Impaired immunoproteasome assembly and immune responses in PA28 super(-/-) mice

In vitro PA28 binds and activates proteasomes. It is shown here that mice with a disrupted PA28b gene lack PA28a and PA28b polypeptides, demonstrating that PA28 functions as a hetero-oligomer in vivo. Processing of antigenic epitopes derived from exogenous or endogenous antigens is altered in PA28 s...

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Published inScience (American Association for the Advancement of Science) Vol. 286; no. 5447; pp. 2162 - 2165
Main Authors Preckel, T, Fung-Leung, Wai-Ping, Cai, Z, Vitiello, A, Salter-Cid, L, Winqvist, O, Wolfe, T G, Von Herrath, M, Angulo, A, Ghazal, P, Lee, Jiing-Dwan, Fourie, A M, Wu, Ying, Yang, Young
Format Journal Article
LanguageEnglish
Published 10.12.1999
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Summary:In vitro PA28 binds and activates proteasomes. It is shown here that mice with a disrupted PA28b gene lack PA28a and PA28b polypeptides, demonstrating that PA28 functions as a hetero-oligomer in vivo. Processing of antigenic epitopes derived from exogenous or endogenous antigens is altered in PA28 super(-/-) mice. Cytotoxic T lymphocyte responses are impaired, and assembly of immunoproteasomes is greatly inhibited in mice lacking PA28. These results show that PA28 is necessary for immunoproteasome assembly and is required for efficient antigen processing, thus demonstrating the importance of PA28-mediated proteasome function in immune responses.
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ISSN:0036-8075
DOI:10.1126/science.286.5447.2162