journal article·2017-11-13

Quantitative Analyses of Dynamic Features of Fibroblasts on Different Protein-Coated Compliant Substrates

Yue Xu, Jing Li, Shuai Zhou, Xuan Tang, Yanli Zhang, Feng Lin, Chunyang Xiong, Chun Yang

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Abstract

Cell response to substrate rigidity, closely related to extracellular matrix protein composition, requires actomyosin-generated contractility. By introducing coefficients describing cell spreading and traction dynamics, and a revised high-resolution traction force microscopy, we analyzed the static and dynamic features of fibroblasts on fibronectin- or collagen- coated stiff or soft substrates. Large cell spreading area and branchlike morphology were more favorable on fibronectin than collagen. Cell spreading on fibronectin-coated substrates was more sensitive to rigidity compared with collagen. Low concentration fibronectin-coated substrate induced more dynamic lamellipodia movement than other conditions. Interestingly, the static average cell traction on high concentration fibronectin-coated stiff and soft substrates showed no difference. However, the lamellipodium traction dynamics was sensitive to rigidity on fibronectin. Particularly, lamellipodia on fibronectin-coated soft substrate performed much higher local traction dynamics compared with other groups. Together, dynamics of cell adhesion and traction are regulated by extracellular matrix protein composition, coupled with substrate rigidity.
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Research context

OpenAlex topics: Cellular Mechanics and Interactions · Tendon Structure and Treatment · Cell Adhesion Molecules Research

SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.

Affiliations

Institute of Biomechanics and Medical Engineering, School of Aerospace Engineering, and ‡Cell Imaging Platform of Protein Research Technology Center, Tsinghua University, Beijing 10084, People’s Republic of China

State Key Laboratory for Turbulence and Complex System, and Department of Mechanics and Engineering Science, College of Engineering, and ⊥Academy for Advanced Interdisciplinary Studies, Peking University, Beijing 100871, People’s Republic of China

Funding

Ministry of Science and Technology of the People's Republic of China · National Natural Science Foundation of China

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