Matrix metalloprotease-9 induces transforming growth factor-β1 production in airway epithelium via activation of epidermal growth factor receptors

Perng, Diahn‐Warng; Chang, Kuo-Ting; Su, Kang‐Cheng; Wu, Yelin; Chen, Chunsheng; Hsu, Wen-Jing; Tsai, Chun‐Ming; Lee, Yu-Chin

doi:10.1016/j.lfs.2011.06.008

Cited by 34 publications

(27 citation statements)

References 38 publications

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“…This suggests that MMP-9 plays a role in tissue repair and remodeling. In this context, MMP-9 has been suggested to release or activate a number of cytokines and growth factors, including TGF-␤1 (33,45).…”

Section: Discussionmentioning

confidence: 99%

“…Among its many functions, MMP-9 has been reported to activate latent transforming growth factor (TGF)-␤ to its active form and to induce TGF-␤ production in epithelial cells (27,33,45). Because TGF-␤ stimulates fibroblasts, these observations have led to the suggestion that MMP-9 plays an important role in the tissue remodeling that characterizes many lung diseases.…”

mentioning

confidence: 99%

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Matrix metalloproteinase-9 activates TGF-β and stimulates fibroblast contraction of collagen gels

Kobayashi

Kim

Liu

et al. 2014

American Journal of Physiology-Lung Cellular and Molecular Phys

171

128

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is a matrix-degrading enzyme implicated in many biological processes, including inflammation. It is produced by many cells, including fibroblasts. When cultured in three-dimensional (3D) collagen gels, fibroblasts contract the surrounding matrix, a function that is thought to model the contraction that characterizes both normal wound repair and fibrosis. The current study was designed to evaluate the role of endogenously produced MMP-9 in fibroblast contraction of 3D collagen gels. Fibroblasts from mice lacking expression of MMP-9 and human lung fibroblasts (HFL-1) transfected with MMP-9 smallinterfering RNA (siRNA) were used. Fibroblasts were cast into type I collagen gels and floated in culture medium with or without transforming growth factor (TGF)-␤1 for 5 days. Gel size was determined daily using an image analysis system. Gels made from MMP-9 siRNA-treated human fibroblasts contracted less than control fibroblasts, as did fibroblasts incubated with a nonspecific MMP inhibitor. Similarly, fibroblasts cultured from MMP-9-deficient mice contracted gels less than did fibroblasts from control mice. Transfection of the MMP-9-deficient murine fibroblasts with a vector expressing murine MMP-9 restored contractile activity to MMP-9-deficient fibroblasts. Inhibition of MMP-9 reduced active TGF-␤1 and reduced several TGF-␤1-driven responses, including activity of a Smad3 reporter gene and production of fibronectin. Because TGF-␤1 also drives fibroblast gel contraction, this suggests the mechanism for MMP-9 regulation of contraction is through the generation of active TGF-␤1. This study provides direct evidence that endogenously produced MMP-9 has a role in regulation of tissue contraction of 3D collagen gels mediated by fibroblasts. lung; repair; transforming growth factor-␤

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Matrix metalloproteinase-9 activates TGF-β and stimulates fibroblast contraction of collagen gels

Kobayashi

Kim

Liu

et al. 2014

American Journal of Physiology-Lung Cellular and Molecular Phys

171

128

View full text Add to dashboard Cite

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“…MMPs modulate cell proliferation primarily by indirect mechanisms. For instance, MMP-9 is known to cleave membrane-bound precursor proteins and release EGF-like ligands that subsequently bind to the EGF receptor (100). Similarly, MMPs may sequester TIMP-1, which could lead to inhibition of TIMP-1-mediated fibroblast proliferation (72).…”

Section: Mechanisms Of Mmp Action In Kidney Diseasementioning

confidence: 99%

Matrix metalloproteinases in kidney homeostasis and diseases

Tan

Liu

2012

American Journal of Physiology-Renal Physiology

215

219

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“…Similar increases in survival time of glioblastoma patients were observed when Temozolomide, the currently approved chemotherapeutic agent for glioblastomas, was combined with Marismastat [43]. Other studies have shown that MMPs can also activate growth factors [44,45] which bind to receptors like EGFR; thereby triggering downstream signalling events leading to enhanced cell growth and migration. Likewise, EGFR can induce MMP expression and hence control cancer cell growth and migration [46] to create an invasion-survival feedback loop.…”

Section: Discussionmentioning

confidence: 69%

The microtubule binding drug EM011 inhibits the growth of paediatric low grade gliomas

2013

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Matrix metalloprotease-9 induces transforming growth factor-β1 production in airway epithelium via activation of epidermal growth factor receptors

Cited by 34 publications

References 38 publications

Matrix metalloproteinase-9 activates TGF-β and stimulates fibroblast contraction of collagen gels

Matrix metalloproteinase-9 activates TGF-β and stimulates fibroblast contraction of collagen gels

Matrix metalloproteinases in kidney homeostasis and diseases

The microtubule binding drug EM011 inhibits the growth of paediatric low grade gliomas

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