| First Author | Chain BM | Year | 2005 |
| Journal | J Immunol | Volume | 174 |
| Issue | 4 | Pages | 1791-800 |
| PubMed ID | 15699105 | Mgi Jnum | J:289041 |
| Mgi Id | MGI:6436231 | Doi | 10.4049/jimmunol.174.4.1791 |
| Citation | Chain BM, et al. (2005) The expression and function of cathepsin E in dendritic cells. J Immunol 174(4):1791-800 |
| abstractText | Cathepsin E is an aspartic proteinase that has been implicated in Ag processing within the class II MHC pathway. In this study, we document the presence of cathepsin E message and protein in human myeloid dendritic cells, the preeminent APCs of the immune system. Cathepsin E is found in a perinuclear compartment, which is likely to form part of the endoplasmic reticulum, and also a peripheral compartment just beneath the cell membrane, with a similar distribution to that of Texas Red-dextran within 2 min of endocytosis. To investigate the function of cathepsin E in processing, a new soluble targeted inhibitor was synthesized by linking the microbial aspartic proteinase inhibitor pepstatin to mannosylated BSA via a cleavable disulfide linker. This inhibitor was shown to block cathepsin D/E activity in cell-free assays and within dendritic cells. The inhibitor blocked the ability of dendritic cells from wild-type as well as cathepsin D-deficient mice to present intact OVA, but not an OVA-derived peptide, to cognate T cells. The data therefore support the hypothesis that cathepsin E has an important nonredundant role in the class II MHC Ag processing pathway within dendritic cells. |
