Identification of defensin binding to C1 complement

FEBS Letters

Ganz, Tomas¹  Tseng, Yiou²  Szold, Oded¹  Panyutich, Alexander V.¹  Poon, Pak H.² 

[1] Will Rogers Pulmonary Research Laboratory, University of California at Los Angeles, CA, USA;Department of Chemistry & Biochemistry, University of California at Los Angeles, CA, USA

关键词: Defensin;    C1 complement;    C1 inhibitor;    Inflammation;    α2M;    α-macroglobulin;    C1i;    C1 inhibitor;    HNP;    human neutrophil peptide;    defensins;    NHS;    normal human serum;    NHP;    normal human plasma;    PAGE;    polyacrylamide gel electrophoresis;    r2s2 C1 tetramer;    catalytic subunit of C1;   

DOI  :  10.1016/0014-5793(94)01261-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

In human serum we found strong defensin binding to the complexes of activated C1 complement (C) and C1 inhibitor (C1i). Purified C1q, activated C1 tetramer ( _{2 2}) and C1i did not bind defensin. When ( _{2 2}) was dissociated by EDTA, only the activated C1s (Cs) bound defensin. Binding of defensins to C complement represents a newly recognized bridge between the complement- and phagocyte-mediated host defenses, and a potential mechanism for protecting infected tissue from cytotoxic injury by defensin.

【 授权许可】

Unknown