Development of collagenase-resistant collagen and its interaction with adult human dermal fibroblasts.
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.
Department of Medical Engineering, Yonsei University College of Medicine, 134 Shinchon-dong, Seodaemun-ku, Seoul, South Korea.
Hyun Chul
HC
Goo
Yu Shik
YS
Hwang
Yon Rak
YR
Choi
Hyun Nam
HN
Cho
Hwal
H
Suh
D008841:Actin Cytoskeleton / Q000378:metabolism* / Q000648:ultrastructure*; D001672:Biocompatible Materials / Q000138:chemical synthesis / Q000737:chemistry; D002392:Catechin / Q000031:analogs & derivatives* / Q000737:chemistry*; D002448:Cell Adhesion / Q000502:physiology; D002455:Cell Division / Q000502:physiology; D002478:Cells, Cultured; D003094:Collagen / Q000138:chemical synthesis / Q000737:chemistry*; D017364:Collagenases / Q000737:chemistry*; D046508:Culture Techniques / Q000379:methods*; D005347:Fibroblasts / Q000502:physiology*; D006801:Humans; D008264:Macrophages / Q000502:physiology; D008297:Male; D020781:Matrix Metalloproteinase 1 / Q000737:chemistry*; D008875:Middle Aged; D011487:Protein Conformation; D012867:Skin / Q000166:cytology; D012879:Skin Physiological Phenomena; D013329:Structure-Activity Relationship; D013696:Temperature; D023822:Tissue Engineering / Q000379:methods
D001672:Biocompatible Materials; D002392:Catechin; D003094:Collagen; C045651:epigallocatechin gallate; D017364:Collagenases; D020781:Matrix Metalloproteinase 1