Ciprofloxacin up-regulates tendon cells to express matrix metalloproteinase-2 with degradation of type I collagen

2010 ◽  
Vol 29 (1) ◽  
pp. 67-73 ◽  
Author(s):  
Wen-Chung Tsai ◽  
Chih-Chin Hsu ◽  
Carl P.C. Chen ◽  
Hsiang-Ning Chang ◽  
Alice M.K. Wong ◽  
...  
2021 ◽  
Vol 41 ◽  
pp. 100959
Author(s):  
Long-Jie Yan ◽  
Le-Chang Sun ◽  
Kai-Yuan Cao ◽  
Yu-Lei Chen ◽  
Ling-Jing Zhang ◽  
...  

2007 ◽  
Vol 236 (6) ◽  
pp. 1683-1693 ◽  
Author(s):  
Mikala Egeblad ◽  
H.-C. Jennifer Shen ◽  
Danielle J. Behonick ◽  
Lisa Wilmes ◽  
Alexandra Eichten ◽  
...  

Blood ◽  
2012 ◽  
Vol 119 (21) ◽  
pp. 5048-5056 ◽  
Author(s):  
Benoit Detry ◽  
Charlotte Erpicum ◽  
Jenny Paupert ◽  
Silvia Blacher ◽  
Catherine Maillard ◽  
...  

Abstract Lymphatic dysfunctions are associated with several human diseases, including lymphedema and metastatic spread of cancer. Although it is well recognized that lymphatic capillaries attach directly to interstitial matrix mainly composed of fibrillar type I collagen, the interactions occurring between lymphatics and their surrounding matrix have been overlooked. In this study, we demonstrate how matrix metalloproteinase (MMP)–2 drives lymphatic morphogenesis through Mmp2-gene ablation in mice, mmp2 knockdown in zebrafish and in 3D-culture systems, and through MMP2 inhibition. In all models used in vivo (3 murine models and thoracic duct development in zebrafish) and in vitro (lymphatic ring and spheroid assays), MMP2 blockage or down-regulation leads to reduced lymphangiogenesis or altered vessel branching. Our data show that lymphatic endothelial cell (LEC) migration through collagen fibers is affected by physical matrix constraints (matrix composition, density, and cross-linking). Transmission electron microscopy and confocal reflection microscopy using DQ-collagen highlight the contribution of MMP2 to mesenchymal-like migration of LECs associated with collagen fiber remodeling. Our findings provide new mechanistic insight into how LECs negotiate an interstitial type I collagen barrier and reveal an unexpected MMP2-driven collagenolytic pathway for lymphatic vessel formation and morphogenesis.


2007 ◽  
Vol 236 (8) ◽  
pp. spc1-spc1
Author(s):  
Mikala Egeblad ◽  
H.-C. Jennifer Shen ◽  
Danielle J. Behonick ◽  
Lisa Wilmes ◽  
Alexandra Eichten ◽  
...  

2012 ◽  
Vol 23 (2) ◽  
pp. 297-309 ◽  
Author(s):  
Amélie Juin ◽  
Clotilde Billottet ◽  
Violaine Moreau ◽  
Olivier Destaing ◽  
Corinne Albiges-Rizo ◽  
...  

Invadosomes are F-actin structures capable of degrading the matrix through the activation of matrix metalloproteases. As fibrillar type I collagen promotes pro-matrix metalloproteinase 2 activation by membrane type 1 matrix metalloproteinase, we aimed at investigating the functional relationships between collagen I organization and invadosome induction. We found that fibrillar collagen I induced linear F-actin structures, distributed along the fibrils, on endothelial cells, macrophages, fibroblasts, and tumor cells. These structures share features with conventional invadosomes, as they express cortactin and N-WASP and accumulate the scaffold protein Tks5, which proved essential for their formation. On the basis of their ability to degrade extracellular matrix elements and their original architecture, we named these structures “linear invadosomes.” Interestingly, podosomes or invadopodia were replaced by linear invadosomes upon contact of the cells with fibrillar collagen I. However, linear invadosomes clearly differ from classical invadosomes, as they do not contain paxillin, vinculin, and β1/β3 integrins. Using knockout mouse embryonic fibroblasts and RGD peptide, we demonstrate that linear invadosome formation and activity are independent of β1 and β3 integrins. Finally, linear invadosomes also formed in a three-dimensional collagen matrix. This study demonstrates that fibrillar collagen I is the physiological inducer of a novel class of invadosomes.


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