Reduction of thrombus size in murine models of thrombosis following administration of recombinant α 1-Proteinase inhibitor mutant proteins

Thrombosis and Haemostasis

Volumn 107, Issue 5, 2012, Pages 972-984

  Sheffield, William P ^a,b   Eltringham Smith, Louise J ^a   Bhakta, Varsha ^b   Gataiance, Sharon ^a  

^a MCMASTER UNIVERSITY   (Canada)

^b CANADIAN BLOOD SERVICES   (Canada)

Author keywords

1 proteinase inhibitor; Coagulation; Heparin cofactor II; Molecular biology; Protein engineering; Serpins; Thrombosis

Indexed keywords

ALPHA 1 ANTITRYPSIN; ALPHA 1 ANTITRYPSIN M358R; BLOOD CLOTTING FACTOR 10A; BLOOD CLOTTING FACTOR 11A; BLOOD CLOTTING FACTOR 12A; DROTRECOGIN; FIBRINOGEN; HAPI M358R; HAPI RCL5; HYBRID PROTEIN; IODINE 125; LIPOPOLYSACCHARIDE; MUTANT PROTEIN; N (G) NITROARGININE METHYL ESTER; UNCLASSIFIED DRUG;

ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; BLEEDING; CAROTID ARTERY; CAVA VEIN; CONTROLLED STUDY; ENDOTOXEMIA; ENZYME LINKED IMMUNOSORBENT ASSAY; FIBRIN DEPOSITION; IMMUNOHISTOCHEMISTRY; ISOTOPE LABELING; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PURIFICATION; THROMBOSIS;

ALPHA 1-ANTITRYPSIN; ANIMALS; ANTITHROMBINS; CAROTID ARTERY INJURIES; CHLORIDES; DISEASE MODELS, ANIMAL; DOSE-RESPONSE RELATIONSHIP, DRUG; ENDOTOXEMIA; ENDOTOXINS; FACTOR XA; FACTOR XIA; FACTOR XIIA; FERRIC COMPOUNDS; FIBRINOGEN; FIBRINOLYTIC AGENTS; HEMORRHAGE; INJECTIONS, INTRAVENOUS; KINETICS; LEUKOCYTE ELASTASE; MICE; MUTATION; NG-NITROARGININE METHYL ESTER; RECOMBINANT FUSION PROTEINS; THROMBIN; THROMBOSIS;

EID: 84860524518     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1160/TH11-09-0604     Document Type: Article

References (37)

