Abstract
Proteases play a determinant role in many biological processes. In blood coagulation several enzymes are interrelated to form a cascade of reactions achieving amplification of the initial trigger reaction. Generally trigger mechanisms show a great diversity including negatively charged surfaces (Hageman Factor dependent pathways), antigen/antibody complexes (activation of the classical complement pathway), polysaccharides and lipopolysaccharides (alternate complement pathway) or specific enzymes such as urokinase or tissue activator in the case of fibrinolysis.
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
U. Abildgaard, Inhibition of the thrombin-fibrinogen reaction by heparin in the absence of cofactor. Inhibition of the thrombin-fibrinogen reaction by heparin and purified cofactor, Scand. J. Haemat. 5: 432 and 440 (1968).
L. Q. Andersson, T. W. Barrowcliffe, E. Holmer, E. A. Johnson, and G. Söderström, Molecular weight dependency of the heparin potentiated inhibition of thrombin and active factor X, Thromb. Res. 15: 531 1979.
M. Aubry, and J. Bieth, A kinetic study of the inhibition of human and bovine trypsins and chymotrypsins by the internet-inhibitor from human plasma, Biochim. Biophys. Acta 438: 221 1976.
A. J. Barrett, M. A. Brown, and C. A. Sayers, The electrophoretically “Slow” and “Fast” forms of the α2-macroglobulin molecule, Biochem. J. 181: 401 1979.
B. Blauhut, S. Necek, H. Vinazzer, and H. Bergmann, Substitution therapy with an antithrombin III concentrate in shock and DIC, Thromb. Res. 27: 271 1982.
I. Björk, C. M. Jackson, H. Jörnvall, and W. J. Salsgiver, The active site of antithrombin. Release of the same proteolytically cleaved form of the inhibitor from complexes with factor IXa, factor Xa, and thrombin, J. Biol. Chem. 257: 2406 (1982).
V. A. Bokisch, and H. J. Müller-Eberhard, Anaphylatoxin inactivator of human plasma: its isolation and characterization as a carboxypeptidase, J. Clin. Invest. 49: 2427 1970.
P. Brandt, J. Jespersen, and G. Gregersen, Postpartum haemolytic-uraemic Syndrom successfully treated with antithrombin III, Brit. Med. J. 280: 6212 1980.
P. Brandt, Observations during the treatment of antithrombin III deficient women with heparin and antithrombin concentrate during pregnancy, parturition, and abortion, Thromb. Res. 22: 15 1981.
G. Bretzel, and K. Hochstrasser, Liberation of an acid stable proteinase inhibitor from the human inter-α-trypsin inhibitor by the action of kallikrein, Hoppe-Seyler’s Z. Physiol. Chem. 357: 487 1976.
M. S. Brower, and P. C. Harpel, Proteolytic cleavage and inactivation of α2-plasmin inhibitor and Cl-inactivator by human polymorphonuclear leukocyte elastase, J. Biol. Chem. 257: 9849 1981.
R. W. Carrell, J. O. Jeppsson, C. B. Laurell, S. O. Brennan, M. C. Owen, L. Vaughan, and D. R. Boswell, Structure and variation of human α1-antitrypsin, Nature 298: 329 1982.
S. Chesne, C. L. Villiers, G. L. Arlaud, M. B. Lacroix, and M. G. Colomb, Fluid-phase interaction of C1-inhibitor (C1-Inh) and the subcomponents Clr and C1s of the first component of complement, C1, Bioch. J. 201: 61 1982.
J. Choay, J. C. Lormeau, M. Petitou, P. Sinay, and J. Fareed, Structural studies on a biologically active hexasaccharide obtained from heparin, Ann. Nat. Acad. Sci. 370: 644 1981.
M. Cicardi, L. Bergamaschini, B. Marasini, G. Boccassini, A. Tucci, and A. Agostoni, Hereditary angioedema: an appraisal of 104 cases, Amer. J. Med. Sci. 284: 2 1982.
D. Collen, Identification and some properties of a New Fast-reacting plasmin inhibitor in human plasma, Eur. J. Biochem. 69: 209 1976.
