scholarly journals Effects of mechanical stress on chondrocyte phenotype and chondrocyte extracellular matrix expression

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Qiang Liu ◽  
Xiaoqing Hu ◽  
Xin Zhang ◽  
Xiaoning Duan ◽  
Peng Yang ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Mechanical Stress ◽  
Chondrocyte Phenotype ◽  
Matrix Expression

Effect of quercetin on chondrocyte phenotype and extracellular matrix expression

2020 ◽  
Vol 18 (12) ◽  
pp. 922-933
Author(s):  
Zhi-Peng GUI ◽  
Yue HU ◽  
Yu-Ning ZHOU ◽  
Kai-Li LIN ◽  
Yuan-Jin XU
Keyword(s):  
Extracellular Matrix ◽  
Chondrocyte Phenotype ◽  
Matrix Expression

Knockdown of IRF3 inhibits extracellular matrix expression in keloid fibroblasts

2017 ◽  
Vol 88 ◽  
pp. 1064-1068 ◽  
Author(s):  
Yi Zhang ◽  
Li Zhang ◽  
Xiao-hua Lin ◽  
Zhi-ming Li ◽  
Qi-yu Zhang
Keyword(s):  
Extracellular Matrix ◽  
Matrix Expression ◽  
Keloid Fibroblasts

Extracellular matrix expression of human prolapsed vaginal wall

2009 ◽  
Vol 29 (4) ◽  
pp. 582-586 ◽  
Author(s):  
Elizabeth Mosier ◽  
Victor K. Lin ◽  
Philippe Zimmern
Keyword(s):  
Extracellular Matrix ◽  
Vaginal Wall ◽  
Matrix Expression

Abstract 573: Mechanical Stress Alters Cell Signaling and Extracellular Matrix Genes in Fetal Cardiac Valves

2018 ◽  
Vol 123 (Suppl_1) ◽  
Author(s):  
Rebekah Macfie ◽  
Alex Bridges ◽  
Herbert M Espinoza ◽  
Isa Lindgren ◽  
Samantha Louey ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Cell Signaling ◽  
Mechanical Stress ◽  
Cardiac Valves

scholarly journals A MicroRNA-29 Mimic (Remlarsen) Represses Extracellular Matrix Expression and Fibroplasia in the Skin

2019 ◽  
Vol 139 (5) ◽  
pp. 1073-1081 ◽  
Author(s):  
Corrie L. Gallant-Behm ◽  
Joseph Piper ◽  
Joshua M. Lynch ◽  
Anita G. Seto ◽  
Seok Jong Hong ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Matrix Expression

Expression of fibronectin splice variants in the postischemic rat kidney

2001 ◽  
Vol 280 (6) ◽  
pp. F1037-F1053 ◽  
Author(s):  
Anna Zuk ◽  
Joseph V. Bonventre ◽  
Karl S. Matlin
Keyword(s):  
Extracellular Matrix ◽  
Splice Variants ◽  
Rat Kidney ◽  
Ischemia Reperfusion ◽  
Single Gene ◽  
Gene Transcript ◽  
Type Iii ◽  
Matrix Expression ◽  
Injured Kidney

Using an in vivo rat model of unilateral renal ischemia, we previously showed that the expression and distribution of fibronectin (FN), a major glycoprotein of plasma and the extracellular matrix, dramatically changes in response to ischemia-reperfusion. In the distal nephron in particular, FN accumulates in tubular lumens, where it may contribute to obstruction. In the present study, we examine whether the tubular FN is the plasma or cellular form, each of which is produced by alternative splicing of a single gene transcript. We demonstrate that FN in tubular lumens does not contain the extra type III A (EIIIA) and/or the extra type III B (EIIIB) region, both of which are unique to cellular FN. It does, however, contain the V95 region, which in the rat is a component of FNs in both plasma and the extracellular matrix. Expression of FN containing EIIIA increases dramatically in the renal interstitium after ischemic injury and continues to be produced at high levels 6 wk later. V95-containing FN also increases in the interstitial space, albeit more slowly and at lower levels than FN containing EIIIA; it also persists 6 wk later. FN containing the EIIIB region is not expressed in the injured kidney. The presence of V95 but not the EIIIA or EIIIB regions of FN in tubular lumens identifies the origin of FN in this location as the plasma; tubular FN is ultimately voided in the urine. The data indicate that both plasma and cellular FNs containing the V95 and/or EIIIA regions may contribute to the pathogenesis of acute renal failure and to the repair of the injured kidney.

scholarly journals Myofibroblast contraction activates latent TGF-β1 from the extracellular matrix

2007 ◽  
Vol 179 (6) ◽  
pp. 1311-1323 ◽  
Author(s):  
Pierre-Jean Wipff ◽  
Daniel B. Rifkin ◽  
Jean-Jacques Meister ◽  
Boris Hinz
Keyword(s):  
Extracellular Matrix ◽  
Growth Factor ◽  
Mechanical Stress ◽  
Protease Activity ◽  
Transforming Growth Factor ◽  
Transforming Growth Factor Β1 ◽  
Stress Fibers ◽  
Fibrotic Diseases ◽  
Triton X ◽  
Tgf Β1

The conjunctive presence of mechanical stress and active transforming growth factor β1 (TGF-β1) is essential to convert fibroblasts into contractile myofibroblasts, which cause tissue contractures in fibrotic diseases. Using cultured myofibroblasts and conditions that permit tension modulation on the extracellular matrix (ECM), we establish that myofibroblast contraction functions as a mechanism to directly activate TGF-β1 from self-generated stores in the ECM. Contraction of myofibroblasts and myofibroblast cytoskeletons prepared with Triton X-100 releases active TGF-β1 from the ECM. This process is inhibited either by antagonizing integrins or reducing ECM compliance and is independent from protease activity. Stretching myofibroblast-derived ECM in the presence of mechanically apposing stress fibers immediately activates latent TGF-β1. In myofibroblast-populated wounds, activation of the downstream targets of TGF-β1 signaling Smad2/3 is higher in stressed compared to relaxed tissues despite similar levels of total TGF-β1 and its receptor. We propose activation of TGF-β1 via integrin-mediated myofibroblast contraction as a potential checkpoint in the progression of fibrosis, restricting autocrine generation of myofibroblasts to a stiffened ECM.

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