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Tytuł pozycji:

Tensile force-induced cytoskeletal remodeling: Mechanics before chemistry.

Tytuł:
Tensile force-induced cytoskeletal remodeling: Mechanics before chemistry.
Autorzy:
Li X; Department of Mathematics and Statistics, Georgia State University, Atlanta, Georgia, United States of America.
Ni Q; Department of Chemical & Biomolecular Engineering, University of Maryland, College Park, Maryland, United States of America.
He X; Department of Mathematics and Statistics, Georgia State University, Atlanta, Georgia, United States of America.
Kong J; Department of Mathematics and Statistics, Georgia State University, Atlanta, Georgia, United States of America.
Lim SM; Department of Medical Physiology, Texas A&M University Health Science Center, Bryan, Texas, United States of America.
Papoian GA; Department of Chemistry & Biochemistry, University of Maryland, College Park, Maryland, United States of America.
Trzeciakowski JP; Department of Medical Physiology, Texas A&M University Health Science Center, Bryan, Texas, United States of America.
Trache A; Department of Medical Physiology, Texas A&M University Health Science Center, Bryan, Texas, United States of America.; Department of Biomedical Engineering, Texas A&M University, College Station, Texas, United States of America.
Jiang Y; Department of Mathematics and Statistics, Georgia State University, Atlanta, Georgia, United States of America.
Źródło:
PLoS computational biology [PLoS Comput Biol] 2020 Jun 10; Vol. 16 (6), pp. e1007693. Date of Electronic Publication: 2020 Jun 10 (Print Publication: 2020).
Typ publikacji:
Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.
Język:
English
Imprint Name(s):
Original Publication: San Francisco, CA : Public Library of Science, [2005]-
MeSH Terms:
Tensile Strength*
Actin Cytoskeleton/*physiology
Actins/physiology ; Animals ; Anisotropy ; Biomechanical Phenomena ; Cells, Cultured ; Computer Simulation ; Fibronectins/physiology ; Image Processing, Computer-Assisted ; Imaging, Three-Dimensional ; Mechanotransduction, Cellular ; Microscopy, Atomic Force ; Myocytes, Smooth Muscle/metabolism ; Myosins/physiology ; Rats ; Stress, Mechanical
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Grant Information:
K25 CA181503 United States CA NCI NIH HHS; U01 CA242936 United States CA NCI NIH HHS; R01 CA201340 United States CA NCI NIH HHS; R01 EY028450 United States EY NEI NIH HHS
Substance Nomenclature:
0 (Actins)
0 (Fibronectins)
EC 3.6.4.1 (Myosins)
Entry Date(s):
Date Created: 20200611 Date Completed: 20200824 Latest Revision: 20210511
Update Code:
20240104
PubMed Central ID:
PMC7326277
DOI:
10.1371/journal.pcbi.1007693
PMID:
32520928
Czasopismo naukowe
Understanding cellular remodeling in response to mechanical stimuli is a critical step in elucidating mechanical activation of biochemical signaling pathways. Experimental evidence indicates that external stress-induced subcellular adaptation is accomplished through dynamic cytoskeletal reorganization. To study the interactions between subcellular structures involved in transducing mechanical signals, we combined experimental data and computational simulations to evaluate real-time mechanical adaptation of the actin cytoskeletal network. Actin cytoskeleton was imaged at the same time as an external tensile force was applied to live vascular smooth muscle cells using a fibronectin-functionalized atomic force microscope probe. Moreover, we performed computational simulations of active cytoskeletal networks under an external tensile force. The experimental data and simulation results suggest that mechanical structural adaptation occurs before chemical adaptation during filament bundle formation: actin filaments first align in the direction of the external force by initializing anisotropic filament orientations, then the chemical evolution of the network follows the anisotropic structures to further develop the bundle-like geometry. Our findings present an alternative two-step explanation for the formation of actin bundles due to mechanical stimulation and provide new insights into the mechanism of mechanotransduction.
Competing Interests: The authors have declared that no competing interests exist.
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