F. H. M. Derkx, B. N. Bouma, H. L. TanTjiong, A. J. Man in ‘T Veld, J. H. B. de Bruyn, and G. J. Wenting, The plasma kallikrein-renin connection, Supplementum to the archives Intern. de Pharmacodynamie et de Therapie, 105 (1980).
V. H. Donaldson, and R. A. Harrisson, Complexes between C1-inhibitor, kallikrein, high molecular weight kininogen, plasma thromboplastin antecedent, and plasmin in normal human plasma and hereditary angioneurotic edema plasmas containing dysmorphic C1-inhibitors: role of cold activation, Blood 60: 121 1982.
C. T. Esmon, N. L. Esmon, and K. W. Harris, Complex formation between thrombin and thrombomodunin inhibits both thrombin-catalized fibrin formation and factor V activation, J. Biol. Chem. 257: 7944 (1982).
M. K. Fagerhol, The Pi-system. Genetic variants of serum α1-antitrypsin, Series Haematologica 1: 153 1968.
D. T. Fearon, and K. F. Austen, Properdin: binding to C3b and stabilization of the C3b-dependent C3-convertase, J. Exp. Med. 142: 856 1975.
R. C. Franz, W. J. C. Coetzee, and R. Anderson, Venous thrombo-embolism and raised alpha-1-anti-trypsin levels: A possible causal relationship between excessive neutral protease inhibition and defective granulocyte-induced fibrinolysis, SA Medical J. 59: 661 1981.
J. E. Gadek, S. W. Hosea, J. A. Gelfand, M. M. Frank, Replacement therapy in hereditary angioedema. Successful treatment of acute episodes of angioedema with partly purified C1-inhibitor, New Eng. J. Med. 302: 542 1980.
J. E. Gadek, H. G. Klein, P. V. Holland, and R. G. Crystal, Replacement therapy of alpha-1-antitrypsin deficiency. Reversal of protease-antiprotease imbalance within the alveolar structures of PiZ subjects, J. Clin. Invest. 68: 1158 1981.
B. Ghebrehiwet, M. Silverberg, and S. P. Kaplan, Activation of the classical pathway of complement by Hageman factor fragments, J. Exp. Med. 153: 665 1981.
P. C. Giclas, Effect of plicatic acid on human serum complement includes interference with C1-inhibitor function, J. Immunol. 129: 168 1982.
P. C. Harpel, Studies on human plasma α2-macroglobulin-enzyme interactions. Evidence for proteolytic modification of the subunit chain structure, J. Exp. Med. 138: 508 1973.
K. Hochstrasser, H. Feuth und O. Steiner, Zur Charakterisierung der säurestabilen Proteaseninhibitoren aus Humanplasma, Hoppe Seyler’s Z. Physiol. Chem. 354: 927 1973.
K. Hochstrasser, J. Niebel, H. Feuth und K. Lempart, Über Abbauprodukte des Inter-alpha-Trypsininhibitors im Serum. I. Der Inter-alpha-Trypsininhibitor als Prekursor des säurestabilen Serum-Trypsin-Inhibitors. II. Säurelabile Derivate des Inter-alpha-Trypsininhibitors, Klin. Wochenschr. 55: 337 1977.
M. Höök, K. Björk, J. Hopwood, U. Lindahl, Anticoagulant activity of heparin of high activity and low activity heparin-species by affinity chromatography on immobilized anti-thrombin, FEBS Lett. 66: 90 1976.
M. J. Imber, and S. V. Pizzo, Clearance and binding of two electrophoretic “Fast” forms of human α2-macroglobulin, J. Biol. Chem. 256: 8134 1981.
A. Janoff, Inhibition of human granulocytes elastase by serum α1-antitrypsin, Am. J. Resp. Dis. 105: 121 1972.
A. Janoff, H. Carp, and D. K. Lee, Cigarette smoke inhalation decreases α1-antitrypsin activity in rat lung, Science 206: 1313 1979.
M. Jochum, S. Lander, N. Heimburger, and H. Fritz, Effect of human granulocytic elastase on isolated human antithrombin III, Hoppe-Seyler’s Z. Physiol. Chem. 362: 103 1981.
