Cathepsin E: A Novel Target for Regulation by Class II Transactivator
pmid: 15100295
Cathepsin E: A Novel Target for Regulation by Class II Transactivator
Abstract The aspartic proteinase cathepsin E (CatE) has been implicated in Ag processing. In this study we report that CatE expression is negatively regulated by the MHC class II transactivator (CIITA). CIITA-deficient murine and human B cells expressed greater CatE than wild-type B cells, whereas overexpression of CIITA in a human gastric carcinoma cell line, AGS, resulted in decreased CatE mRNA and protein. AGS cells expressing CIITA also exhibited decreased processing of OVA Ag. Inhibition of CatE expression is specific to the type III CIITA isoform and maps to the acidic and proline/serine/threonine-rich (PST) protein domains of CIITA. We found that CatE expression is inducible by PU.1 and p300, and that this induction can be reversed by CIITA. These findings demonstrate a novel phenomenon: regulation of CatE Ag processing by CIITA in an isoform-dependent manner.
- University of Michigan–Flint United States
- Indiana University School of Medicine United States
- Indiana University United States
- University of Michigan–Ann Arbor United States
Mice, Knockout, Antigen Presentation, Enzyme Precursors, Ovalbumin, Down-Regulation, Nuclear Proteins, Cathepsin E, Peptide Fragments, Cell Line, Isoenzymes, Mice, Inbred C57BL, Mice, Cell Line, Tumor, Proto-Oncogene Proteins, Animals, Humans, Genes, Tumor Suppressor, Enzyme Repression, E1A-Associated p300 Protein, Cell Line, Transformed
Mice, Knockout, Antigen Presentation, Enzyme Precursors, Ovalbumin, Down-Regulation, Nuclear Proteins, Cathepsin E, Peptide Fragments, Cell Line, Isoenzymes, Mice, Inbred C57BL, Mice, Cell Line, Tumor, Proto-Oncogene Proteins, Animals, Humans, Genes, Tumor Suppressor, Enzyme Repression, E1A-Associated p300 Protein, Cell Line, Transformed
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