Related Experiment Video
Updated: Apr 3, 2026

A Novel Stretching Platform for Applications in Cell and Tissue Mechanobiology
Published on: June 3, 2014
Rheological behavior of actin stress fibers in myoblasts after nanodissection: Effects of oxidative stress
Zili Ma1, Yiqian Shirley Wu2, Arthur F T Mak1,2,3
1Department of Electronic Engineering, The Chinese University of Hong Kong, Hong Kong, China.
Background:
Cytoskeletal stress fibers (SFs) play important roles in cell rheology. Oxidative stress, as caused by excessive hydrogen peroxide (H2O2) or other reactive oxygen species, can cause cell damages via multiple pathways. Stress fiber mechanics in an oxidative environment is important for the understanding of such pathological challenges.
Objective:
This investigation aimed to assess the effects of oxidative stress on the mechanical conditions of single stress fibers in living cells.
Methods:
Utilizing a femtosecond (fs) laser to sever single SFs inside living C2C12 myoblasts, we investigated the retraction rheology of the severed single SFs to probe the mechanical conditions of the cells and the effect of H2O2 on them.
Results:
The equilibration time of the retraction of the severed SFs became longer in the H2O2-treated myoblasts compared to the control. The initial gap between the two severed ends of the SF immediately after fs laser severing was larger in the H2O2-treated groups. This suggested that H2O2 exposure could promote the pre-stress in individual SFs in-situ.
Conclusion:
Oxidative stress could significantly affect the mechanical conditions of cytoskeletal SFs in myoblasts. The results were consistent with cell stiffness measured on single myoblasts under oxidative stress.
Related Concept Videos
Actin Filament Depolymerization
In F-actin, the ADF/cofilin proteins...
Studying the Cytoskeleton
The Role of Actin and Myosin in Non-muscle Cells
Actin Treadmilling
Generation of Straight or Branched Actin Filaments
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...