1. Rau JC, Beaulieu LM, Huntington JA, et al. Serpins in thrombosis, hemostasis and fibrinolysis. J Thromb Haemost 2007; 5 (Suppl 1): 102-115.
2. Beatty K, Bieth J, Travis J. Kinetics of association of serine proteinases with native and oxidized alpha-1-proteinase inhibitor and alpha-1-antichymotrypsin. J Biol Chem 1980; 255: 3931-3934.
3. Schapira M, Scott C F, Colman RW. Contribution of plasma protease inhibitors to the inactivation of kallikrein in plasma. J Clin Invest 1982; 69: 462-468.
4. Aoki N. The past, present and future of plasmin inhibitor. Thromb Res 2005; 116: 455-464.
5. Sim RB, Arlaud GJ, Colomb MG. Kinetics of reaction of human C1-inhibitor with the human complement system proteases C1r and C1s. Biochim Biophys Acta 1980; 612: 433-449.
6. de Agostini A, Lijnen HR, Pixley RA, et al. Inactivation of factor XII active fragment in normal plasma. Predominant role of C-1-inhibitor. J Clin Invest 1984; 73: 1542-1549.
7. Lane DA, Olds RR, Thein SL. Antithrombin and its deficiency states. Blood Co-agul Fibrinolysis 1992; 3: 315-341.
8. Kueppers F. The role of augmentation therapy in alpha-1 antitrypsin deficiency. Curr Med Res Opin 2011; 27: 579-588.
9. Khan DA. Hereditary angioedema: Historical aspects, classification, pathophysi-ology, clinical presentation, and laboratory diagnosis. Allergy Asthma Proc 2011; 32: 1-10.
10. Owen MC, Brennan SO, Lewis JH, et al. Mutation of antitrypsin to antithrombin. alpha 1-antitrypsin Pittsburgh (358 Met leads to Arg), a fatal bleeding disorder. N Engl J Med 1983; 309: 694-698.
11. Travis J, Owen M, George P, et al. Isolation and properties of recombinant DNA produced variants of human alpha 1-proteinase inhibitor. J Biol Chem 1985; 260: 4384-4389.
12. Dai E, Guan H, Liu L, et al. Serp-1, a viral anti-inflammatory serpin, regulates cellular serine proteinase and serpin responses to vascular injury. J Biol Chem 2003; 278: 18563-18572.
13. Tardif JC, L'Allier PL, Gregoire J, et al. A randomized controlled, phase 2 trial of the viral serpin Serp-1 in patients with acute coronary syndromes undergoing percutaneous coronary intervention. Circ Cardiovasc Interv 2010; 3: 543-548.
14. Hopkins PC, Crowther DC, Carrell RW, et al. Development of a novel recom-binant serpin with potential antithrombotic properties. J Biol Chem 1995; 270: 11866-11871.
15. Hopkins PC, Pike RN, Stone SR. Evolution of serpin specificity: cooperative interactions in the reactive-site loop sequence of antithrombin specifically restrict the inhibition of activated protein C. J Mol Evol 2000; 51: 507-515.
16. Filion ML, Bhakta V, Nguyen LH, et al. Full or partial substitution of the reactive center loop of alpha-1-proteinase inhibitor by that of heparin cofactor II: P1 Arg is required for maximal thrombin inhibition. Biochemistry 2004; 43: 14864-14872.
17. Sutherland JS, Bhakta V, Filion ML, et al. The transferable tail: fusion of the N-ter-minal acidic extension of heparin cofactor II to alpha1-proteinase inhibitor M358R specifically increases the rate of thrombin inhibition. Biochemistry 2006; 45: 11444-11452.
18. Sutherland JS, Bhakta V, Sheffield W P. The appended tail region of heparin cofac-tor II and additional reactive centre loop mutations combine to increase the reactivity and specificity of alpha1-proteinase inhibitor M358R for thrombin. Thromb Haemost 2007; 98: 1014-1023.
19. Sutherland JS, Bhakta V, Sheffield W P. Investigating serpin-enzyme complex formation and stability via single and multiple residue reactive centre loop substitutions in heparin cofactor II. Thromb Res 2006; 117: 447-461.
20. Syed S, Schuyler PD, Kulczycky M, et al. Potent antithrombin activity and delayed clearance from the circulation characterize recombinant hirudin genetically fused to albumin. Blood 1997; 89: 3243-3252.
21. Sheffield W P, McCurdy TR, Bhakta V. Fusion to albumin as a means to slow the clearance of small therapeutic proteins using the Pichia pastoris expression system: a case study. Methods Mol Biol 2005; 308: 145-154.
22. Sheffield W P, Eltringham-Smith LJ, Gataiance S, et al. A long-lasting, plasmin-ac-tivatable thrombin inhibitor aids clot lysis in vitro and does not promote bleeding in vivo. Thromb Haemost 2009; 101: 867-877.
23. Cunningham MA, Bhakta V, Sheffield W P. Altering heparin cofactor II at VAL439 (P6) either impairs inhibition of thrombin or confers elastase resistance. Thromb Haemost 2002; 88: 89-97.
24. Olson ST, Bjork I, Shore JD. Kinetic characterization of heparin-catalyzed and un-catalyzed inhibition of blood coagulation proteinases by antithrombin. Methods Enzymol 1993; 222: 525-559.
25. Fraker PJ, Speck JC, Jr. Protein and cell membrane iodinations with a sparingly soluble chloroamide, 1,3,4,6-tetrachloro-3a,6a-diphrenylglycoluril. Biochem Biophys Res Commun 1978; 80: 849-857.
26. Wang X, Smith PL, Hsu MY, et al. Murine model of ferric chloride-induced vena cava thrombosis: evidence for effect of potato carboxypeptidase inhibitor. J Thromb Haemost 2006; 4: 403-410.
27. Wang X, Smith PL, Hsu M Y, et al. Deficiency in thrombin-activatable fibrinolysis inhibitor (TAFI) protected mice from ferric chloride-induced vena cava thrombosis. J Thromb Thrombolysis 2007; 23: 41-49.
28. Jaimes EA, del Castillo D, Rutherford MS, et al. Countervailing influence of tumor necrosis factor-alpha and nitric oxide in endotoxemia. J Am Soc Nephrol 2001; 12: 1204-1210.
29. Chen D, Giann opou los K, Shiels PG, et al. Inhibition o f int ravascular t hrom b osis in murine endotoxemia by targeted expression of hirudin and tissue factor pathway inhibitor analogs to activated endothelium. Blood 2004; 104: 1344-1349.
30. Dellinger R P, Levy MM, Carlet JM, et al. Surviving Sepsis Campaign: international guidelines for management of severe sepsis and septic shock: 2008. Crit Care Med 2008; 36: 296-327.
31. Wang X. Lipopolysaccharide augments venous and arterial thrombosis in the mouse. Thromb Res 2008; 123: 355-360.
32. Colman RW, Flores DN, De La Cadena RA, et al. Recombinant alpha 1-antitrypsin Pittsburgh attenuates experimental gram-negative septicemia. Am J Pathol 1988; 130: 418-426.
33. Harper PL, Taylor FB, DeLa Cadena RA, et al. Recombinant antitrypsin Pittsburgh undergoes proteolytic cleavage during E. coli sepsis and fails to prevent the associated coagulopathy in a primate model. Thromb Haemost 1998; 80: 816-821.
34. Carrell RW, Owen MC. Plakalbumin, alpha 1-antitrypsin, antithrombin and the mechanism of inflammatory thrombosis. Nature 1985; 317: 730-732.
35. Hatton MW, Ross B, Southward SM, et al. Pretreatment of rabbits with either hi-rudin, ancrod, or warfarin significantly reduces the immediate uptake of fibri-nogen and platelets by the deendothelialized aorta wall after balloon-catheter injury in vivo. Arterioscler Thromb Vasc Biol 1998; 18: 816-824.
36. Karimi M, Bereczky Z, Cohan N, et al. Factor XIII Deficiency. Semin Thromb He-most 2009; 35: 426-438.
37. Massberg S, Grahl L, von Bruehl ML, et al. Reciprocal coupling of coagulation and innate immunity via neutrophil serine proteases. Nat Med 2011; 16: 887-896.