BIOMAT Database Logo BIOMAT Database Logo

alpha 1-Microglobulin destroys the proteinase inhibitory activity of alpha 1-inhibitor-3 by complex formation. 1995

C Falkenberg, and M Allhorn, and I B Thøgersen, and Z Valnickova, and S V Pizzo, and G Salvesen, and B Akerström, and J J Enghild
Department of Medical and Physiological Chemistry, University of Lund, Sweden.

The immunoregulatory plasma protein alpha 1-microglobulin (alpha 1-m) and the proteinase inhibitor alpha 1-inhibitor-3 (alpha 1I3) form a complex in rat plasma. In the present work, it was demonstrated that the alpha 1I3.alpha 1-m complex has no inhibitory activity, the bait region was not cleaved by low amounts of proteinases, and it was unable to covalently incorporate proteinases. The results also indicated that the thiolester bond of the alpha 1I3.alpha 1-m complex was broken. The alpha 1I3.alpha 1-m complex was cleared from the circulation much faster than native alpha 1I3, with a half-life of approximately 7 min. Structurally, however, the alpha 1I3.alpha 1-m complex was similar to native alpha 1I3 rather than alpha 1I3 cleaved by proteinases. It is speculated that the role of alpha 1-m is to destroy the function of alpha 1I3 by blocking the bait region and breaking the thiolester and causing its physical elimination by rapid clearing from the blood circulation. It is also possible that the formation of complexes between alpha 1-m and alpha 1I3 may serve as a mean to regulate the function of alpha 1-m since its complex with alpha 1I3 is taken up rapidly by cellular receptors for alpha-macroglobulins.

UI MeSH Term Description Entries
D008744 Methylamines Derivatives of methylamine (the structural formula CH3NH2).
D008968 Molecular Conformation The characteristic three-dimensional shape of a molecule. Molecular Configuration,3D Molecular Structure,Configuration, Molecular,Molecular Structure, Three Dimensional,Three Dimensional Molecular Structure,3D Molecular Structures,Configurations, Molecular,Conformation, Molecular,Conformations, Molecular,Molecular Configurations,Molecular Conformations,Molecular Structure, 3D,Molecular Structures, 3D,Structure, 3D Molecular,Structures, 3D Molecular
D011480 Protease Inhibitors Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES). Antiprotease,Endopeptidase Inhibitor,Endopeptidase Inhibitors,Peptidase Inhibitor,Peptidase Inhibitors,Peptide Hydrolase Inhibitor,Peptide Hydrolase Inhibitors,Peptide Peptidohydrolase Inhibitor,Peptide Peptidohydrolase Inhibitors,Protease Antagonist,Protease Antagonists,Antiproteases,Protease Inhibitor,Antagonist, Protease,Antagonists, Protease,Hydrolase Inhibitor, Peptide,Hydrolase Inhibitors, Peptide,Inhibitor, Endopeptidase,Inhibitor, Peptidase,Inhibitor, Peptide Hydrolase,Inhibitor, Peptide Peptidohydrolase,Inhibitor, Protease,Inhibitors, Endopeptidase,Inhibitors, Peptidase,Inhibitors, Peptide Hydrolase,Inhibitors, Peptide Peptidohydrolase,Inhibitors, Protease,Peptidohydrolase Inhibitor, Peptide,Peptidohydrolase Inhibitors, Peptide
D004952 Esters Compounds derived from organic or inorganic acids in which at least one hydroxyl group is replaced by an –O-alkyl or another organic group. They can be represented by the structure formula RCOOR’ and are usually formed by the reaction between an acid and an alcohol with elimination of water. Ester
D000209 Acute-Phase Proteins Proteins that are secreted into the blood in increased or decreased quantities by hepatocytes in response to trauma, inflammation, or disease. These proteins can serve as inhibitors or mediators of the inflammatory processes. Certain acute-phase proteins have been used to diagnose and follow the course of diseases or as tumor markers. Acute Phase Reactant,Acute-Phase Glycoprotein,Acute-Phase Reactant,Acute-Phase Reactants,Proteins, Acute-Phase,Reactants, Acute-Phase,Acute-Phase Glycoproteins,Acute-Phase Protein,Acute Phase Glycoprotein,Acute Phase Glycoproteins,Acute Phase Protein,Acute Phase Proteins,Acute Phase Reactants,Glycoprotein, Acute-Phase,Glycoproteins, Acute-Phase,Phase Reactant, Acute,Protein, Acute-Phase,Proteins, Acute Phase,Reactant, Acute Phase,Reactant, Acute-Phase,Reactants, Acute Phase
D000510 Alpha-Globulins Serum proteins that have the most rapid migration during ELECTROPHORESIS. This subgroup of globulins is divided into faster and slower alpha(1)- and alpha(2)-globulins. Alpha-Globulin,Alpha Globulin,Alpha Globulins
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
D013438 Sulfhydryl Compounds Compounds containing the -SH radical. Mercaptan,Mercapto Compounds,Sulfhydryl Compound,Thiol,Thiols,Mercaptans,Compound, Sulfhydryl,Compounds, Mercapto,Compounds, Sulfhydryl
D017207 Rats, Sprague-Dawley A strain of albino rat used widely for experimental purposes because of its calmness and ease of handling. It was developed by the Sprague-Dawley Animal Company. Holtzman Rat,Rats, Holtzman,Sprague-Dawley Rat,Rats, Sprague Dawley,Holtzman Rats,Rat, Holtzman,Rat, Sprague-Dawley,Sprague Dawley Rat,Sprague Dawley Rats,Sprague-Dawley Rats
D051381 Rats The common name for the genus Rattus. Rattus,Rats, Laboratory,Rats, Norway,Rattus norvegicus,Laboratory Rat,Laboratory Rats,Norway Rat,Norway Rats,Rat,Rat, Laboratory,Rat, Norway,norvegicus, Rattus

