Document Detail


Development of collagenase-resistant collagen and its interaction with adult human dermal fibroblasts.
MedLine Citation:
PMID:  14568426     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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 degrees 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.
Authors:
Hyun Chul Goo; Yu Shik Hwang; Yon Rak Choi; Hyun Nam Cho; Hwal Suh
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Publication Detail:
Type:  Evaluation Studies; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Biomaterials     Volume:  24     ISSN:  0142-9612     ISO Abbreviation:  Biomaterials     Publication Date:  2003 Dec 
Date Detail:
Created Date:  2003-10-21     Completed Date:  2004-08-03     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  8100316     Medline TA:  Biomaterials     Country:  England    
Other Details:
Languages:  eng     Pagination:  5099-113     Citation Subset:  IM    
Affiliation:
Department of Medical Engineering, Yonsei University College of Medicine, 134 Shinchon-dong, Seodaemun-ku, Seoul, South Korea.
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MeSH Terms
Descriptor/Qualifier:
Biocompatible Materials / chemical synthesis,  chemistry
Catechin / analogs & derivatives*,  chemistry*
Cell Adhesion / physiology
Cell Division / physiology
Cells, Cultured
Collagen / chemical synthesis,  chemistry*
Collagenases / chemistry*
Culture Techniques / methods*
Fibroblasts / physiology*
Humans
Macrophages / physiology
Male
Matrix Metalloproteinase 1 / chemistry*
Microfilaments / metabolism*,  ultrastructure*
Middle Aged
Protein Conformation
Skin / cytology
Skin Physiological Phenomena
Structure-Activity Relationship
Temperature
Tissue Engineering / methods
Chemical
Reg. No./Substance:
0/Biocompatible Materials; 154-23-4/Catechin; 9007-34-5/Collagen; 989-51-5/epigallocatechin gallate; EC 3.4.24.-/Collagenases; EC 3.4.24.7/Matrix Metalloproteinase 1

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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