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

Cited 16 time in Web of Science Cited 16 time in Scopus
Authors
Son, Eui Dong; Kim, Hyaekyoung; Chi, Hyunjung; Lee, So Hee; Kim, Sujung; Lee, Sera; Hwang, Jae Sung; Chung, Jin Ho; Closs, B.; Lee, Jin Young
Issue Date
2009-02
Publisher
ELSEVIER IRELAND LTD
Citation
JOURNAL OF DERMATOLOGICAL SCIENCE; Vol.53(2); 150-152
Keywords
FibronectinExtracellular matrixCathepsin GSkin agingFibronectin fragments
Abstract
Fibronectin (Fn) is a glycoprotein that is found in the plasma
and is a component of the extracellular matrix (ECM). It binds to
collagen and fibulin, as well as a class of the cell surface
adhesion receptors termed integrins, and has been shown to be
involved in various biological activities, including cell attachment,
cell migration, and wound healing [1]. Fn is readily
degraded into fibronectin fragment (Fn-frs) through the action
of many different types of proteases [2] containing cathepsin G
[3]. The expression of MMP (matrix metalloproteinase) by Fn-frs
(Fn-f29; N-terminal heparin binding fragment, 45 kDa; Fn-f45,
collagen binding fragment, and 110 kDa; Fn-f110 cell binding
fragment) has been studied in chondrocytes [4–6], however,
little is known about the roles of Fn-frs, or cathepsin G-mediated
fragmentation of Fn, in aged human skin and normal human
fibroblasts (NHFs).
ISSN
0923-1811
Language
English
URI
http://hdl.handle.net/10371/78179
DOI
https://doi.org/10.1016/j.jdermsci.2008.08.006
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College of Medicine/School of Medicine (의과대학/대학원)Dermatology (피부과학전공)Journal Papers (저널논문_피부과학전공)
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