| Literature DB >> 8405375 |
Y Matsunaga1, T Saibara, H Kido, N Katunuma.
Abstract
Cellular and humoral immune responses to vaccines of hepatitis B type and rabies were inhibited by specific inhibitors of cathepsin B, specific synthetic substrates of cathepsin B and anti-cathepsin B antibody. Therefore the lysosomal cathepsin B of antigen presenting cells plays an essential role in processing of these antigens for presentation to MHC class II. One of the active sites of cathepsin B, VN217-222 shares highly homologous sequences with a part of the desetope, a binding domain of antigenic peptides, VN57-62 of MHC class II, beta-chain. This evidence suggests that the peptides processed by the substrate specificity of cathepsin B exhibit a common affinity to bind with the desetope of MHC class II, beta-chain.Entities:
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Year: 1993 PMID: 8405375 DOI: 10.1016/0014-5793(93)80144-j
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124