R. E. Jordan, D. Beeler, and R. D. Rosenberg, Fractionation of low molecular weight heparin species and their interaction with antithrombin, J. Biol. Chem. 254: 2902 1979.
R. E. Jordan, G. M. Oosta, W. T. Gardner, and R. D. Rosenberg, The binding of low molecular weight heparin to hemostatic enzymes, J. Biol. Chem. 255: 10073 1980.
F. Josso, D. Benamon-Djiane, J. M. Lavergne, C. Weilland, and M. Steinbuch, Investigations of plasma antithrombin activity using 131 I labelled human thrombin, 7th Congr. Clin. Chem. Geneva, M. Roth ed., Karger 2: 46 1970.
J. Kaplan, and M. L. Nielsen, Analysis of macrophage surface receptors. I. Binding of α-macroglobulinprotease complexes to rabbit alveolar macrophages. II. Internalization of’ α2-macroglobulin-trypsin complexes by rabbit alveolar macrophages, J. Biol. Chem. 254: 7323 and 7329 (1979).
M. D. Kazatchkine, D. T. Fearon, and K. F. Austen, Human alternative complement pathway: membraneassociated sialic acid regulates the competition between B and B1H for cell-bound C3b, J. Immunol. 122: 75 1979.
W. Kisiel, W. M. Canfield, L. H. Ericsson, and E. W. Davie, Anticoagulant properties of bovine plasma protein suite. C following activation by thrombin, Biochemistry 16: 5824 (1977).
P. Lambin, R. Audran, and M. Steinbuch, Etude des fragments de 1’inter-alpha-trypsine inhibiteur obtenus par digestion plasminique, Pathol. Biol. Suppl. 25: 31 1977.
P. Lambin, J. M. Fine, and M. Steinbuch, Inhibition of plasmin by a small molecular weight inhibitor derived from human inter-alpha-trypsin inhibitor, Thromb. Res. 13: 563 1978.
P. Lambin, F. Pochon, J. M. Fine, and M. Steinbuch, α2-M macroglobulin/thrombin interaction in the presence of hydroxylamine, in press (1983).
C. Larsson, Natural history and life expectancy in severe alpha1-antitrypsin deficiency, PiZ. Intermediate alpha1-antitrypsin deficiency, Pi M-, Acta Med. Scand. 204: 345 and 353 (1978).
C. B. Laurell, Comparison of alpha1-antitrypsin and alpha2-macroglobulin, in: “Pulmonary Emphysema and Proteolysis,” C. Mittman, ed., Academic Press, New York-London (1972).
F. van Leuven, P. Marynen, J. J. Cassiman, and H. van den Berghe, Relation of internal thioesters to conformational change and receptor recognition site in α2-macroglobulin complexes, Biochem. J. 203: 405 1982.
H. R. Lijnen, M. Hoylaerts, and D. Collen, Isolation and characterization of a human protein with affinity for the lysine-binding sites in plasminogen. Role in the regulation of fibrinolysis and identification as histidine-rich-glycoprotein, J. Biol. Chem. 255: 10214 1980.
M. 0. Longas, and T. H. Finlay, The covalent nature of the human antithrombin III-thrombin bond, Biochem. J. 189: 481 1980.
R. J. Mandle, and A. P. Kaplan, Hageman-factor dependent fibrinolysis: generation of fibrinolytic activity by the interaction of human activated factor XI and plasminogen, Blood 54: 850 1979.
P. Marynen, F. van Leuven, J. J. Cassiman, and H. van den Berghe, A monoclonal antibody to a neoantigen on α2-macroglobulin complexes inhibits receptor-mediated endocytosis, J. Immunol. 127: 1782 1981.
H. L. Meier, J. V. Pierce, R. W. Colman, and A. P. Kaplan, Activation and function of human Hageman factor. The role of high molecular weight kininogen and prekallikrein, J. Clin. Invest. 60: 18 (1977).
