• Title/Summary/Keyword: human collagen

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Effects of human collagen α-1 type I-derived proteins on collagen synthesis and elastin production in human dermal fibroblasts

  • Hwang, Su Jin;Kim, Su Hwan;Seo, Woo-Young;Jeong, Yelin;Shin, Min Cheol;Ryu, Dongryeol;Lee, Sang Bae;Choi, Young Jin;Kim, KyeongJin
    • BMB Reports
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    • v.54 no.6
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    • pp.329-334
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    • 2021
  • Collagen type I is the most abundant form of collagen in human tissues, and is composed of two identical α-1 type I chains and an α-2 type I chain organized in a triple helical structure. A previous study has shown that human collagen α-2 type I (hCOL1A2) promotes collagen synthesis, wound healing, and elastin production in normal human dermal fibroblasts (HDFs). However, the biological effects of human collagen α-1 type I (hCOL1A1) on various skin properties have not been investigated. Here, we isolate and identify the hCOL1A1-collagen effective domain (CED) which promotes collagen type I synthesis. Recombinant hCOL1A1-CED effectively induces cell proliferation and collagen biosynthesis in HDFs, as well as increased cell migration and elastin production. Based on these results, hCOL1A1-CED may be explored further for its potential use as a preventative agent against skin aging.

Human collagen alpha-2 type I stimulates collagen synthesis, wound healing, and elastin production in normal human dermal fibroblasts (HDFs)

  • Hwang, Su Jin;Ha, Geun-Hyoung;Seo, Woo-Young;Kim, Chung Kwon;Kim, KyeongJin;Lee, Sang Bae
    • BMB Reports
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    • v.53 no.10
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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.

Analysis of Telopeptide Removal in Type I Collagen Purified From Human Umbilical Cords (사람 탯줄로부터 추출된 Type I Collagen의 Telopeptide 제거에 대한 분석)

  • Suh, Hwal;Ahn, Sue-Jin;Kim, Yo-Sook;Lee, Ha-Gyui
    • Journal of Biomedical Engineering Research
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    • v.17 no.3
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    • pp.297-304
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    • 1996
  • Although collagen is still considered to be a poor immunogen, animals can produce antibodies to a number of different sites in the collagen molecule. In type I collagen, three classes of antigenic determinants have been described those are recogrlized as different degrees in different species. These are essentially composed of helical, conformation-dependent antigenic determinants and terminal, nonhelical antigenic determinants, and finally central antigenic determinants exposed only after denaturation of the collagen molecule. To utilize collagen as implantable biomateriall human e61bryonic collagen, ten immunological to body, was purified from human umbilical cords and found to contain [$\alpha$1(I)]$_2$. [$\alpha$2(I). Each step of purification were observed by polarized light microscope and analyzed through SDS-PAGE. The conclusious are follows; 1 . The purified collagen revealed gradual fiber indenties on each step of purification by polarized microscope. 2. The structual changes of extracted collagen as removed telopeptide were confirmed by SDS-PAGE.

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The Durability of Elastin-Incorporated Collagen Matrix for Dermal Substitute in Vitro Condition (In vitro 환경에서 엘라스틴을 혼합한 콜라겐 진피 지지체의 내구성)

  • Lew, Dae Hyun;Hong, Jong Won;Tark, Kwan Chul
    • Archives of Plastic Surgery
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    • v.35 no.1
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    • pp.7-12
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    • 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($Integra^{(R)}$).

A STUDY ON THE EXPRESSION OF TYPE I AND TYPE II COLLAGEN GENES AND PROTEINS IN THE DEVELOPING HUMAN MANDIBLE

  • Kook, Yoon-Ah;Kim, Sang-Cheol;Kim, Eun-Cheol
    • The korean journal of orthodontics
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    • v.25 no.6 s.53
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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.

