Characterization and functional analysis of integrin αV in Sebastes schlegelii: Implications for apoptosis, adhesion, and migration in intestinal cells

Integrins, as essential cell adhesion molecules, consist of an α subunit and a β subunit that interact with extracellular matrix proteins and cell surface ligands to mediate cellular adhesion and signaling. The integrin αV subfamily is widely expressed on the cell surface and plays a critical role in regulating cell growth, apoptosis, and various cellular processes. To explore the function of integrin αV in teleosts, we retrieved the integrin αV (SsITGαV) sequences from the Sebastes schlegelii genome and assessed the tissue expression and response to Edwardsiella tarda stimuli of SsITGαV. We evaluated the effects of SsITGαV in the intestinal cell line on apoptosis, migration, and adhesion using flow cytometry, scratch assays, and cell adhesion experiments by overexpressing and RNA interference methods. The results showed that the coding sequence of SsITGαV comprises 1055 amino acids, containing a signal peptide and a transmembrane domain. SsITGαV is expressed in various tissues, with the highest expression observed in the gill. We investigated the expression pattern of SsITGαV in the head kidney post E. tarda stimulation and observed an increase in its expression. Subcellular localization revealed that SsITGαV predominantly resides in the extracellular matrix. SsITGαV facilitated apoptosis, enhanced cell adhesion, and promoted cell migration in the intestinal cell line. According to the qRT-PCR analysis, alterations in the expression levels of apoptosis-related genes caspase-3, caspase-8, and caspase-10, along with inflammatory factors IL-1 β, IL-6, and IL-8, were positively linked to changes in SsITGαV. These findings provide insights into the function of the integrin αV gene in teleosts, establishing a foundation for further investigation into the role of the integrin α subfamily in lower vertebrates.