Abstract
The control of proteolytic enzyme activities in blood and other tissues is exerted, primarily, by nine plasma proteins (1). These inhibitors, which represent more than 10% of the total protein in plasma, have a broad spectrum of regulatory functions in controlling coagulation, fibrinolysis, complement activation, and connective tissue turnover.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
J. Travis and G. S. Salvesen, Human plasma proteinase inhibitors, Ann. Rev. Biochem., in press (1983).
K. Kurachi, T. Chandra, S. J, F. Degen, T. T. White, T. L. Marchiano, S. L. C. Woo, and E. W. Davie, Clonine and sequence of cDNA coding for α1-antitrypsin, Proc. Natl. Acad. Sci. U.S.A. 78: 6826 (1981).
L. Vaughan and R. Carrell, α1-antitrypsin isoforms: Structural basis of microheterogeneity, Biochemistry International 2: 461 (1981).
J. O. Jeppson, Amino acid substitution Glu-Lys in α1 antitrypsin PiZ, FEBS Letters 65: 195 1976.
D. A. Johnson and J. Travis, Structural evidence for methionine at the reactive site of human α1-proteinase inhibitor, J. Biol. Chem. 253: 7142 1978.
K. Beatty, J. Bieth, and J. Travis, Kinetics of association of serine proteinases with native and oxidized α1-proteinase inhibitor and α1-antichymotrypsin, J. Biol. Chem. 255: 3931 1980.
D. A. Johnson and J. Travis, The oxidative inactivation of human α1-proteinase inhibitor. Further evidence for methionine at the reactive center, J. Biol. Chem. 254: 4022 1979.
N. R. Matheson, P. S. Wong, and J. Travis, Enzymatic inactivation of human α1-proteinase inhibitor by neutrophil myeloperoxidase, Biochem. Biophys. Res. Commun. 88: 402 1979.
C. B. Laurell and S. Eriksson, The electrophoretic α1-globulin pattern of serum in a-antitrypsin deficiency, Scand. J. Clin. Lab. Invest. 15: 132 1963.
J. G. Bieth, Pathophysiological interpretation of kinetic constants of protease inhibitors, Bull. Europeen de Physiopath. Respiratoire 15: 183 (1980).
A. Janoff, H. Carp, D. K. Lee, and R. T. Drew, Cigarette smoke inhalation decreases α1-antitrypsin activity in rat lung, Science 206: 1313 1979.
J. E. Gadek, G. A. Fells, and R. G. Crystal, Cigarette smoking induces functional antiprotease deficiency in the lower respiratory tract of humans, Science 206: 1315 1979.
H. Carp, F. Miller, J. R. Hoidal, and A. Janoff, Potential mechanism of emphysema: α1-proteinase inhibitor recovered from lungs of cigarette smokers contains oxidized methionine and has decreased elastase inhibitory capacity, Proc. Natl. Acad. Sci. U.S.A. 79: 2041 (1982).
P. S. Wong and J. Travis, Isolation and properties of oxidized α1-proteinase inhibitor from human rheumatoid synovial fluid. Biochem. Biophys. Res. Commun. 96: 1449 1980.
K. Beatty, P. Robertie, R. M. Senior, and J. Travis, Determination of oxidized α1-proteinase inhibitor in serum. J. Lab. Clin. Med. 100: 186 1982.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1984 Plenum Press, New York
About this chapter
Cite this chapter
Travis, J., Beatty, K., Matheson, N. (1984). Oxidation of Alpha-1-Proteinase Inhibitor: Significance for Pathobiology. In: Hörl, W.H., Heidland, A. (eds) Proteases. Advances in Experimental Medicine and Biology, vol 167. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-9355-3_6
Download citation
DOI: https://doi.org/10.1007/978-1-4615-9355-3_6
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4615-9357-7
Online ISBN: 978-1-4615-9355-3
eBook Packages: Springer Book Archive