Depletion of calpain2 accelerates epithelial barrier establishment and reduces growth factor-induced cell scattering.
Cell Signal
; 121: 111295, 2024 Sep.
Article
de En
| MEDLINE
| ID: mdl-38996955
ABSTRACT
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, ß-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.
Mots clés
Texte intégral:
1
Collection:
01-internacional
Base de données:
MEDLINE
Sujet principal:
Calpain
/
Adhérence cellulaire
/
Cellules épithéliales
Limites:
Animals
Langue:
En
Journal:
Cell Signal
Année:
2024
Type de document:
Article
Pays d'affiliation:
République tchèque
Pays de publication:
Royaume-Uni