BIOMAT Database Logo BIOMAT Database Logo

Kinetics of association of serine proteinases with native and oxidized alpha-1-proteinase inhibitor and alpha-1-antichymotrypsin. 1980

K Beatty, and J Bieth, and J Travis

The association rate constants for the interaction of alpha-1-proteinase inhibitor, oxidized alpha-1-proteinase inhibitor, and alpha-1-antichymotrypsin with several mammalian serine proteinases have been determined. The results indicate that leukocyte elastase reacts more rapidly with alpha-1-proteinase inhibitor than any other proteinase tested, while leukocyte cathepsin G shows the strongest association with alpha-1-antichymotrypsin. Oxidation of the critical methionine residue of alpha-1-proteinase inhibitor reduces the association with leukocyte elastase by a factor of more than 2000 and also lowers the association with all of the other enzymes tested with the exception of chymotrypsin. Significantly, oxidation completely abolishes any interaction of alpha-1-proteinase inhibitor with porcine elastase, human plasmin or human thrombin. These data support previous results (Johnson, D., and Travis, J. (1979) J. Biol. Chem. 254, 4022-4026) which indicated that oxidation of human alpha-1-proteinase inhibitor in vivo could reduce the effectiveness of this inhibitor in controlling proteolysis. In the lung, in particular, oxidizing agents of both chemical and biological sources could, indirectly, augment elastolysis in this tissue, resulting in the development of pulmonary emphysema.

UI MeSH Term Description Entries
D007700 Kinetics The rate dynamics in chemical or physical systems.
D008433 Mathematics The deductive study of shape, quantity, and dependence. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed) Mathematic
D010084 Oxidation-Reduction A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471). Redox,Oxidation Reduction
D010450 Endopeptidases A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS. Endopeptidase,Peptide Peptidohydrolases
D011485 Protein Binding The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. Plasma Protein Binding Capacity,Binding, Protein
D002918 Chymotrypsin A serine endopeptidase secreted by the pancreas as its zymogen, CHYMOTRYPSINOGEN and carried in the pancreatic juice to the duodenum where it is activated by TRYPSIN. It selectively cleaves aromatic amino acids on the carboxyl side. Alpha-Chymotrypsin Choay,Alphacutanée,Avazyme
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000514 alpha 1-Antichymotrypsin Glycoprotein found in alpha(1)-globulin region in human serum. It inhibits chymotrypsin-like proteinases in vivo and has cytotoxic killer-cell activity in vitro. The protein also has a role as an acute-phase protein and is active in the control of immunologic and inflammatory processes, and as a tumor marker. It is a member of the serpin superfamily. Serpin A3,alpha(1)-Antichymotrypsin,alpha 1 Antichymotrypsin
D000515 alpha 1-Antitrypsin Plasma glycoprotein member of the serpin superfamily which inhibits TRYPSIN; NEUTROPHIL ELASTASE; and other PROTEOLYTIC ENZYMES. Trypsin Inhibitor, alpha 1-Antitrypsin,alpha 1-Protease Inhibitor,alpha 1-Proteinase Inhibitor,A1PI,Prolastin,Serpin A1,Zemaira,alpha 1 Antiprotease,alpha 1-Antiproteinase,1-Antiproteinase, alpha,Antiprotease, alpha 1,Inhibitor, alpha 1-Protease,Inhibitor, alpha 1-Proteinase,Trypsin Inhibitor, alpha 1 Antitrypsin,alpha 1 Antiproteinase,alpha 1 Antitrypsin,alpha 1 Protease Inhibitor,alpha 1 Proteinase Inhibitor
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia

Related Publications

K Beatty, and J Bieth, and J Travis
Interaction of horse plasma antithrombin III and alpha 1-proteinase inhibitor with some serine proteinases.
January 1981, Acta biologica et medica Germanica,
K Beatty, and J Bieth, and J Travis
Interaction of mouse macrophage elastase with native and oxidized human alpha 1-proteinase inhibitor.
May 1987, The Journal of clinical investigation,
K Beatty, and J Bieth, and J Travis
Kinetic studies on the interaction of alpha 1-proteinase inhibitor (Pittsburgh) with trypsin-like serine proteinases.
September 1986, Biological chemistry Hoppe-Seyler,
K Beatty, and J Bieth, and J Travis
Effect of serine proteinase inhibitors on neutrophil function: alpha-1-proteinase inhibitor, antichymotrypsin, and a recombinant hybrid mutant of antichymotrypsin (LEX032) modulate neutrophil adhesion interactions.
January 1998, Journal of leukocyte biology,
K Beatty, and J Bieth, and J Travis
Synthesis and release of platelet-activating factor is inhibited by plasma alpha 1-proteinase inhibitor or alpha 1-antichymotrypsin and is stimulated by proteinases.
October 1988, The Journal of experimental medicine,
K Beatty, and J Bieth, and J Travis
Interactions of alpha-1-antichymotrypsin, alpha-1-proteinase inhibitor, and alpha-2-macroglobulin with the fungal enzyme, seaprose.
May 1994, Biological chemistry Hoppe-Seyler,
K Beatty, and J Bieth, and J Travis
Inhibition of human chymotrypsin-like proteases by alpha 1-proteinase inhibitor and alpha 1-antichymotrypsin.
January 1988, Advances in experimental medicine and biology,
K Beatty, and J Bieth, and J Travis
Analysis of the plasma elimination kinetics and conformational stabilities of native, proteinase-complexed, and reactive site cleaved serpins: comparison of alpha 1-proteinase inhibitor, alpha 1-antichymotrypsin, antithrombin III, alpha 2-antiplasmin, angiotensinogen, and ovalbumin.
February 1991, Biochemistry,
K Beatty, and J Bieth, and J Travis
Inactivation of human alpha 1-proteinase inhibitor by thiol proteinases.
June 1977, The Biochemical journal,
K Beatty, and J Bieth, and J Travis
Determination of oxidized alpha-1-proteinase inhibitor in serum.
August 1982, The Journal of laboratory and clinical medicine,
Copied contents to your clipboard!