Mechanical communication-associated cell directional migration and branching connections mediated by calcium channels, integrin β1, and N-cadherin

Cell–cell mechanical communications at a large spatial scale (above hundreds of micrometers) have been increasingly recognized in recent decade, which shows importance in tissue-level assembly and morphodynamics. The involved mechanosensing mechanism and resulted physiological functions are still to...

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Main Authors: Mingxing Ouyang, Yiming Zhu, Jiajia Wang, Qingyu Zhang, Yanling Hu, Bing Bu, Jia Guo, Linhong Deng
Format: Article
Language:English
Published: Frontiers Media S.A. 2022-08-01
Series:Frontiers in Cell and Developmental Biology
Subjects:
Online Access:https://www.frontiersin.org/articles/10.3389/fcell.2022.942058/full
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author Mingxing Ouyang
Yiming Zhu
Jiajia Wang
Qingyu Zhang
Yanling Hu
Bing Bu
Jia Guo
Linhong Deng
author_facet Mingxing Ouyang
Yiming Zhu
Jiajia Wang
Qingyu Zhang
Yanling Hu
Bing Bu
Jia Guo
Linhong Deng
author_sort Mingxing Ouyang
collection DOAJ
description Cell–cell mechanical communications at a large spatial scale (above hundreds of micrometers) have been increasingly recognized in recent decade, which shows importance in tissue-level assembly and morphodynamics. The involved mechanosensing mechanism and resulted physiological functions are still to be fully understood. Recent work showed that traction force sensation in the matrix induces cell communications for self-assembly. Here, based on the experimental model of cell directional migration on Matrigel hydrogel, containing 0.5 mg/ml type I collagen, we studied the mechano-responsive pathways for cell distant communications. Airway smooth muscle (ASM) cells assembled network structure on the hydrogel, whereas stayed isolated individually when cultured on glass without force transmission. Cell directional migration, or network assembly was significantly attenuated by inhibited actomyosin activity, or inhibition of inositol 1,4,5-trisphosphate receptor (IP3R) calcium channel or SERCA pump on endoplasmic reticulum (ER) membrane, or L-type calcium channel on the plasma membrane. Inhibition of integrin β1 with siRNA knockdown reduced cell directional migration and branching assembly, whereas inhibition of cell junctional N-cadherin with siRNA had little effect on distant attractions but blocked branching assembly. Our work demonstrated that the endoplasmic reticulum calcium channels and integrin are mechanosensing signals for cell mechanical communications regulated by actomyosin activity, while N-cadherin is responsible for traction force-induced cell stable connections in the assembly.
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spelling doaj.art-2a91fd8295964c109f7bd1857603dac32022-12-22T01:41:29ZengFrontiers Media S.A.Frontiers in Cell and Developmental Biology2296-634X2022-08-011010.3389/fcell.2022.942058942058Mechanical communication-associated cell directional migration and branching connections mediated by calcium channels, integrin β1, and N-cadherinMingxing OuyangYiming ZhuJiajia WangQingyu ZhangYanling HuBing BuJia GuoLinhong DengCell–cell mechanical communications at a large spatial scale (above hundreds of micrometers) have been increasingly recognized in recent decade, which shows importance in tissue-level assembly and morphodynamics. The involved mechanosensing mechanism and resulted physiological functions are still to be fully understood. Recent work showed that traction force sensation in the matrix induces cell communications for self-assembly. Here, based on the experimental model of cell directional migration on Matrigel hydrogel, containing 0.5 mg/ml type I collagen, we studied the mechano-responsive pathways for cell distant communications. Airway smooth muscle (ASM) cells assembled network structure on the hydrogel, whereas stayed isolated individually when cultured on glass without force transmission. Cell directional migration, or network assembly was significantly attenuated by inhibited actomyosin activity, or inhibition of inositol 1,4,5-trisphosphate receptor (IP3R) calcium channel or SERCA pump on endoplasmic reticulum (ER) membrane, or L-type calcium channel on the plasma membrane. Inhibition of integrin β1 with siRNA knockdown reduced cell directional migration and branching assembly, whereas inhibition of cell junctional N-cadherin with siRNA had little effect on distant attractions but blocked branching assembly. Our work demonstrated that the endoplasmic reticulum calcium channels and integrin are mechanosensing signals for cell mechanical communications regulated by actomyosin activity, while N-cadherin is responsible for traction force-induced cell stable connections in the assembly.https://www.frontiersin.org/articles/10.3389/fcell.2022.942058/fullcell mechanical communicationsmechanosensationcalcium channelsintegrinN-cadherin
spellingShingle Mingxing Ouyang
Yiming Zhu
Jiajia Wang
Qingyu Zhang
Yanling Hu
Bing Bu
Jia Guo
Linhong Deng
Mechanical communication-associated cell directional migration and branching connections mediated by calcium channels, integrin β1, and N-cadherin
Frontiers in Cell and Developmental Biology
cell mechanical communications
mechanosensation
calcium channels
integrin
N-cadherin
title Mechanical communication-associated cell directional migration and branching connections mediated by calcium channels, integrin β1, and N-cadherin
title_full Mechanical communication-associated cell directional migration and branching connections mediated by calcium channels, integrin β1, and N-cadherin
title_fullStr Mechanical communication-associated cell directional migration and branching connections mediated by calcium channels, integrin β1, and N-cadherin
title_full_unstemmed Mechanical communication-associated cell directional migration and branching connections mediated by calcium channels, integrin β1, and N-cadherin
title_short Mechanical communication-associated cell directional migration and branching connections mediated by calcium channels, integrin β1, and N-cadherin
title_sort mechanical communication associated cell directional migration and branching connections mediated by calcium channels integrin β1 and n cadherin
topic cell mechanical communications
mechanosensation
calcium channels
integrin
N-cadherin
url https://www.frontiersin.org/articles/10.3389/fcell.2022.942058/full
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