L. A. Miles, J. P. Burnier, M. S. Verlander, M. Goodman, A. J. Kleiss, and J. H. Griffin, Inactivation of purified human α2-antiplasmin and purified human C1-inhibitor By synthetic fibrinolytic agents, Blood 57: 1015 1981.
M. Moroi, and N. Aoki, Isolation and characterization of alpha2-plasmin inhibitor from human plasma. A novel proteinase inhibitor which inhibits activator-induced clot lysis, J. Biol. Chem. 251: 5956 1976.
M. Moroi, and N. Aoki, Inhibition of plasminogen binding to fibrin by α2-plasmin inhibitor, Thromb. Res. 10: 851 1977.
S. Müllertz, and I. Clemmensen, The primary inhibitor of plasmin in human plasma, Biochem. J. 159: 545 1977.
B. Osterud, and S. I. Rapaport, Activation of 125I factor IX and 125I-factor X: Effect of tissue factor and factor VII, factor Xa and thrombin, Scand. J. Haematol. 24: 213 1980.
M. K. Pangburn, and H. J. Müller-Eberhard, Complement C3-convertase: cell surface restriction of β H control and generation of restriction on neuraminidase-treated cells, Proc. Nat. Acad. Sci. 75: 2416 1978.
M. K. Pangburn, and H. J. Müller-Eberhard, Relation of a putative thioester bond in C3 to activation of the alternative pathway and the binding of C3b to biological targets of complement, J. Exp. Med. 152: 1102 1980.
M. K. Pangburn, R. D. Schreiber, and H. J. Müller-Eberhard, Human complement C3b-inactivator: isolation, characterization and demonstration of an absolute requirement for the serum protein β-1H for cleavage of C3b and C4b in solution, J. Exp. Med. 146: 257 1977.
E. F. Plow, Leukocyte elastase release during blood coagulation, J. Clin. Invest. 69: 564 1982.
E. F. Plow, and T. S. Edgington, An alternative pathway for fibrinolysis. I. The cleavage of fibrinogen by leukocyte proteases at physiologic pH, J. Clin. Invest. 56: 30 1975.
M. B. Prandini, B. Wiman, M. Samama, and D. Collen, Effects of the synthetic fibrinolytic agents ortho-thymotic acid and S-1623 on the reaction between human plasmin and antiplasmin, Thromb. Res. 13: 165 1978.
R. Radcliffe, A. Bagdasarian, R. W. Colman, and Y. Nemerson, Activation of factor VII by Hageman factor fragments, Blood 50: 611 1977.
R. D. Rosenberg, and L. Lam, Correlation between structure and function of heparin, Proc. Nat. Acad. Sci. 76: 1218 1979.
H. C. Ryley, and T. D. Brogan, Quantitative immuno-electrophoretic analysis of the plasma proteins in the sol phase of sputum from patients with chronic bronchitis, J. Clin. Path. 26: 852 1973.
C. A. Sayers, and A. J. Barett, Binding of anhydrotrypsin to α2-macroglobulin, Biochem. J. (Mol. Aspects) 189: 255 (1980).
M. Schapira, C. F. Scott, and R. W. Colman, Contribution of plasma protease inhibitors to the inactivation of kallikrein in plasma, J. Clin. Invest 69: 462 1982.
M. A. Shifman, and S. V. Pizzo, The “in vivo” metabolism of antithrombin III and antithrombin III complexes, J. Biol. Chem. 257: 3243 1981.
L. Sottrup-Jensen, T. E. Petersen, and S. Magnusson, A thiol-ester in α2-macroglobulin cleaved during proteinase complex formation, FEBS Lett. 121: 275 1980.
P. van der Starre, D. Sinclair, J. Damen, and H. Brummelhuis, Inhibition of the hypotensive effect of plasma protein solutions by C1-esterase inhibitor, J. Thor. Cardiovasc. Surg. 79: 738 1980.
M. Steinbuch, R. Audran, P. Lambin and J. M. Fine, Subunit structure of human alpha-2-macroglobulin. Its relationships with its biological activity, in: “The Protides of the Biological Fluids,” H. Peters, ed., Pergamon Press, Oxford, New York (1976).
