The nuclear protein HMGB1, a new kind of chemokine?

FEBS Letters

de Virgilio, Maddalena¹  Degryse, Bernard¹ 

[1]Department of Cell Biology, Division of Vascular Biology/VB5, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92130, USA

关键词: Chemokine;    Inflammation;    Cell migration;    HMGB1;    Urokinase;    Urokinase receptor;    Macrophage migration inhibitory factor;    C5a;    S19;    Thioredoxin;    7TM-R;    seven-transmembrane domain receptor;    C5aR;    C5a receptor;    ECM;    extracellular matrix;    HMGB;    high mobility group box;    IL;    interleukin;    IL-6R;    IL-6 α-receptor subunit;    LPS;    lipopolysaccharides;    MEL;    murine erythroleukemia;    MIF;    macrophage migration inhibitory factor;    PA;    plasminogen activator;    PT;    pertussis toxin;    RAGE;    receptor for advanced glycation endproducts;    RP S19d;    ribosomal protein S19 dimer;    SMC;    smooth muscle cells;    Trx;    thioredoxin;    uPA;    urokinase;    uPAR;    urokinase receptor;   

DOI  :  10.1016/S0014-5793(03)01027-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The chromosomal protein HMGB1 is now regarded as a proinflammatory cytokine. Importantly, HMGB1 has chemotactic activity suggesting its involvement in the early and late events of the inflammatory reaction. Therefore, HMGB1 has all the hallmarks of a chemokine (chemotactic cytokine). We propose to classify HMGB1 into a new group of proteins unrelated structurally to chemokines but having chemokine-like functions, and to name this class CLF (chemokine-like functions). The CLF class should include other unrelated molecules such as urokinase and its receptor, cytokines macrophage migration inhibitory factor (MIF) and interleukin (IL)-6, anaphylatoxin C5a, ribosomal protein S19, and thioredoxin that have similar chemokine-like activities. This innovative concept may lead to the identification of new therapeutic targets.

【 授权许可】

Unknown