BIOMAT Database Logo BIOMAT Database Logo

Regulation of plasmin, miniplasmin, and streptokinase-plasmin complex by alpha 2-antiplasmin, alpha 2-macroglobulin, and antithrombin III in the presence of heparin. 1990

P K Anonick, and B Wolf, and S L Gonias
Department of Pathology, University of Virginia Health Sciences Center, Charlottesville 22908.

The regulation of plasmin, miniplasmin, and streptokinase-plasmin complex (SkPm) was studied in vitro in the presence of unfractionated porcine intestinal heparin using purified plasma proteinase inhibitors. Heparin enhanced the reaction of antithrombin III (AT) with plasmin (up to 40-fold with 20 units/ml). The rate of plasmin inhibition by alpha 2-antiplasmin (alpha 2AP) and by alpha 2-macroglobulin (alpha 2M) was not changed by heparin (0.5-100 units/ml); the rank-order of plasmin-inhibitory activity remained alpha 2AP greater than alpha 2M greater than AT. The reaction of miniplasmin with AT was studied also. The second order rate constant was 9.2 x 10(2) M-1s-1 without heparin and 2.6 x 10(4) M-1s-1 in the presence of 20 units/ml heparin. Heparin did not affect the rank-order of miniplasmin-inhibitory activity; it remained alpha 2M greater than alpha 2AP greater than AT. While the reaction of AT with SkPm was negligible, heparin stimulated this reaction dramatically. The SkPm-inhibitory activity of alpha 2AP was not changed by heparin. When plasma concentrations of alpha 2AP (1.05 microM) and AT (4.76 microM) were compared, AT inhibited greater amounts of SkPm in the presence of more than 5 units/ml of heparin. The increased SkPm-inhibitory activity of AT in heparin did not result from SkPm dissociation, and heparin did not decrease the rapid rate of streptokinase association with plasmin. These studies demonstrate that heparin can affect the regulation of fibrinolysis at multiple levels of the enzyme cascade.

UI MeSH Term Description Entries
D007700 Kinetics The rate dynamics in chemical or physical systems.
D010446 Peptide Fragments Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques. Peptide Fragment,Fragment, Peptide,Fragments, Peptide
D005341 Fibrinolysin A product of the lysis of plasminogen (profibrinolysin) by PLASMINOGEN activators. It is composed of two polypeptide chains, light (B) and heavy (A), with a molecular weight of 75,000. It is the major proteolytic enzyme involved in blood clot retraction or the lysis of fibrin and quickly inactivated by antiplasmins. Plasmin,Fibrogammin,Glu-Plasmin,Protease F,Thrombolysin,Glu Plasmin
D005342 Fibrinolysis The natural enzymatic dissolution of FIBRIN. Fibrinolyses
D006493 Heparin A highly acidic mucopolysaccharide formed of equal parts of sulfated D-glucosamine and D-glucuronic acid with sulfaminic bridges. The molecular weight ranges from six to twenty thousand. Heparin occurs in and is obtained from liver, lung, mast cells, etc., of vertebrates. Its function is unknown, but it is used to prevent blood clotting in vivo and vitro, in the form of many different salts. Heparinic Acid,alpha-Heparin,Heparin Sodium,Liquaemin,Sodium Heparin,Unfractionated Heparin,Heparin, Sodium,Heparin, Unfractionated,alpha Heparin
D000511 alpha-Macroglobulins Glycoproteins with a molecular weight of approximately 620,000 to 680,000. Precipitation by electrophoresis is in the alpha region. They include alpha 1-macroglobulins and alpha 2-macroglobulins. These proteins exhibit trypsin-, chymotrypsin-, thrombin-, and plasmin-binding activity and function as hormonal transporters. Slow alpha 2-Macroglobulins,alpha 2-Acute Phase Globulins,alpha-Macrofetoproteins,45S RNP,Acute-Phase alpha 1-Protein,Slow alpha 2-Globulin,alpha 1-Acute Phase Globulin,alpha 1-Acute Phase Protein,alpha 1-Macroglobulin,alpha 2-Acute Phase Globulin,alpha-Macrofetoprotein,Acute Phase alpha 1 Protein,RNP, 45S,Slow alpha 2 Globulin,Slow alpha 2 Macroglobulins,alpha 1 Acute Phase Globulin,alpha 1 Acute Phase Protein,alpha 1 Macroglobulin,alpha 1-Protein, Acute-Phase,alpha 2 Acute Phase Globulin,alpha 2 Acute Phase Globulins,alpha 2-Globulin, Slow,alpha 2-Macroglobulins, Slow,alpha Macrofetoprotein,alpha Macrofetoproteins,alpha Macroglobulins
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
D000979 alpha-2-Antiplasmin A member of the serpin superfamily found in plasma that inhibits the lysis of fibrin clots which are induced by plasminogen activator. It is a glycoprotein, molecular weight approximately 70,000 that migrates in the alpha 2 region in immunoelectrophoresis. It is the principal plasmin inactivator in blood, rapidly forming a very stable complex with plasmin. alpha 2-Plasmin Inhibitor,Serpin F2,alpha(2)-Plasmin Inhibitor,alpha-2 Antiplasmin,alpha 2 Antiplasmin,alpha 2 Plasmin Inhibitor
D000990 Antithrombin III A plasma alpha 2 glycoprotein that accounts for the major antithrombin activity of normal plasma and also inhibits several other enzymes. It is a member of the serpin superfamily. Heparin Cofactor I,Antithrombin III-Alpha,Atenativ,Heparin Co-Factor I,Kybernin,Serpin C1,Thrombate III,Antithrombin III Alpha,Antithrombin IIIAlpha,Cofactor I, Heparin,Heparin Co Factor I
D013300 Streptokinase Streptococcal fibrinolysin . An enzyme produced by hemolytic streptococci. It hydrolyzes amide linkages and serves as an activator of plasminogen. It is used in thrombolytic therapy and is used also in mixtures with streptodornase (STREPTODORNASE AND STREPTOKINASE). EC 3.4.-. Avelizin,Awelysin,Celiase,Distreptase,Kabikinase,Kabivitrum,Streptase,Streptodecase

