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Development of collagenase-resistant collagen and its interaction with adult human dermal fibroblasts

Authors
 Hyun Chul Goo  ;  Yu-Shik Hwang  ;  Hwal Suh  ;  Hyun Nam Cho  ;  Yon Rak Choi 
Citation
 BIOMATERIALS, Vol.24(28) : 5099-5113, 2003 
Journal Title
 BIOMATERIALS 
ISSN
 0142-9612 
Issue Date
2003
MeSH
Actin Cytoskeleton/metabolism* ; Actin Cytoskeleton/ultrastructure* ; Biocompatible Materials/chemical synthesis ; Biocompatible Materials/chemistry ; Catechin/analogs & derivatives* ; Catechin/chemistry* ; Cell Adhesion/physiology ; Cell Division/physiology ; Cells, Cultured ; Collagen/chemical synthesis ; Collagen/chemistry* ; Collagenases/chemistry* ; Culture Techniques/methods* ; Fibroblasts/physiology* ; Humans ; Macrophages/physiology ; Male ; Matrix Metalloproteinase 1/chemistry* ; Middle Aged ; Protein Conformation ; Skin/cytology ; Skin Physiological Phenomena ; Structure-Activity Relationship ; Temperature ; Tissue Engineering/methods
Keywords
EGCG ; Collagen ; Collagenase resistance ; Structural stability ; Free-radical scavenging activity ; Cell adhesion ; Actin filament
Abstract
Collagen is regarded as one of the most useful biomaterials. The excellent biocompatibility and safety due to its biological characteristics, such as biodegradability and weak antigenecity, made collagen the primary source in biomedical application. Collagen has been widely used in the crosslinked form to extend the durability of collagen. The chemical treatment influences the structural integrity of collagen molecule resulting in the loss of triple helical characteristic. The structural characteristic of collagen is importantly related to its biological function for the interaction with cell. In this study, structural stability of collagen was enhanced thought EGCG treatment, resulting in high resistance against degradation by bacterial collagenase and MMP-1, which is confirmed by collagen zymography. The triple helical structure of EGCG-treated collagen could be maintained at 37°C in comparison with collagen, which confirmed by CD spectra analysis, and EGCG-treated collagen showed high free-radical scavenging activity. Also, with fibroblasts culture on EGCG-treated collagen, the structural stability of EGCG-treated collagen provided a favorable support for cell function in cell adhesion and actin filament expression. These observations underscore the need for native, triple helical collagen conformation as a prerequisite for integrin-mediated cell adhesion and functions. According to this experiment, EGCG-treated collagen assumes to provide a practical benefit to resist the degradation by collagenase retaining its structural characteristic, and can be a suitable biomaterial for biomedical application.
Full Text
http://www.sciencedirect.com/science/article/pii/S0142961203004319
DOI
10.1016/S0142-9612(03)00431-9
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Medical Engineering (의학공학교실) > 1. Journal Papers
Yonsei Authors
Suh, Hwal(서활)
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/114008
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