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Cyclophilin A is a new M cell marker of bovine intestinal epithelium
journal contributionposted on 2023-05-20, 07:32 authored by Hondo, T, Someya, S, Nagasawa, Y, Terada, S, Watanabe, H, Chen, X, Watanabe, K, Ohwada, S, Kitazawa, H, Michael RoseMichael Rose, Nochi, T, Aso, H
Microfold (M) cells in the follicle-associated epithelium (FAE) of Peyerâ€™s patches contribute to the mucosal immune response by the transcytosis of microorganisms. The mechanism by which M cells take up microorganisms, and the functional proteins by which they do this, are not clear. In order to explore one such protein, we developed a 2H5-F3 monoclonal antibody (2H5-F3 mAb) through its binding to bovine M cells, and identified the antibody reactive molecule as cyclophilin A (Cyp-A). The localization patterns of Cyp-A were very similar to the localization pattern of cytokeratin (CK) 18-positive M cells. Cyp-A was identified at the luminal surface of CK18-positive M cells in bovine jejunal and ileal FAE. The membranous localization of Cyp-A in the bovine intestinal cell line (BIE cells) increased as cells differentiated toward M cells, as determined by flow cytometry analysis. Additionally, BIE cells released Cyp-A to the extracellular space and the differentiation of BIE cells to M cells increased the secretion of Cyp-A, as determined by western blotting. Accordingly, Cyp-A may be localized in M cells in the small intestinal epithelium of cattle. The rise of the membranous localization and secretion of Cyp-A by differentiation toward M cells indicates that Cyp-A has an important role in the function of M cells. While Cyp-A of the M cell membrane may contribute to the uptake of viruses with peptidyl-prolyl cis-trans isomerase activity, in the extracellular space Cyp-A may work as a chemokine and contribute to the distribution of immuno-competent cells.
Publication titleCell and Tissue Research
Department/SchoolTasmanian Institute of Agriculture (TIA)
Place of publication175 Fifth Ave, New York, USA, Ny, 10010
Rights statementCopyright 2016 Springer-Verlag Berlin Heidelberg