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Papers In Press, published online ahead of print November 21, 2001
Laboratory of Oral Aging Science, Kyushu University, Fukuoka 812-8582
Corresponding Author: nakandeg{at}mbox.nc.kyushu-u.ac.jp
We have attempted to elucidate an involvement of cathepsin E (CE) in major histocompatibility complex (MHC) class II-mediated antigen presentation by microglia. In primary cultured murine microglia, CE was localized mainly in early endosomes and its expression level was markedly increased upon stimulation with interferon (INF)-g. Pepstatin A, a specific inhibitor of aspartic proteases, significantly inhibited interleukin-2 production from an OVA267-282 specific Th cell hybridomas upon stimulation with native OVA presented by IFN-g -treated microglia. However, pepstatin A failed to inhibit the presentation of OVA267-282 peptide. The possible involvement of CE in the processing of native OVA into antigenic peptide was further substantiated by that digested fragments of native OVA by CE could be recognized by OVA-specific Th cells. Cathepsin D (CD) also degraded native OVA into antigenic peptide, whereas microglia prepared from CD-deficient mice retained an ability for antigen presentation. On the other hand, the requirement for cystein proteases such as cathepsins S and B in the processing of invariant chain (Ii) was confirmed by immunoblot analyses in the presence of their specific inhibitors. In conclusion, CE is required for the generation of an antigenic epitope from OVA but not for the processing of Ii in microglia.
J. Biol. Chem, 10.1074/jbc.M108382200
Submitted on August 30, 2001
Revised on November 8, 2001
Accepted on November 21, 2001
Involvement of cathepsin E in exogenous antigen processing in primary cultured murine microglia
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