Evolutionary Dynamics of Matrix Metalloproteases with Collagenolytic Activity in Teleosts

Matrix metalloproteases (MMPs) are zinc-dependent endopeptidases that are critical for extracellular matrix (ECM) remodeling, with key roles in tissue development and repair, and immune responses. Despite their evolutionary and functional importance, the diversification and regulatory dynamics of MMPs genes in teleosts remain poorly understood. This study investigates the evolutionary history of MMPs with collagenolytic activity in the vertebrates with an emphasis on teleosts. Using comparative genomics and phylogenetics we identified conserved single-copy <i>mmp2</i> and <i>mmp9</i> genes and duplicated <i>mmp11</i> and <i>mmp13</i> paralogs in all non-salmonid teleosts. Phylogenetic and synteny analyses suggest that <i>mmp11</i> paralogs originated from the teleost-specific genome duplication (TSGD), whereas the origin of <i>mmp13</i> paralogs originated from a more complex evolutionary scenario. Protein domain analysis confirmed conserved catalytic motifs across species, supporting functional retention. The expression patterns of paralog genes were studied in two model marine teleosts, the <i>Sparus aurata</i> (gilthead sea bream) and <i>Dicentrarchus labrax</i> (European sea bass). Developmental and adult tissue transcriptome analyses revealed three major expression patterns among the paralogs: similar expression, stage-specific or tissue-specific expression. The overall data point to varied evolutionary dynamics of <i>MMP</i> genes in the teleosts, tracing their origin to different whole-genome duplication events. Expression profiles on paralog genes in model teleosts suggest regulatory sub-functionalization as the most possible fate of retained MMPs paralogs in teleosts following whole-genome duplication.