scholarly journals Sarcomeric model of stretch-induced stress fiber reorganization

2010 ◽  
pp. 13 ◽  
Author(s):  
Roland Kaunas ◽  
Hsu ◽  
Deguchi
Keyword(s):  
Stress Fiber ◽  
Induced Stress

scholarly journals Activation of Na+-H+Exchange Is Necessary for RhoA-induced Stress Fiber Formation

1996 ◽  
Vol 271 (37) ◽  
pp. 22281-22284 ◽  
Author(s):  
Zinaida S. Vexler ◽  
Marc Symons ◽  
Diane L. Barber
Keyword(s):  
Stress Fiber ◽  
Fiber Formation ◽  
Stress Fiber Formation ◽  
Induced Stress

scholarly journals Tumor Necrosis Factor-α Induces Stress Fiber Formation through Ceramide Production: Role of Sphingosine Kinase

2001 ◽  
Vol 12 (11) ◽  
pp. 3618-3630 ◽  
Author(s):  
Atef N. Hanna ◽  
Luc G. Berthiaume ◽  
Yutaka Kikuchi ◽  
David Begg ◽  
Sylvain Bourgoin ◽  
...  
Keyword(s):  
Focal Adhesion ◽  
Tumor Necrosis ◽  
Sphingosine Kinase ◽  
Stress Fiber ◽  
Fiber Formation ◽  
Stress Fiber Formation ◽  
Induced Stress ◽  
Tnf Α ◽  
Factor Α ◽  
Necrosis Factor

Tumor necrosis factor-α (TNF-α) is a proinflammatory cytokine that activates several signaling cascades. We determined the extent to which ceramide is a second messenger for TNF-α-induced signaling leading to cytoskeletal rearrangement in Rat2 fibroblasts. TNF-α, sphingomyelinase, or C2-ceramide induced tyrosine phosphorylation of focal adhesion kinase (FAK) and paxillin, and stress fiber formation. Ly 294002, a phosphatidylinositol 3-kinase (PI 3-K) inhibitor, or expression of dominant/negative Ras (N17) completely blocked C2-ceramide- and sphingomyelinase-induced tyrosine phosphorylation of FAK and paxillin and severely decreased stress fiber formation. The TNF-α effects were only partially inhibited. Dimethylsphingosine, a sphingosine kinase (SK) inhibitor, blocked stress fiber formation by TNF-α and C2-ceramide. TNF-α, sphingomyelinase, and C2-ceramide translocated Cdc42, Rac, and RhoA to membranes, and stimulated p21-activated protein kinase downstream of Ras-GTP, PI 3-K, and SK. Transfection with inactive RhoA inhibited the TNF-α- and C2-ceramide-induced stress fiber formation. Our results demonstrate that stimulation by TNF-α, which increases sphingomyelinase activity and ceramide formation, activates sphingosine kinase, Rho family GTPases, focal adhesion kinase, and paxillin. This novel pathway of ceramide signaling can account for ∼70% of TNF-α-induced stress fiber formation and cytoskeletal reorganization.

scholarly journals Polymyxin B Alleviates Angiotensin II-Induced Stress Fiber Formation and Cellular Hypertrophy

2014 ◽  
Vol 05 (09) ◽  
pp. 903-910
Author(s):  
Kwang-Seok Oh ◽  
Jeong Hyun Lee ◽  
Byung Koo Oh ◽  
Jihye Mun ◽  
Byung Kil Park ◽  
...  
Keyword(s):  
Angiotensin Ii ◽  
Polymyxin B ◽  
Stress Fiber ◽  
Fiber Formation ◽  
Cellular Hypertrophy ◽  
Stress Fiber Formation ◽  
Induced Stress

Stretch-Induced Stress Fiber Remodeling and MAPK Activations Depend on Mechanical Strain Rate

2011 ◽  
Author(s):  
Hui-Ju Hsu ◽  
Andrea Locke ◽  
Susan Q. Vanderzyl ◽  
Roland Kaunas
Keyword(s):  
Cell Function ◽  
Myosin Ii ◽  
Mechanical Strain ◽  
Optimal Level ◽  
Stress Fiber ◽  
Stress And Strain ◽  
Structural Elements ◽  
Cell Matrix ◽  
Induced Stress ◽  
The Matrix

Actin stress fibers (SFs), bundles of actin filaments crosslinked by α-actinin and myosin II in non-muscle cells, are mechanosensitive structural elements that respond to applied stress and strain to regulate cell morphology, signal transduction and cell function. Results from various studies indicate that myosin-generated contraction extends SFs beyond their unloaded lengths and cells maintain fiber strain at an optimal level that depends on actomyosin activity (Lu et al., 2008). Stretching the matrix upon which cells adhere perturbs the cell-matrix traction forces and cells respond by actively re-establishing the preexisting level of force (Brown et al., 1998; Gavara et al., 2008). We have developed a sarcomeric model of SF networks (Kaunas et al., 2011) to predict the effects of stretch on SF reorganization depending on the rates of matrix stretching, SF turnover, and SF stress relaxation.

scholarly journals Activation of Na+-H+ exchange is necessary for RhoA-induced stress fiber formation.

