{Reference Type}: Journal Article
{Title}: Depletion of calpain2 accelerates epithelial barrier establishment and reduces growth factor-induced cell scattering.
{Author}: Rasl J;Caslavsky J;Grusanovic J;Chvalova V;Kosla J;Adamec J;Grousl T;Klimova Z;Vomastek T;
{Journal}: Cell Signal
{Volume}: 121
{Issue}: 0
{Year}: 2024 Sep 10
{Factor}: 4.85
{DOI}: 10.1016/j.cellsig.2024.111295
{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, β-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.