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Examining the Dynamics of Cellular Adhesion and Spreading of Epithelial Cells on Fibronectin During Oxidative Stress
Published on: October 13, 2019
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Phosphorylated fibronectin enhances cell attachment and upregulates mechanical cell functions
Garif Yalak1, Jau-Ye Shiu1, Ingmar Schoen1
1Laboratory of Applied Mechanobiology, Institute of Translational Medicine, Department of Health Sciences and Technology, ETH Zürich, Zurich, Switzerland.
Plos One
|July 11, 2019
Summary
Phosphorylation of fibronectin, a key cell adhesion protein, enhances fibroblast functions like cell spreading and metabolic activity. This discovery offers new strategies for targeting disease and developing cancer markers.
Area of Science:
- Biochemistry
- Cell Biology
- Biomaterials Science
Background:
- Extracellular matrix (ECM) proteins are often phosphorylated, but the functional impact remains largely unknown.
- Fibronectin is a crucial adhesion protein mediating cell-matrix interactions.
Purpose of the Study:
- To investigate how fibronectin phosphorylation influences fibroblast behavior and cellular functions.
- To explore the potential of fibronectin phosphorylation as a biomarker.
Main Methods:
- Controlled in vitro phosphorylation of fibronectin using casein kinase II (CKII).
- Measurement of fibroblast traction forces and strain energy on nanopillar arrays.
- Mass spectrometry analysis of human plasma fibronectin.
Main Results:
- CKII-mediated fibronectin phosphorylation significantly increased fibroblast traction forces and strain energy.
- Enhanced cell spreading and metabolic activity were observed following fibronectin phosphorylation.
- A constitutively phosphorylated site and CKII-inducible phosphorylation sites were identified in fibronectin.
Conclusions:
- Fibronectin phosphorylation directly impacts fundamental cell behaviors.
- These findings suggest novel therapeutic strategies targeting ECM in disease.
- Fibronectin phosphorylation states may serve as diagnostic or prognostic cancer markers.
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