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COMPARISON OF THE BIOMECHANICAL AND BIOSYNTHETIC BEHAVIOR OF NORMAL HUMAN FIBROBLASTS AND FIBROBLASTS ISSUE FROM A FOREHEAD WRINKLE

  • Jouandeaud, M.;Viennet, C.;Chadebec, P.;Bordes, S.;Closs, B.;Humbert, P.
    • Proceedings of the SCSK Conference
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    • 2003.09a
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    • pp.192-202
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    • 2003
  • The wrinkles correspond to the most obvious expression of skin ageing and are manifested by changes on the organization and dermal structure. In the extracellular matrix, decreased quantities of collagens and glycosaminoglycans as well as a deterioration of the fibrillary network is noted, result in a reduction of dermal thickness. In addition, the activity of the collagenases increases in contrast to the synthesis of collagen fibers. Nor are cells spared during the aging process. We thus studied and compared the contractile capacity as well as the synthesis capacity of normal human fibroblasts and human fibroblasts obtained from biopsies of forehead wrinkles. The capacity of the fibroblasts to be adhered to the collagen network and to maintain a three-dimensional structure of dermis was studied on a model of equivalent dermis. The metabolic activity was studied by evaluating the capacities of synthesis of collagen I, main component of dermis. Human fibroblasts resulting from the forehead wrinkle contract less the gel of collagen than the normal human fibroblasts and present an activity of biosynthesis of collagen I less important than normal human fibroblasts. These results show that fibroblasts with aging present a deceleration of their metabolic activity and lose their capacity of adhesion to collagen fibers thus limiting the possibility of organizing the dermal tissue. We investigated the potential of an active ingredient able to compensate for the reduction of the metabolic activity and to restore the contractile capacity of fibroblasts obtained from forehead wrinkles. This effect was compared with a reference molecule: the vitamin C.

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Comparison of Human Bone Marrow Stromal Cells with Fibroblasts in Cell Proliferation and Collagen Synthesis (골수기질세포와 섬유아세포의 세포 증식과 교원질 합성능 비교)

  • Han, Seung-Kyu;Yoon, Tae-Hwan;Kim, Woo-Kyung
    • Archives of Plastic Surgery
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    • v.32 no.3
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    • pp.343-346
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    • 2005
  • It has been established that a graft of fibroblasts is able to improve wound healing. However, there has been no research on the effect of a graft of bone marrow stromal cells on wound healing. The wound healing process requires cell proliferation and production of extracellular matrix and various growth factors. The purpose of this study was to compare the abilities of human fibroblasts and bone marrow stromal cells, which contains mesenchymal stem cells, to proliferate and to produce collagen. Human bone marrow stromal cells and fibroblasts were isolated from bone marrow and dermis of the same patients and grown in culture respectively. Cell proliferation and production of type I collagen by human bone marrow stromal cells and dermal fibroblasts were examined by MTT method and by ELISA of cell culture media on day 1, 3, and 5 days post-incubating. The human bone marrow stromal cells showed 11-17% higher cell proliferation than fibroblasts at each time interval. The levels of type I collagen in the human bone marrow stromal cell group was also significantly higher than those in the fibroblast group. The results indicate that the grafts of human bone marrow stromal cells can show more promising effect than that of fibroblasts for healing of chronic wounds.

ISOLATION OF HUMAN ALVEOLAR BONE-DERIVED CELLS AND IN VITRO AMPLIFICATION FOR TISSUE ENGINEERING (조직공학용 사람 치조골세포의 인공증식)

