Chemoattractant activity of Staphylococcus aureus serine proteinase modified human plasma alpha-1-proteinase inhibitor.
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.
Baran
K
K
Department of Microbiology and Immunology, Jan Zurzycki Institute of Molecular Biology, Jagiellonian University, Cracow, Poland.
Górka
M
M
Potempa
J
J
Porwit-Bóbr
Z
Z
D002634:Chemotaxis, Leukocyte / Q000187:drug effects*; D004306:Dose-Response Relationship, Immunologic; D006801:Humans; D009504:Neutrophils / Q000276:immunology; D012697:Serine Endopeptidases / Q000378:metabolism*; D013203:Staphylococcal Infections / Q000276:immunology; D013211:Staphylococcus aureus / Q000201:enzymology*; D000515:alpha 1-Antitrypsin / Q000378:metabolism*
D000515:alpha 1-Antitrypsin; D012697:Serine Endopeptidases