Depletion of calpain2 accelerates epithelial barrier establishment and reduces growth factor-induced cell scattering

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F24%3A00588259" target="_blank" >RIV/61388971:_____/24:00588259 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/68378050:_____/24:00588259 RIV/00216208:11310/24:10487646

Výsledek na webu

<a href="https://www.sciencedirect.com/science/article/pii/S0898656824002638?via%3Dihub" target="_blank" >https://www.sciencedirect.com/science/article/pii/S0898656824002638?via%3Dihub</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.cellsig.2024.111295" target="_blank" >10.1016/j.cellsig.2024.111295</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Depletion of calpain2 accelerates epithelial barrier establishment and reduces growth factor-induced cell scattering

Popis výsledku v původním jazyce

Calpain2 is a conventional member of the non-lysosomal calpain protease family that has been shown to affect the dynamics of focal and cell-cell adhesions by proteolyzing the components of adhesion complexes. Here, we inactivated calpain2 using CRISPR/Cas9 in epithelial MDCK cells. We show that depletion of calpain2 has multiple effects on cell morphology and function. Calpain2-depleted cells develop epithelial shape, however, they cover a smaller area, and cell clusters are more compact. Inactivation of calpain2 enhanced restoration of transepithelial electrical resistance after calcium switch, decreased cell migration, and delayed cell scattering induced by HGF/SF. In addition, calpain2 depletion prevented morphological changes induced by ERK2 overexpression. Interestingly, proteolysis of several calpain2 targets, including E-cadherin, I3-catenin, talin, FAK, and paxillin, was not discernibly affected by calpain2 depletion. Taken together, these data suggest that calpain2 regulates the stability of cell-cell and cell-substratum adhesions indirectly without affecting the proteolysis of these adhesion complexes.

Název v anglickém jazyce

Depletion of calpain2 accelerates epithelial barrier establishment and reduces growth factor-induced cell scattering

Popis výsledku anglicky

Calpain2 is a conventional member of the non-lysosomal calpain protease family that has been shown to affect the dynamics of focal and cell-cell adhesions by proteolyzing the components of adhesion complexes. Here, we inactivated calpain2 using CRISPR/Cas9 in epithelial MDCK cells. We show that depletion of calpain2 has multiple effects on cell morphology and function. Calpain2-depleted cells develop epithelial shape, however, they cover a smaller area, and cell clusters are more compact. Inactivation of calpain2 enhanced restoration of transepithelial electrical resistance after calcium switch, decreased cell migration, and delayed cell scattering induced by HGF/SF. In addition, calpain2 depletion prevented morphological changes induced by ERK2 overexpression. Interestingly, proteolysis of several calpain2 targets, including E-cadherin, I3-catenin, talin, FAK, and paxillin, was not discernibly affected by calpain2 depletion. Taken together, these data suggest that calpain2 regulates the stability of cell-cell and cell-substratum adhesions indirectly without affecting the proteolysis of these adhesion complexes.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10601 - Cell biology

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2024

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Cellular Signalling

ISSN

0898-6568

e-ISSN

1873-3913

Svazek periodika

121

Číslo periodika v rámci svazku

September 2024

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

9

Strana od-do

111295

Kód UT WoS článku

001271754400001

EID výsledku v databázi Scopus

2-s2.0-85198270418