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Cosmetics Biotechnology Symposium : 공동개최 : (재)제주테크노파크 : 좌장 : 변 상 요(아주대)

Cathepsin G increases MMP expression in normal human fibroblasts through fibronectin fragmentation, and induces the conversion of proMMP-1 to active MMP-1

초록

영어

Among matrix proteins, fibronectin (Fn) has been known to adhesion protein containing binding site to extracellular matrix proteins (collagen, fibulin) and cell surface receptor (integrin). Although the expression of MMP by fibronectin fragments (Fn-frs) have been investigated in chondrocyte, little is known about the roles of Fn-frs in aged human skin and normal human fibroblasts (NHFs), and the roles of cathepsin G that digested Fn. Therefore, the purpose of this study was to investigate the relationship between cathepsin G-mediated fragmentation of Fn and induction of MMPs that leads to increased extracellular matrix degradation during intrinsic aging and photoaging in skin.Fn-frs were measured in young and aged skin, and then compared with cathepsin G. We also investigated whether Fn-frs increase MMP-1 expression and cathepsin G stimulate proMMP-1 to convert active MMP-1. We found that cathepsin G expression is higher in aged skin than in young skin, and that this is correlated with increased fragmentation of Fn. Studies with cultured normal human fibroblasts (NHFs) showed that specific Fn fragments (Fn-f45:N-terminal gelatin binding fragment, Fn-f70:N-terminal heparin and gelatin binding fragment) induced MMP-1 expression and MMP-2 activity.Thus, the generation of Fn fragments by cathepsin G contributes to damage of matrix in aged skin.

저자정보

  • Eui Dong SON Bioscience Research Institute, AMOREPACIFIC CORPORATION R&D CENTER.

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