0588259 - MBÚ 2025 RIV NL eng J - Článek v odborném periodiku
Rasl, Jan - Čáslavský, Josef - Grušanovič, Josipa - Chvalová, Věra - Kosla, Jan - Adamec, J. - Groušl, Tomáš - Klímová, Zuzana - Vomastek, Tomáš
Depletion of calpain2 accelerates epithelial barrier establishment and reduces growth factor-induced cell scattering.
Cellular Signalling. Roč. 121, September 2024 (2024), č. článku 111295. ISSN 0898-6568. E-ISSN 1873-3913
Grant CEP: GA ČR(CZ) GA19-08013S; GA MZd(CZ) NU23-03-00557; GA MŠMT(CZ) LM2023050
Grant ostatní: AV ČR(CZ) StrategieAV21/33
Program: StrategieAV
Institucionální podpora: RVO:61388971 ; RVO:68378050
Klíčová slova: mediated proteolysis * focal adhesion * integrin engagement * adherens junctions * crystal-structure * plasma-membrane * beta-catenin * mu-calpain * e-cadherin * kinase * Calpains * Proteases * Epithelial polarity * Transepithelial electrical resistance * Tight junctions * Actin * Adherens junctions * Focal adhesions * erk * Migration * Cell scattering * hgf/sf
Obor OECD: Cell biology; Cell biology (UMG-J)
Impakt faktor: 4.4, rok: 2023 ; AIS: 1.012, rok: 2023
Způsob publikování: Omezený přístup
Web výsledku:
https://www.sciencedirect.com/science/article/pii/S0898656824002638?via%3DihubDOI: https://doi.org/10.1016/j.cellsig.2024.111295

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.
Trvalý link: https://hdl.handle.net/11104/0355679