1996 ◽  
Vol 271 (48) ◽  
pp. 31008
Author(s):  
Zinaida S. Vexler ◽  
Marc Symons ◽  
Diane L. Barber
Keyword(s):  
Stress Fiber ◽  
Fiber Formation ◽  
Stress Fiber Formation ◽  
Induced Stress

scholarly journals Stress fiber growth and remodeling determines cellular morphomechanics under uniaxial cyclic stretch

2019 ◽  
Author(s):  
Aritra Chatterjee ◽  
Paturu Kondaiah ◽  
Namrata Gundiah
Keyword(s):  
Effective Elastic Modulus ◽  
Stress Fiber ◽  
Cyclic Stretch ◽  
Stress Fibers ◽  
Avoidance Reaction ◽  
Cortical Actin ◽  
Fiber Growth ◽  
Induced Stress ◽  
Reorientation Dynamics ◽  
And Migration

AbstractStress fibers in the cytoskeleton are essential in maintaining cellular shape, and influence their adhesion and migration. Cyclic uniaxial stretching results in cellular reorientation orthogonal to the applied stretch direction via a strain avoidance reaction; the mechanistic cues in cellular mechanosensitivity to this response are currently underexplored. We show stretch induced stress fiber lengthening, their realignment and increased cortical actin in fibroblasts stretched over varied amplitudes and durations. Higher amounts of actin and alignment of stress fibers were accompanied with an increase in the effective elastic modulus of cells. Microtubules did not contribute to the measured stiffness or reorientation response but were essential to the nuclear reorientation. We modeled stress fiber growth and reorientation dynamics using a nonlinear, orthotropic, fiber-reinforced continuum representation of the cell. The model predicts the observed fibroblast morphology and increased cellular stiffness under uniaxial cyclic stretch. These studies are important in exploring the differences underlying mechanotransduction and cellular contractility under stretch.

TIS21/BTG2 inhibits doxorubicin-induced stress fiber-vimentin networks via Nox4-ROS-ABI2-DRF-linked signal cascade

2017 ◽  
Vol 30 ◽  
pp. 179-190 ◽  
Author(s):  
In Kyoung Lim ◽  
Jung-A Choi ◽  
Eun Young Kim ◽  
Bit Na Kim ◽  
Soohyun Jang ◽  
...  
Keyword(s):  
Stress Fiber ◽  
Induced Stress ◽  
Signal Cascade

scholarly journals Interplay between Solo and keratin filaments is crucial for mechanical force–induced stress fiber reinforcement

2016 ◽  
Vol 27 (6) ◽  
pp. 954-966 ◽  
Author(s):  
Sachiko Fujiwara ◽  
Kazumasa Ohashi ◽  
Toshiya Mashiko ◽  
Hiroshi Kondo ◽  
Kensaku Mizuno
Keyword(s):  
Tensile Force ◽  
Fiber Reinforcement ◽  
Stress Fiber ◽  
Mechanical Force ◽  
Fiber Formation ◽  
Stress Fibers ◽  
Nucleotide Exchange ◽  
Cellular Mechanisms ◽  
Rhoa Activation ◽  
Induced Stress

Mechanical force–induced cytoskeletal reorganization is essential for cell and tissue remodeling and homeostasis; however, the underlying cellular mechanisms remain elusive. Solo (ARHGEF40) is a RhoA-targeting guanine nucleotide exchange factor (GEF) involved in cyclical stretch–induced human endothelial cell reorientation and convergent extension cell movement in zebrafish gastrula. In this study, we show that Solo binds to keratin-8/keratin-18 (K8/K18) intermediate filaments through multiple sites. Solo overexpression promotes the formation of thick actin stress fibers and keratin bundles, whereas knockdown of Solo, expression of a GEF-inactive mutant of Solo, or inhibition of ROCK suppresses stress fiber formation and leads to disorganized keratin networks, indicating that the Solo-RhoA-ROCK pathway serves to precisely organize keratin networks, as well as to promote stress fibers. Of importance, knockdown of Solo or K18 or overexpression of GEF-inactive or deletion mutants of Solo suppresses tensile force–induced stress fiber reinforcement. Furthermore, knockdown of Solo or K18 suppresses tensile force-induced RhoA activation. These results strongly suggest that the interplay between Solo and K8/K18 filaments plays a crucial role in tensile force–induced RhoA activation and consequent actin cytoskeletal reinforcement.

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