Focal adhesion kinase activation is required for TNF-α-induced production of matrix metalloproteinase-2 and proinflammatory cytokines in cultured human periodontal ligament fibroblasts

2015 ◽  
Vol 123 (4) ◽  
pp. 249-253 ◽  
Author(s):  
Peng Zhang ◽  
Ya-jing Li ◽  
Liu-yun Guo ◽  
Guo-fang Wang ◽  
Ke Lu ◽  
...  
Keyword(s):  
Matrix Metalloproteinase ◽  
Focal Adhesion Kinase ◽  
Focal Adhesion ◽  
Proinflammatory Cytokines ◽  
Periodontal Ligament ◽  
Matrix Metalloproteinase 2 ◽  
Periodontal Ligament Fibroblasts ◽  
Kinase Activation ◽  
Tnf Α ◽  
Human Periodontal Ligament Fibroblasts

Regulation of mouse blastocyst adhesion, outgrowth and matrix metalloproteinase-2 by focal adhesion kinase

2003 ◽  
Vol 48 (5) ◽  
pp. 475-479
Author(s):  
Guodong Tie ◽  
Yongqiang Tian ◽  
Shuyi Chen ◽  
Yujing Cao ◽  
Zelong Liu ◽  
...  
Keyword(s):  
Matrix Metalloproteinase ◽  
Focal Adhesion Kinase ◽  
Focal Adhesion ◽  
Matrix Metalloproteinase 2 ◽  
Mouse Blastocyst

Matrix metalloproteinase-2 stimulates collagen-I expression through phosphorylation of focal adhesion kinase in rat cardiac fibroblasts

2012 ◽  
Vol 303 (9) ◽  
pp. C947-C953 ◽  
Author(s):  
Yasutomo Hori ◽  
Takashige Kashimoto ◽  
Tomohiro Yonezawa ◽  
Naoya Sano ◽  
Ryuta Saitoh ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Matrix Metalloproteinase ◽  
Focal Adhesion Kinase ◽  
Focal Adhesion ◽  
Cardiac Fibroblasts ◽  
Primary Cultures ◽  
Collagen I ◽  
Matrix Metalloproteinase 2 ◽  
Dependent Manner ◽  
Simultaneous Treatment

Collagen-I is thought to be the main component of the extracellular matrix in cardiac fibrosis, the accumulation of which occurs with excessive activation of matrix metalloproteinase-2 (MMP-2). MMP-2 degrades the extracellular matrix; however, the relative importance of MMP-2 to collagen-I synthesis in cardiac fibroblasts remains unclear. We investigated whether extracellular activation of MMP-2 regulates collagen-I synthesis and phosphorylation of focal adhesion kinase (FAK) in rat cardiac fibroblasts. Primary cultures of rat cardiac fibroblasts were incubated with purified active MMP-2 to determine whether extracellular MMP-2 affects collagen-I synthesis and FAK phosphorylation in cardiac fibroblasts. Exogenous MMP-2 significantly stimulated FAK (Tyr397) phosphorylation and induced collagen-I expression in a time-dependent manner. Simultaneous treatment with the FAK inhibitor PF573228 abolished exogenous MMP-2-enhanced FAK (Tyr397) phosphorylation and collagen-I expression. Cells were then stimulated with norepinephrine (NE) to investigate whether endogenous MMP-2 could also induce collagen-I expression through FAK (Tyr397) phosphorylation. NE-stimulated endogenous MMP-2 activation in conditioned medium was significantly attenuated by simultaneous treatment with the MMP inhibitor PD166793. Similarly, NE-induced FAK (Tyr397) phosphorylation and collagen-I expression were significantly inhibited by simultaneous treatment with PD166793 or PF573228. Furthermore, MMP-2 knockdown induced by small interfering RNA (siRNA) significantly abolished endogenous MMP-2 expression and activation. MMP-2 siRNA significantly abolished NE-induced FAK (Tyr397) phosphorylation and collagen-I expression. These findings suggest that the extracellular activation of MMP-2 accelerated collagen-I synthesis in rat cardiac fibroblasts and that FAK phosphorylation (Tyr397) plays a pivotal role in MMP-2-stimulated collagen-I synthesis.

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