Advances in the research of modulation of dermal collagen fibrin assembly by decorin.
- Author:
Deqing QI
;
Yue ZHOU
;
Xuanfen ZHANG
- Publication Type:Journal Article
- MeSH:
Collagen;
Decorin;
metabolism;
Extracellular Matrix;
Extracellular Matrix Proteins;
metabolism;
pharmacology;
Fibrillar Collagens;
metabolism;
ultrastructure;
Fibrin;
metabolism;
Humans;
Microfibrils;
metabolism;
Proteoglycans;
metabolism;
pharmacology
- From:
Chinese Journal of Burns
2015;31(2):157-159
- CountryChina
- Language:Chinese
-
Abstract:
Formation of dermal collagen fiber is a complicated and sequential process with the progressive assembly of collagen. Collagen monomers form stepped and orderly protofibrils through longitudinal displacement. Subsequently, protofibrils or protofibrils and collagen are bonded by covalent bonds to form orderly lamellar structure of collagen fibers. Then collagen fibers are tightly wound into coarse collagen fiber bundles by covalent crosslinking. Decorin is a multifunctional small leucine-rich proteoglycan. It can prevent the aggregation of protofibrils by binding to the specific site of collagen with its core protein, and adjusting the spacing between the protofibrils with its glycosaminoglycan chain. Thus, by effecting the formation of collagen fibers with regulation of collagen assembly, decorin may help prevent scar formation and even promote regeneration.
