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Inhibition of neutrophil superoxide production by human plasma α 1 ‐antitrypsin
Author(s) -
Bucurenci Nadia,
Blake David R.,
Chidwick Keith,
Winyard Paul G.
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80156-b
Subject(s) - superoxide , chemistry , respiratory burst , microbiology and biotechnology , serpin , concanavalin a , serine protease , cytochalasin , biochemistry , neutrophile , in vitro , biology , enzyme , protease , cell , gene , cytoskeleton
We report here that human plasma α 1 ‐antitrypsin (α 1 ‐AT) inhibited human neutrophil O 2 − release elicited by a variety of stimulants. In comparison, the inhibitory capacities of two serine protease inhibitors, l ‐1‐tosylamide 2‐phenylethylchloromethyl ketone (TPCK) and soybean trypsin inhibitor (SBTI) and the human recombinant α 1 ‐AT mutant, α 1 ‐AT‐Arg 358 were in the order: α 1 ‐AT ‐ TPCK> α 1 ‐AT‐Arg 358 > SBTI when cells were stimulated with concanavalin A plus cytochalasin E. These data suggest that, in human inflammatory fluks containing relatively high concentrations of α 1 ‐AT (such as rheumatoid arthritis synovial fluids) (i) α 1 ‐AT may down‐regulate the inflammatory process by inhibiting the neurophil respiratory burst and (ii) serpin oxidation by neutrophil‐released oxygen species is unlikely to occur.