carbodiimide hydrochlorid(EDC) in ethanol, followed by pressing, cleaning and lyophilization process after the type I atelo-collagen solutions in D.I water(pH3). The experimental conditions are collagen concentration of 1.0 wt%, 3.0 wt%, 5.0 wt% and differential concentration of cross-linker. Then, parametric studies were performed by varying the parameters to investigate the morphology, the porosity, the swelling ratio and the thickness and genotoxicity of the scaffolds. The scaffolds thickness pattern was regular to concentration of the degree of cross-linker and collagen. It was observed that the swelling ratio, the degree of crosslink, and the pore size(thickness of scaffold) can be controlled by adjusting the collagen, crosslinker. Among the parameters investigated, the smallest thickness can be achieved by collagen, crosslinker concentrate condition. The collagen scaffold is induced no genotoxicity. The lowest swelling ratio, as an indication of the highest degree of crosslink, can be obtained by adding crosslink agent.

• Fisheries and Aquatic Sciences
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• 제10권2호
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• pp.53-59
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• 2007

In order to utilize skin of bullfrog (Rana catesbeiana Shaw) as an alternative source of collagen, we investigated and compared biochemical and physical properties of collagens isolated from bullfrog skin. Two kinds of collagen (BSASC; bullfrog skin acid-soluble collagen and BSPSC; bullfrog skin pepsin-solubilized collagen) were isolated by subsequent treatments with acetic acid and pepsin. The amounts of skin collagen isolated in the subsequent treatments were 7.3% BSASC and 18.2% BSPSC on the basis of lyophilized bullfrog skin weight, respectively. According to the electrophoretic pattern and CM-cellulose column chromatogram, the BSASC has the chain composition of ${\alpha}1{\alpha}2{\alpha}3$ heterotrimer, and the BSPSC consists of two ${\alpha}$ chains of ${\alpha}1{\alpha}2$. In addition, the denaturation temperatures of all collagens tested were ranged from $30^{\circ}C\;to\;38^{\circ}C$. This study suggests that there is a possibility to use bullfrog skin collagen as an alternative source of collagen for industrial purposes, and subsequently it may increase the economical value of the bullfrog.

• 한국식품영양과학회지
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• 제26권3호
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• pp.475-479
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• 1997

A decrease in the circulating levels of estrogen, occuring as a consequence of post menopausal decline or from surgical ovariectomy, results in an accelerated loss of bone. Estrogen has been shown to stimulate lysyl oxidase activity, and the treatment with estrogen increased the pyridinium content of cortical bone. a trivalent mature cross-links collagen fibrils named pyridinoline, which is especially abundant in collagen of cartilage and bone, markedly increases with growth in humans and rats. The main aim of this study was to examine the increased bone loss caused by ovariectomy through monitoring the concentrations of the collagen and the pyridinium cross-links of collagen, pyridinoline. The ovariectomized rats, 4 weeks old, were divided at random into two or three groups of 5. Ovariectomies were carried out on both of the saline-treated group(OVX(NH)) and the estrogen-treated group(OVX(H)) using the dorsal approach and sham operations were performed on the sham-operated group(sham). They were maintained under identical conditions for 4 or 8 weeks and were allowed free access to food and water. it was observed that there was no significant difference between the control group and the sham-operated group, however, the control group had a higher content of collagen than the saline-treated group after 4 weeks and 8 weeks. Based on these results, iot is supposed that estrogen can enhance collagen synthesis and affects the pyridinoline formation in collagen fibrils through stimulating lysyl oxidase activity.

• 한국식품영양과학회지
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• 제26권3호
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• pp.501-506
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• 1997

As pyridinoline is one of the predominant cross-lins in a mature collagen, pyridinoline formation may be an essential step during the growth process to obtain normal mechanical strength in collagen fibrils. However, the excess formation of pyridinoline in collagen will probably make the tissue stiffer, less soluble and less digestible by enzymes. We investigated the changes of pyridinoline of bone collagen and the role of ascforbic acid(AsA) on the formation of pyridinoline. The pyridinoline content of bone collagen significantly increased during incubation for 1~5 weeks at 37$^{\circ}C$ in vitro. The addition of AsA decreased pyridinoline to half the amount found in controls with 5 week incubation. When dehydroascorbic acid(DHA) and L-2, 3-diketogulonic acid (DKG), the oxidative products of AsA, were supplemented to bone collagen solution instead of AsA, the content of pyridinoline in bone collagen was about 80% or 70% that of controls, respectively. These results suggest that pyridinoline content decreases by the addition of AsA in vitro. Furthermore, it was shown that AsA in oxidized from also affected the formation of pyridinoline.