• Macromolecular Research
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• v.15 no.3
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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 the Society of Cosmetic Scientists of Korea
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• v.44 no.1
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• pp.23-29
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• 2018

In this study, sequential cross-linked collagen gels were successfully prepared with collagen, which is biomaterial, and acrylamide (AAm), which is a synthetic monomer. The elastic moduli (E) of cross-linked collagen gels were increased from 1.5 to 3.0 kPa by varying of AAm concentrations. In addition, human dermal fibroblasts were encapsulated into the porous pores introduced into the gels, and cell growth and behavior were investigated. Increasing E of the gels led to decreases in cell growth rate, while the cellular glycosaminoglycan (GAG) production level was elevated. Overall, the growth and cellular activity of skin cells were influenced by the extracellular matrix properties of the collagen gels. In conclusion, these results will be highly useful for designing reconstructive skins and various tissue engineering researches.

• The Journal of the Korean dental association
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• v.11 no.8
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• pp.525-530
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• 1973

True collagenolytic enzymes in animal tissues were first demonstrated by Gross and Lapiere (1962), who showed the ability of such an enzyme in the culture medium of living explants of tadpole tissue to degrade a specific substrate of undenatured collagen under physiological conditions. Recently, tumor-associated collagenolytic activity has been demonstrated in human neoplasm and in ascites V Carcinoma. This investigation have been peforme to determine whether or not a collagen lytic enzyme could e found in isolated solid Tawa sarcoma of Donryu female rat obtained the culture medium. The results were as follows. 1. 11.5mg% of hydroxyproline contained in Donryu rat skin collagen, which was extracted by 0.5M acetic acid. 2. Cultivation of solid Tawa sarcoma tissues on reconstituted rat skin collagen gels showed lysis of adjacent gel after 18 hours, and much more extensive lysis after 5 days. 3. Collagen substrate was not attacked by the common proteolytic enzymes, trypsin, pepsin, and pronase.

• Journal of Ginseng Research
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• v.44 no.1
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• pp.115-122
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• 2020

Background: In aged skin, degradation of collagen fibers, which occupy the majority of the extracellular matrix in the dermis, and changes of aquaporin 3 (AQP3) and skin constituents, such as hyaluronic acid and ceramide, cause wrinkles and decrease skin moisturization to contribute to dryness and lower elasticity skin. Red ginseng (RG) is used as a cosmetic and food material and is known to protect from UVB-induced cell death, increase skin hydration, prevent wrinkles, and have an antioxidative effect. But, in general, RG used as a material is the soluble liquid portion in the solvent, and the part that is not soluble in the solvent is discarded. Thus, we made the whole RG into microgranulation and dispersed in water to produce gel form for using entire RG, and it was named red ginseng NaturalGEL (RG NGEL). Methods: RG NGEL was investigated for matrix metalloproteinases inhibitory activity, induction of Type I collagen, AQP3, hyaluronan synthetase 2, serine palmitoyl transferase, ceramide synthase 3, and filaggrin expression and compared with RG water extract. Results: RG NGEL reduced the levels of UV-induced matrix metalloproteinases and increased Type I collagen in human fibroblast cells and upregulated AQP3, hyaluronan synthetase 2, serine palmitoyl transferase, ceramide synthase 3, and filaggrin expressions in human keratinocytes compared with RG water extract. Conclusion: RG NGEL has the potential as an effective reagent for antiaging cosmetics to improve wrinkle formation and skin hydration.

• Journal of the Society of Cosmetic Scientists of Korea
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• v.44 no.4
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• pp.419-425
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• 2018

In this study, cross-linked collagen gels were successfully prepared with varying of elastic modulus from 0.7 to 17.7 kPa using a chemical cross-linker. Then, human dermal fibroblasts were encapsulated into the porous pores introduced into the gels, and cell growth and behavior were examined by gel's mechanical properties. Specifically, increasing elastic modulus of the gel led to decreases in procollagen synthesis from 47 to 32 ng. In addition, there could be optimum elastic modulus for procollagen production, when the gels were treated with adenosine. However, interestingly, this study discovered that the procollagen production level was not influenced by the elastic modulus of the gel for functional peptide. In conclusion, these results would be highly useful for designing reconstructed skins with varying of elastic modulus to examine functional materials in cosmetics.

• BMB Reports
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• v.40 no.5
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• pp.825-831
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• 2007

Tumor cell invasion and metastasis are often associated with matrix metalloproteinases (MMPs), among which MMP-2 and MMP-9 are of central importance. We previously showed that H-Ras, but not N-Ras, induced invasion of MCF10A human breast epithelial cells in which the enhanced expression of MMP-2 was involved. MMP-2 is produced as a latent pro-MMP-2 (72 kDa) to be activated resulting the 62 kDa active MMP-2. The present study investigated if H-Ras and/or N-Ras induces pro-MMP-2 activation of MCF10A cells when cultured in two-dimensional gel of type I collagen. Type I collagen induced activation of pro-MMP-2 only in H-Ras MCF10A cells but not in N-Ras MCF10A cells. Induction of active MMP-2 by type I collagen was suppressed by blocking integrin ${\alpha}2$, indicating the involvement of integrin signaling in pro-MMP-2 activation. Membrane-type (MT)1-MMP and tissue inhibitor of metalloproteinase (TIMP)-2 were up-regulated by H-Ras but not by N-Ras in the type I collagen-coated gel, suggesting that H-Ras-specific up-regulation of MT1-MMP and TIMP-2 may lead to the activation of pro-MMP-2. Since acquisition of pro-MMP-2 activation can be associated with increased malignant progression, these results may help understanding the mechanisms for the cell surface matrix-degrading potential which will be crucial to the prognosis and therapy of breast cancer metastasis.