Related Publications

C Falkenberg, and M Allhorn, and I B Thøgersen, and Z Valnickova, and S V Pizzo, and G Salvesen, and B Akerström, and J J Enghild
The trypsin-inhibitory efficiency of human alpha 2-macroglobulin in the presence of alpha 1-proteinase inhibitor: evidence for the formation of an alpha 2-macroglobulin--alpha 1-proteinase inhibitor complex.
January 1999, Journal of enzyme inhibition,
C Falkenberg, and M Allhorn, and I B Thøgersen, and Z Valnickova, and S V Pizzo, and G Salvesen, and B Akerström, and J J Enghild
Inhibitory activity and conformational transition of alpha 1-proteinase inhibitor variants.
December 1991, European journal of biochemistry,
C Falkenberg, and M Allhorn, and I B Thøgersen, and Z Valnickova, and S V Pizzo, and G Salvesen, and B Akerström, and J J Enghild
In vitro complex formation between cholesterol and alpha 1-proteinase inhibitor.
February 1993, FEBS letters,
C Falkenberg, and M Allhorn, and I B Thøgersen, and Z Valnickova, and S V Pizzo, and G Salvesen, and B Akerström, and J J Enghild
Proteinase binding and inhibition by the monomeric alpha-macroglobulin rat alpha 1-inhibitor-3.
July 1989, The Journal of biological chemistry,
C Falkenberg, and M Allhorn, and I B Thøgersen, and Z Valnickova, and S V Pizzo, and G Salvesen, and B Akerström, and J J Enghild
The inhibitory complex of human alpha 1-proteinase inhibitor and human leukocyte elastase is a neutrophil chemoattractant.
May 1988, The Journal of experimental medicine,
C Falkenberg, and M Allhorn, and I B Thøgersen, and Z Valnickova, and S V Pizzo, and G Salvesen, and B Akerström, and J J Enghild
Acetaldehyde decreases the antitryptic activity of alpha 1-proteinase inhibitor.
January 1992, Alcohol (Fayetteville, N.Y.),
C Falkenberg, and M Allhorn, and I B Thøgersen, and Z Valnickova, and S V Pizzo, and G Salvesen, and B Akerström, and J J Enghild
Ozone effects on alpha-1-proteinase inhibitor in vivo: blood plasma inhibitory activity is unchanged.
January 1986, Experimental lung research,
C Falkenberg, and M Allhorn, and I B Thøgersen, and Z Valnickova, and S V Pizzo, and G Salvesen, and B Akerström, and J J Enghild
Isolation of rat serum alpha 1-microglobulin. Identification of a complex with alpha 1-inhibitor-3, a rat alpha 2-macroglobulin homologue.
September 1990, The Journal of biological chemistry,
C Falkenberg, and M Allhorn, and I B Thøgersen, and Z Valnickova, and S V Pizzo, and G Salvesen, and B Akerström, and J J Enghild
Inactivation of alpha 1-proteinase inhibitor by peroxynitrite.
January 1992, Chemical research in toxicology,
C Falkenberg, and M Allhorn, and I B Thøgersen, and Z Valnickova, and S V Pizzo, and G Salvesen, and B Akerström, and J J Enghild
Stabilization of alpha-1-proteinase inhibitor by citrate.
January 1984, Vox sanguinis,
Copied contents to your clipboard!