Differential distribution of intermediate filament proteins in the bovine and ovine tongues

Abstract

AbstractIntermediate filaments constitute the most heterogeneous class among the major classes of cytoskeletal proteins of mammalian cells. The 40 or more intermediate filament proteins have been classified into five types which show very specific rules of expression in specialized cell types. This study aimed to investigate the immunohistochemical distribution of cytokeratins (CKs) 8, 18, and 19 as well as the intermediate filaments vimentin, laminin, and desmin in bovine and ovine tongues. Immunohistochemical staining was performed for CKs 8, 18, 19, vimentin, laminin, and desmin. Our results revealed similar immunostaining intensity and distribution among various CKs, contrasting with distinct patterns for vimentin, laminin, and desmin. Immunoreactions were primarily localized in serous acini and ductal epithelium for cytokeratins, while vimentin and laminin were evident in connective tissue, endothelium, serous acini, and desmin in striated and smooth muscles. This study highlighted the absence of CKs 8, 18, 19, vimentin, and desmin in the lingual epithelium of bovine and ovine tongues. These findings enabled the classification of epithelial cells based on their specific cytokeratin patterns. Furthermore, vimentin was identified in mesodermal tissues and organs, desmin in muscle tissue, and laminin played crucial roles in basement membrane formation, nerve tissue regeneration, innervation of epithelial taste buds, and tissue separation and connection. Our findings provide essential insights into intermediate filament dynamics at the cellular and tissue levels. They serve as a foundation for future studies using systematic molecular biological techniques in this field.