• Journal of the Korean Association of Oral and Maxillofacial Surgeons
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• v.35 no.3
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• pp.146-152
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• 2009

Traditional surgical method or injection using filler is performed for soft tissue augmentation. Surgical methods have disadvantage of surgical morbidity. Commercially available injectable materials have the disadvantages such as resorption, short-term effect. repeated application and hypersensitivity. Significant shortcoming of cell therapy using autologous fibroblasts is delay of treatment effect. Chitosan/${\beta}$-glycerol phosphate (GP) solution has thermosensitive property and allows sol-gel transition at physiologic pH and temperature. These properties may resolve the delay of treatment effect. The purposes of this study are to evaluate the viscosity and pH changes of chitosan/${\beta}$-GP solutions and to evaluate the effect of chitosan/${\beta}$-GP solution on fibroblast proliferation and production of collagen. We measured the viscosity and pH as function of temperature, of the solution containing 1:0.7, 1:0.75, 1:0.8 chitosan (1, 10, 100, 700 kDa) /${\beta}$-GP. Fibroblasts from ears of 5 rats were cultured in chitosan/${\beta}$-GP solutions for 3 weeks. Cell proliferation and collagen contents were measured every week with WST (water-soluble tetrazolium salt) assay and Collagen assay respectively. The Results are 1) Chitosan(100 kDa<)/${\beta}$-GP solution (1:0.75) showed sol-gel transition at physiologic pH and body temperature and injectable properties. It will enable to resolve the delay in treatment effect 2) Cell proliferation and total collagen contents of the control group were increased with time. However, these decreased after the 1st week in experimental group 3) Collagen contents in the experimental group are higher than that of control group. Chitosan/${\beta}$-GP solution may provide favorable conditions for cell function

• YAKHAK HOEJI
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• v.52 no.5
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• pp.394-401
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• 2008

In order to access the suppressive effects of piroxicam (PX) and hydrolyzed products of Scutellariae Radix (PSH) on arthritis, we investigated whether PSH gel could suppress the progression of collagen-induced arthritis. PX, one of nonsteroidal anti-inflammatory drugs has been used in the systemic and topical treatment in a variety of inflammatory conditions. Scutellariae Radix, one of the herbal medicines, was used for the purpose of anti-inflammatory and anti-bacterials. For the purpose of transdermal absorption of the hydrogel preparations, two classes of hydrogels (PX, PSH) were formulated with carbomer 940, diethylene glycol monoethyl ether, polyethylene glycol-8-glyceryl caprylate/caprate and triethanolamine. In carrageenan-induced edema in rat hind paws, inhibition of foot swelling was more increased in PSH than PX hydrogel. Rheumatoid factors including serum IgG, IgM and collagen specific antibody were present much lower in PSH gel treated mice than control. Histological examination revealed that PSH hydrogel inhibited infiltration of inflammatory cells into affected paw joint, compared with control. The PSH hydrogel would be a suitable preparation to increase transdermal treatment for anti-inflammatory effects on collagen-induced arthritis.

• Journal of Life Science
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• v.6 no.4
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• pp.241-249
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• 1996

A collagenase was isolated from the culture filtrate of Vibrio mimicus (ATCC 33658). The enzyme was purified to homogeneity by ammonium sulfate precipitation and DEAE-Sephadex A-50 chromatography, which an activity recovery of 22%. The molecular weight of the purified enzyme was estimated to be 42 kDa by SDS-polyacrylamide gel electrophoresis and gel filtration, indication a monomer structure. The optimum pH and temperature od the enzyme for insoluble collagen (Type I) were around 7.75 and 28$\circ$C, respectively. Some chelating agents and serine protease inhibitor inactivated the enzyme, but L-cysteine and histidine did not affect the activity. The amino acid composition indicated that the collagenase contained high amounts of amino acid residues of glycine and alanine. The K$_{m}$ and R$_{cat}$/K$_{m}$ values for the collagenase, using insoluble collagen (type I) as substrate, were 2.86 mg/ml and 972.28 U/mg-protein, respectively.

• Microbiology and Biotechnology Letters
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• v.21 no.4
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• pp.381-391
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• 1993

As the first stage of development of an artificial skin, fibroblasts were cultured in the collagen matrices to make a living dermal equivalent. Mouse embryonic fibroblasts were incorporated into a collagen matrices on plastic dishes containing concentrated DMEM culture media supplemented with sodium bicarbonate, hepes, antibiotics and fetal bovine serum. As the growth stimulation components, glycosaminoglycans were added: hyaluronic acid, chondroitin sulfate, heparin, chitosan were incorporated into the media at a concentration of either 1% or 5% w/w/ to collagen in order to investigate the effect on development of dermal equivalent. After the few days of incubation, gel matrics were contracted and firm dermal equivalent were formed. And the keratinocytes were cultured on top of dermal equivalent and make a three dimensional artificial skin tissue.