M. Steinbuch, L. Pejaudier, M. Quentin, and V. Martin, Molecular alteration of α2-macroglobulin by aliphatic amines, Biochim. Biophys. Acta 154: 228 1968.
T. Sugo, N. Ikari, H. Kato, S. Iwanaga, and S. Fujii, Functional sites of bovine high molecular weight kininogen as a cofactor in kaolin-mediated activation of factor XII (Hageman factor), Biochemistry 19: 3215 1980.
K. Suzuki, B. Dahlbäck, and J. Stenflo, Thrombin-catalysed activation of human coagulation factor V, J. Biol. Chem. 257: 6556 1982.
R. P. Swenson, and J. B. Howard, Characterization of alkylamine-sensitive site in α2-macroglobulin, Proc. Nat. Acad. Sci. 76: 4313 1979.
A. Takada, T. Koide, and Y. Takada, Interaction of thrombin with antithrombin III and α2-macroglobulin in the plasma, Thromb. Res. 16: 59 1979.
D. P. Thomas, R. E. Merton, T. W. Barrowcliffe, and U. Lindhal, Effects of heparin oligosaccarides with high affinity for antithrombin III in experimental venous thrombosis, Thromb. Haemost. 47: 244 1982.
D. M. Tollefsen, D. W. Majerus, and M. K. Blank, Heparin cofactor II, J. Biol. Chem. 257: 2162 1982.
J. Travis, R. Baugh, P. J. Giles, D. Johnson, J. Bowen and C. F. Reilly, Human leukocyte elastase and cathepsin G: Isolation, characterization and interaction with plasma proteinase inhibitors, in: “Neutral Proteases of Human Polymorphonuclear Leukocytes,” K. Havemann, A. Janoff, eds., Urban & Schwarzenberg, Baltimore/Munich (1978).
J. Travis, N. Matheson, D. Johnson, and K. Beatty, Human alpha-1-proteinase inhibitor and human alpha-1-antichymotrypsin: properties and mechanism studies, in: “The Chemistry and Physiology of the Human Plasma Proteins,” D. H. Bing, ed., Pergamon Press, Oxford-New York (1978).
D. Tsuru, K. Kado, K. Fujiwara, M. Tomimatsu, and K. Ogita, Interaction of porcine α2-macroglobulin with chemically modified proteinases, J. Biochem. 83: 1345 1978.
G. Vehar, and E. W. Davies, Preparation and properties of bovine factor VIII (antihemophilic factor), Biochemistry 19: 401 (1980).
F. J. Walker, P. W. Sexton, and C. T. Esmon, The inhibition of blood coagulation by activated protein C through the selective inactivation of activated factor V, Biochim. Biophys, Acta 571: 333 1979.
K. Whaley, and S. Ruddy, Modulation of the alternative complement pathway by 1H globulin, J. Exp. Med. 144: 1147 1976.
B. Wiman, and D. Collen, On the mechanism of the reaction between plasmin and α2-antiplasmin. Kinetics and structural changes, in: The Physiological Inhibitors of Coagulation and Fibrinolysis,” D. Collen, B. Wiman, M. Verstraete, eds., Biomedical Press, Elsevier, Holland (1979).
B. Wiman, and P. Wallen, The specific interaction betweer plasminogen and fibrin. A physiological role of the lysine binding site in plasminogen, Thromb. Res. 10: 213 1977.
K. Wu, D. Wang, and R. D. Feinman, Inhibition of proteases by α2-macroglobulin, J. Biol. Chem. 256: 10409 1981.
P. Wunderwald, W. J. Schrenk, and H. Port, Antithrombin BM from human plasma: an antithrombin binding moderately to heparin, Thromb. Res. 25: 177 1982.
R. J. Ziccardi, A new role for C1-inhibitor in homeostasis: control of activation of the first component of human complement, J. Immunol. 128: 2505 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
Steinbuch, M. (1984). Regulation of Protease Activity. 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_2
Download citation
DOI: https://doi.org/10.1007/978-1-4615-9355-3_2
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4615-9357-7
Online ISBN: 978-1-4615-9355-3
eBook Packages: Springer Book Archive