Strain-dependent glutathionylation of fibronectin fibers impacts mechano-chemical behavior and primes an integrin switch
Wei Li,
Leandro Moretti,
Xinya Su,
Chiuan-Ren Yeh,
Matthew P. Torres and
Thomas H. Barker ()
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Wei Li: Georgia Institute of Technology
Leandro Moretti: University of Virginia
Xinya Su: Georgia Institute of Technology
Chiuan-Ren Yeh: University of Virginia
Matthew P. Torres: Georgia Institute of Technology
Thomas H. Barker: University of Virginia
Nature Communications, 2024, vol. 15, issue 1, 1-12
Abstract:
Abstract The extracellular matrix (ECM) is a protein polymer network that physically supports cells within a tissue. It acts as an important physical and biochemical stimulus directing cell behaviors. For fibronectin (Fn), a predominant component of the ECM, these physical and biochemical activities are inextricably linked as physical forces trigger conformational changes that impact its biochemical activity. Here, we analyze whether oxidative post-translational modifications, specifically glutathionylation, alter Fn’s mechano-chemical characteristics through stretch-dependent protein modification. ECM post-translational modifications represent a potential for time- or stimulus-dependent changes in ECM structure-function relationships that could persist over time with potentially significant impacts on cell and tissue behaviors. In this study, we show evidence that glutathionylation of Fn ECM fibers is stretch-dependent and alters Fn fiber mechanical properties with implications on the selectivity of engaging integrin receptors. These data demonstrate the existence of multimodal post-translational modification mechanisms within the ECM with high relevance to the microenvironmental regulation of downstream cell behaviors.
Date: 2024
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-52742-3
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DOI: 10.1038/s41467-024-52742-3
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