Akademik Veri Yönetim Sistemi
World Immune Regulation Meeting XVIIl, Zürich, İsviçre, 13 - 16 Mart 2024, cilt.18, sa.16, ss.39
Bovine beta-casein A2 milk is gaining popularity, within producers and consumers showing a growing preference for its production. At the beta-casein locus, alleles A1 and A2 differ at amino acid position 67, where A1 encodes histidine, and A2 encodes proline. The digestion of A1 beta-casein results in the production of beta-casomorphin (BCM)-7, a bioactive peptide with morphine-like activity. This study aims to comprehensively examine the impact of BCM-7 and BCM-9, which are bioactive peptides resulting from the digestion of A1 and A2 milk, respectively, on the gut epithelial barrier. A microfluidic guton- a-chip plate was utilized to streamline the formation of a tubular barrier using Caco-2 cells, enabling the evaluation of the effects of BCMs on the gut epithelial cells and their barrier. Following cytotoxicity assessment, transepithelial electrical resistance (TER) measurement, paracellular permeability assay, wound healing assay, targeted proteomics using proximity extension assay, and RNA sequencing were performed. Caco-2 monolayer cultures did not exhibit cytotoxic effects upon exposure to Bovine BCM-7 and BCM-9. Moreover, no significant findings were observed in the targeted proteomics assessment in two panels consisting 182 inflammation and immune response related proteins with the proximity extension assay. However, our RNA sequencing investigations revealed a unique and fascinating finding: the introduction of Bovine BCM-7 (20ug/ml) resulted in a notable variation in transcriptomic outcomes. Pathway analysis highlighted pathways associated with cellular metabolism and biogenesis, encompassing signal transduction, organelle organization and biogenesis, cytoskeleton, and microtubule organization, as well as cell cycle checkpoints. Taken together, while BCM-7 showed significant differences in transcriptomic profiling, BCM-9 displayed an inactive nature to Caco2 cells.