TY - JOUR
T1 - Cathepsin E in follicle associated epithelium of intestine and tonsils
T2 - localization to M cells and possible role in antigen processing
AU - Finzi, Giovanna
AU - Cornaggia, Matteo
AU - Capella, Carlo
AU - Fiocca, Roberto
AU - Bosi, Federica
AU - Solcia, Enrico
AU - Samloff, I. Michael
PY - 1993/3
Y1 - 1993/3
N2 - A specific rabbit anti-human serum was used selectively to localize the aspartic proteinase cathepsin E to follicle associated epithelium (FAE) of human and rat intestine, including jejunum, ileum, appendix, colon and rectum, as well as of human palatine, pharyngeal and lingual tonsils. Coexpression of class II histocompatibility antigen HLA-DR antigen has been observed in some of the cathepsin E-positive epithelial cells. In addition, cathepsin E has been detected in a few mononuclear cells of intestinal lymphoid structures and tonsils resembling interdigitating reticulum cells of lymph nodes. Another aspartic proteinase, cathepsin D, has been found to be poorly represented in FAE and intensely expressed by macrophages. Electron immunocytochemistry localized cathepsin E to endosomal vesicles and endoplasmic reticulum of M cells in rat and human ileum as well as of M-like cells in human palatine tonsil. The results suggest a possible role of endosomal cathepsin E in the processing of macromolecules and microorganisms transported by M cells and related epithelial cells to mucosal associated lymphoid tissue (MALT).
AB - A specific rabbit anti-human serum was used selectively to localize the aspartic proteinase cathepsin E to follicle associated epithelium (FAE) of human and rat intestine, including jejunum, ileum, appendix, colon and rectum, as well as of human palatine, pharyngeal and lingual tonsils. Coexpression of class II histocompatibility antigen HLA-DR antigen has been observed in some of the cathepsin E-positive epithelial cells. In addition, cathepsin E has been detected in a few mononuclear cells of intestinal lymphoid structures and tonsils resembling interdigitating reticulum cells of lymph nodes. Another aspartic proteinase, cathepsin D, has been found to be poorly represented in FAE and intensely expressed by macrophages. Electron immunocytochemistry localized cathepsin E to endosomal vesicles and endoplasmic reticulum of M cells in rat and human ileum as well as of M-like cells in human palatine tonsil. The results suggest a possible role of endosomal cathepsin E in the processing of macromolecules and microorganisms transported by M cells and related epithelial cells to mucosal associated lymphoid tissue (MALT).
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U2 - 10.1007/BF00269138
DO - 10.1007/BF00269138
M3 - Article
C2 - 8491674
AN - SCOPUS:0027464718
VL - 99
SP - 201
EP - 211
JO - Zeitschrift für Zellforschung und Mikroskopische Anatomie. Abteilung Histochemie
JF - Zeitschrift für Zellforschung und Mikroskopische Anatomie. Abteilung Histochemie
SN - 0948-6143
IS - 3
ER -