Journal
JOURNAL OF BIOMEDICINE AND BIOTECHNOLOGY
Volume -, Issue -, Pages -Publisher
HINDAWI LTD
DOI: 10.1155/2010/915234
Keywords
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Funding
- National Natural Science Foundation of China [30670411]
- Eleventh Five-year Plan of PLA [06H027]
- Natural Science Foundation of Chongqing (CSCT) [2008BB5022]
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HMGB1, composed of the A box, B box, and C tail domains, is a critical proinflammatory cytokine involved in diverse inflammatory diseases. The B box mediates proinflammatory activity, while the A box alone acts as a specific antagonist of HMGB1. The C tail contributes to the spatial structure of A box and regulates HMGB1 DNA binding specificity. It is unknown whether the C tail can enhance the anti-inflammatory effect of A box. In this study, we generated fusion proteins consisting of the A box and C tail, in which the B box was deleted and the A box and C tail were linked either directly or by the flexible linker sequence (Gly(4)Ser)(3). In vitro and in vivo experiments showed that the two fusion proteins had a higher anti-inflammatory activity compared to the A box alone. This suggests that the fused C tail enhances the anti-inflammatory effect of the A box.
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