Interleukin‐8 processing by neutrophil elastase, cathepsin G and proteinase‐3

FEBS Letters

Walz, Alfred¹  Baggiolini, Marco¹  Padrines, Marc¹  Wolf, Marlene¹ 

[1] Theodor-Kocher Institute, University of Bern, PO Box, CH-3000 Bern 9, Switzerland

关键词: IL-8;    Chemokine;    Neutrophil activation;    Neutrophil proteinase;    Processing;    HPLC;    high-performance liquid chromatography;    PAGE;    polyacrylamide gel electrophoresis;    PBS;    phosphate-buffered saline. IL-8(72);    IL-8(70);    N-terminally truncated forms of IL-8 with 77;    72 and 70 amino acids;    respectively;   

DOI  :  10.1016/0014-5793(94)00952-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Activated neutrophils secrete two forms of IL-8 with 77 and 72 amino acids, IL-8(77) and IL-8(72), along with proteinases that could process these cytokines. Significant conversion of IL-8(77) to more potent, N-terminally truncated forms was observed upon incubation with neutrophil granule lysates and purified proteinase-3. IL-8(72) was considerably more resistant to proteolytic processing than IL-8(77). The present observations indicate that neutrophil proteinases released in inflamed tissues convert IL-8 to more active forms and therefore tend to conserve or enhance, rather than decrease IL-8 activity.

【 授权许可】

Unknown