Abstract
S. aureus serine proteinase inactivates human α-1-proteinase inhibitor (α-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 α-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.
Similar content being viewed by others
References
Arvidson SO (1983) Extracellular enzymes from Staphylococcus aureus. In: Jeliaszewicz J (Ed) Staphylococci and Staphylococcal Infections 2 (pp 745–808) Academic Press Inc., London
Banda JM, Rice AG, Griffin GL & Senior RM (1988a) α-1-proteinase inhibitor is a neutrophil chemoattractant after proteolytic inactivation by macrophage elastase. J. Biol. Chem. 263: 4481–4484
Banda JM, Rice AG, Griffin GL & Senior RM (1988b) The inhibitory complex of human α-1-proteinase inhibitor and human leukocyte elastase is a neutrophil chemoattractant. J. Exp. Med. 167: 1608–1615
Baran K, Miedzobrodzki J & Porwit-Bobr Z (1988) Preliminary estimation of chemoattractant activity of staphylococcal serine proteinase in vitro. Chemoattractant activity of staphylococcal serine proteinase. Antonie van Leeuwenhoek J Microbiol. 54: 85–87
Boxer LA & Smolen JE (1988) Neutrophil granule constituents and their release in health and disease. Hematol. Oncol. Clin. N. America 2: 101–134
Cates RW, Ray CE & Quie PG (1978) Modified Boyden chambers method of measuring polymorphonuclear leukocyte chemotaxis. In: Gallin JI & Quie PG (Eds) Leukocyte Chemotaxis (pp 76–71) Raven Press
Cates KL & Quie PG (1979) Neutrophil chemotaxis in patients with Staphyloccocus aureus furunculosis. Infect. Immun. 26: 1004–1008
Carrell RW & Owen M (1985) Plakalbumin, α-1-antitrypsin, antithrombin and the mechanism of inflammatory thrombosis. Nature 317: 730–732
Loebermann H, Tokuoka R, Deisenhofer J & Huber R (1984) Human α-1-proteinase inhibitor. Crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function. J. Mol. Biol. 177: 531–556
Potempa J, Watorek W & Travis J (1986) The inactivation of human plasma α-1-proteinase inhibitor by proteinases from Staphylococcus aureus. J. Biol. Chem. 261: 14330–14334
Potempa J, Dubin A, Watorek W & Travis J (1988) An elastase inhibitor from equine leukocytes cytosol belongs to the serpin superfamily. Further characterization and amino sequence of the reactive center. J. Biol. Chem. 263: 7364–7369
Russell RJ, Wilkinson PC, McInroy RJ, McKay AC, McCartney AC & Arbuthnott JP (1976) Effect of staphylococcal products on locomotion and chemotaxis of human blood neutrophils and monocytes. J. Med. Microbiol. 8: 433–439
Swain M & Pizzo SV (1988) Methionone sulphoxide and the oxidative regulation of plasma proteinase inhibitors. J. Leukocyte Biol. 43: 365–379
Travis J & Salvesen GS (1983) Human plasma proteinase inhibitors. Annu. Rev. Biochem. 52: 655–709
Tylski S, Tylawska S, Hryniewicz W & Jeliaszewicz J (1987) Induction of human neurtophil chemotaxis by staphylococal lipase. Zbl. Bakt. Hyg. A265: 360–368
Weitz JI, Huang AJ, Landman SL, Nicholson SC & Silverstein SC (1987) Elastase-mediated fibrinogenolysis by chemoattractant-stimulated neutrophils occurs in the presence of physiologic concentrations of antiproteinases. J. Exp. Med. 66: 1836–1850
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Baran, K., Górka, M., Potempa, J. et al. Chemoattractant activity of Staphylococcus aureus serine proteinase modified human plasma α-1-proteinase inhibitor. Antonie van Leeuwenhoek 56, 361–365 (1989). https://doi.org/10.1007/BF00443750
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF00443750