Related Publications

P K Anonick, and B Wolf, and S L Gonias
Regulation of streptokinase-human plasmin complex by the plasma proteinase inhibitors alpha 2-antiplasmin and alpha 2-macroglobulin is species specific and temperature dependent.
November 1988, Blood,
P K Anonick, and B Wolf, and S L Gonias
The determination of antithrombin III, alpha 2-macroglobulin and alpha 2-antiplasmin in plasma by laser nephelometry.
April 1980, Journal of clinical chemistry and clinical biochemistry. Zeitschrift fur klinische Chemie und klinische Biochemie,
P K Anonick, and B Wolf, and S L Gonias
Imbalance between thrombin and plasmin activity in disseminated intravascular coagulation. Assessment by the thrombin-antithrombin-III complex/plasmin-alpha-2-antiplasmin complex ratio.
January 1992, Haemostasis,
P K Anonick, and B Wolf, and S L Gonias
On the reaction of plasmin or plasmin-streptokinase complex with aprotinin or alpha 2-antiplasmin.
January 1980, Thrombosis research,
P K Anonick, and B Wolf, and S L Gonias
[Antiplasmin, antitrypsin and antithrombin activity of alpha-2-macroglobulin].
January 1967, Transfusion,
P K Anonick, and B Wolf, and S L Gonias
[Plasma levels of antithrombin III, thrombin-antithrombin III complex, alpha 2 plasmin inhibitor and plasmin alpha 2 plasmin inhibitor complex in normal and sick newborn infants].
July 1991, [Rinsho ketsueki] The Japanese journal of clinical hematology,
P K Anonick, and B Wolf, and S L Gonias
Antithrombin III, plasminogen, plasmin, and alpha-2-antiplasmin in donor blood and plasma components.
January 1985, Annals of clinical and laboratory science,
P K Anonick, and B Wolf, and S L Gonias
Interaction of plasmin with alpha 2-macroglobulin and alpha 2-antiplasmin in the presence and absence of tranexamic acid.
January 1980, Thrombosis research,
P K Anonick, and B Wolf, and S L Gonias
The temperature-dependent reaction between alpha 2-macroglobulin and streptokinase-plasmin(ogen) complex.
March 1987, The Journal of biological chemistry,
P K Anonick, and B Wolf, and S L Gonias
Kinetics of the reactions between streptokinase, plasmin and alpha 2-antiplasmin.
October 1979, European journal of biochemistry,
Copied contents to your clipboard!