  • Choi, Byung-Ho;Park, Jin-Hyoung;Huh, Jin-Young;Yoo, Jae-Ha
    • Journal of the Korean Association of Oral and Maxillofacial Surgeons
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    • v.27 no.5
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    • pp.453-456
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    • 2001
  • Background: Autogenous alveolar bone cell transplantation may be suitable for tissue engineering for alveolar bone reconstruction. This study aimed to isolate human alveolar bone-derived cells (HABDCs) and to evaluate the ability of collagen gels to support HABDC proliferation and differentiation for human alveolar bone tissue engineering applications. Method: Cultures of primary HABDCs were established from alveolar bone chips obtained from 10 persons undergoing tooth extraction. These cells were expanded in vitro until passage 3 and used for the in vitro characterization of HABDCs and the in vitro analysis of collagen gels for alveolar bone tissue engineering. Results: Of the 10 attempts made to obtain HABDC cultures, eight were successful. HABDCs expressed the osteoblastic phenotype characterized by alkaline phosphatase activity, osteocalcin expression and the mineralization of the extracellular matrix in vitro. When seeded on collagen gels, HABDCs penetrated into the collagen gel matrices and proliferated inside the gels. Significantly, when HABDCs were embedded into the gels, collagen fibers and mineralization were produced within the gels. Conclusion: This study demonstrates the feasibility of using cultured HABDCs and collagen gels for human alveolar bone tissue engineering applications.

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Processed Panax ginseng, Sun Ginseng Increases Type I Collagen by Regulating MMP-1 and TIMP-1 Expression in Human Dermal Fibroblasts

  • Song, Kyu-Choon;Chang, Tong-Shin;Lee, Hye-Jin;Kim, Jin-Hee;Park, Jeong-Hill;Hwang, Gwi-Seo
    • Journal of Ginseng Research
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    • v.36 no.1
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    • pp.61-67
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    • 2012
  • In the present study, effects of sun ginseng (SG) on the collagen synthesis and the proliferation of dermal fibroblast were investigated. Collagen synthesis was measured by assaying procollagen type I C-peptide production. In addition, the level of matrix metalloproteinase (MMP)-1 was assessed by western blot analysis. SG suppressed the MMP-1 protein level in a dose-dependent manner. In contrast, SG dose-dependently increased tissue inhibitors of MMP (TIMP)-1 production in fibroblasts. SG increased type I collagen production directly and/or indirectly by reducing MMP-1 and stimulating TIMP-1 production in human dermal fibroblasts. SG dose-dependently induced fibroblast proliferation and this, in turn, can trigger more collagen production. These results suggest that SG may be a potential pharmacological agent with anti-aging properties in cultured human skin fibroblast.

THE EFFECT OF ADHESIVE GLYCOPROTEINS ON THE ATTACHMENT AND PROLIFERATION OF HUMAN PULPAL CELLS (부착단백질이 사람 치수세포의 부착 및 증식에 미치는 영향에 관한 연구)

  • Shin, Young-Joo;Choi, Ho-Young
    • Restorative Dentistry and Endodontics
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    • v.21 no.1
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    • pp.54-69
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    • 1996
  • The purpose of this vitro study was to evaluate attachment and proliferation of human pulpal cells to the attachment glycoprotein-coated and non-coated culture dishes. Well known adhesive glycoproteins were used, such as type I collagen, type IV collagen, fibronectin, laminin, and vitronection. Each adhesive glycoproteins applied onto the culture dishes. In this study, the protein coated and non-coated dishes were classified as each groups. Human pulpal cells onto each culture dishes. After 90 minute, 4 hour and 24 hour incubation attached cells in each group were counted with hematocytometer for evaluation of the attachemnt of human pulpal cells. The configurations of attached human pulpal cells were done by SEM observation. The results as follows : 1. After 90 minute incubation the score of attachment of human pulpal cells was best in laminin-coated group among groups. Then fibronectin, type IV collagen group were better, and all proteins were higher than control. 2. After 4 hour incubation the numbers of attachment of human pulpal cells were most in fibronectin coated group. 3. After 24 hour incubation all of adhesive glycoproteins showed high and similar attachemtn effect to human pulpal cells. 4. In SEM observation, fibronectin and type IV collagen groups showed well spreaded human pulpal cells, then laminin group was moderately spreaded, and vitronectin group was mildly spreaded as well as control group.

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