Identification of defensin binding to C1 complement

In human serum we found strong defensin binding to the complexes of activated C1 complement (C 1 ) and C1 inhibitor (C1i). Purified C1q, activated C1 tetramer ( r 2 s 2) and C1i did not bind defensin. When ( r 2 s 2) was dissociated by EDTA, only the activated C1s (C 1 s) bound defensin. Binding of...

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Veröffentlicht in:	FEBS letters 1994-12, Vol.356 (2), p.169-173
Hauptverfasser:	Panyutich, Alexander V., Szold, Oded, Poon, Pak H., Tseng, Yiou, Ganz, Tomas
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Autoradiography Blood Proteins - drug effects Blood Proteins - isolation & purification Blood Proteins - metabolism C1 complement C1 inhibitor C1i, C1 inhibitor Calcium - pharmacology Complement C1 - isolation & purification Complement C1 - metabolism Complement C1q - isolation & purification Complement C1q - metabolism Defensin Defensins Edetic Acid HNP, human neutrophil peptide, defensins Humans Immunoblotting Immunoglobulin G Inflammation Iodine Radioisotopes Macromolecular Substances Neutrophils - physiology NHP, normal human plasma NHS, normal human serum PAGE, polyacrylamide gel electrophoresis Protein Binding r2s2 C1 tetramer, catalytic subunit of C1 Reference Values Swine α2M, α-macroglobulin
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Zusammenfassung:	In human serum we found strong defensin binding to the complexes of activated C1 complement (C 1 ) and C1 inhibitor (C1i). Purified C1q, activated C1 tetramer ( r 2 s 2) and C1i did not bind defensin. When ( r 2 s 2) was dissociated by EDTA, only the activated C1s (C 1 s) bound defensin. Binding of defensins to C 1 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.
ISSN:	0014-5793 1873-3468
DOI:	10.1016/0014-5793(94)01261-X