
doi: 10.1007/bf00443750
pmid: 2619289
S. aureus serine proteinase inactivates human alpha-1-proteinase inhibitor (alpha-1-PI) by attacking a single peptide bond between Glu354 and Ala355 giving a modified inhibitor which is a tight complex of Mr = 4,000 and 48,000 fragments. In the present paper we show that this proteolytically inactivated alpha-1-PI is a potent chemotactic factor for human neutrophiles at a nanomolar concentration, and we discuss its potential involvement in the inflammatory reaction due to S. aureus infections.
Chemotaxis, Leukocyte, Staphylococcus aureus, Neutrophils, alpha 1-Antitrypsin, Serine Endopeptidases, Dose-Response Relationship, Immunologic, Humans, Staphylococcal Infections
Chemotaxis, Leukocyte, Staphylococcus aureus, Neutrophils, alpha 1-Antitrypsin, Serine Endopeptidases, Dose-Response Relationship, Immunologic, Humans, Staphylococcal Infections
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