Influence of Contact System Deficiencies during Cardiopulmonary Bypass

Angelo Agostini; Massimo Cugno

doi:10.1055/s-0037-1615673

Thrombosis and Haemostasis, Inhaltsverzeichnis

Thromb Haemost 2001; 85(02): 191-192
DOI: 10.1055/s-0037-1615673

Commentary

Schattauer GmbH

Influence of Contact System Deficiencies during Cardiopulmonary Bypass

Angelo Agostini

¹Department of Internal Medicine, IRCCS Maggiore Hospital, University of Milan, Milan, Italy

,

Massimo Cugno

¹Department of Internal Medicine, IRCCS Maggiore Hospital, University of Milan, Milan, Italy

› Institutsangaben

Abstract

Summary

As a result of the expanding indications for cardiopulmonary bypass (CPB) there is a growing number of patients undergoing this procedure who are at high surgical risk, and increasing efforts to investigate the mechanisms involved in CPB complications are warranted. Blood contact with foreign surfaces triggers systemic inflammatory response and may induce coagulation (1), this is believed to be responsible of most of the unwanted effects associated with CPB. During this procedure, contact phase activation occurs (2), involving factor XII (FXII), prekallikrein (PK) and high molecular weight kininogen (HK). FXII binds to negatively charged surfaces undergoing autoactivation with cleavage of Arg353-Val354 to form a two-chain molecule of 80 kD, i.e. activated FXII (FXIIa, also known as FXIIa). FXIIa can cleave PK to kallikrein which in turn cleaves FXII to produce FXIIa and a factor XII fragment of 28-30 kD (FXIIf, also known as FXIIa) and cleaves HK to HKa generating the nonapeptide bradykinin. FXIIa can cleave both FXI and PK to active enzymes, while FXIIf (which cannot bind to surfaces) cleaves PK (2) and the first component of complement (C1) (3). These mechanisms of activation differ from those initiating the coagulation cascade during in vivo haemostasis through the tissue factor pathway as a result of tissue injury (4).

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Referenzen

References
1 Spiess BD. Cardiopulmonary bypass: coagulation and inflammation issues. Introduction. J Cardiovasc Pharm 1996; 27 (Suppl. 01) v-vii.
2 Colman RW. Biologic activities of the contact factors in vivo. Potentiation of hypotension, inflammation, and fibrinolysis, and inhibition of cell adhesion, angiogenesis and thrombosis. Thromb Haemost 1999; 82: 1568-77.
3 Ghebrehiwet B, Silverberg M, Kaplan AP. Activation of the classical pathway of complement by Hageman factor fragment. J Exp Med 1981; 153: 665-76.
4 Rapaport SI, Rao LVM. The tissue factor pathway: how it has become a “prima ballerina”. Thromb Haemost 1995; 74: 7-17.
5 Wachtfogel YT, Harpel PC, Edmunds Jr LH, Colman RW. Formation of Cqs-C1-inhibitor, kallikrein-C1-inhibitor, and plasmin-alpha2-plasmin-inhibitor complexes during cardiopulmonary bypass. Blood 1989; 73: 468-71.
6 Wachtfogel YT, Kucich U, Hack CE, Gluszko P, Niewiarowski S, Colman RW, Edmunds Jr LH. Aprotinin inhibits the contact, neuthrophil and platelet activation systems during simulated extracorporeal perfusion. J Thorac Cardiovasc Surg 1993; 106: 1-10.
7 Boisclair MD, Lane DA, Philippou H, Esnouf MP, Sheikh S, Hunt B, Smith KJ. Mechanisms of thrombin generation during surgery and cardiopulmonary bypass. Blood 1993; 82: 3350-7.
8 Kappelmayer J, Bernabei A, Edmunds Jr LH, Edgington TS, Colman RW. Tissue factor is expressed on monocytes during simulated extracorporeal circulation. Circulation Res 1993; 72: 1075-81.
9 Philippou H, Adami A, Davidson SJ, Pepper JR, Burman JF, Lane DA. Tissue factor is rapidly elevated in plasma collected from the pericardial cavity during cardiopulmonary bypass. Thromb Haemost 2000; 84: 124-8.
10 Davidson SJ, Burman JF, Rutherford LC, Keogh BF, Yacoub MH. High molecular weight kininogen deficiency: a patient who underwent cardiac surgery. Thromb Haemost 2001; 85: 195-7.
11 Burman JF, Chung HI, Lane DA, Philippou H, Adami A, Lincoln JCR. Role of factor XII in thrombin generation and fibrinolysis during cardiopulmonary bypass. Lancet 1994; 344: 1192-3.
12 Woodman RC, Harker LA. Bleeding complications associated with cardio-pulmonary bypass. Blood 1990; 76: 1680-97.
13 Nieuwland R, Berckmans RJ, Rotteveel-Eijkman RC, Maquelin KN, Roozendaal KJ, Jansen PGM, ten Have K, Eijsman L, Hack CE, Sturk A. Cell-derived microparticles generated in patients during cardiopulmonary bypass are highly procoagulant. Circulation 1997; 96: 3524-41.
14 Bradford HN, Dela Cadena RA, Kunapuli SP, Dong J-F, Lopez JA, Colman RW. Human kininogens regulate thrombin binding to platelets through the glycoprotein Ib-IX-V complex. Blood 1997; 90: 1508-15.
15 Cugno M, Nussberger J, Biglioli P, Giovagnoni MG, Gardinali M, Agostoni A. Cardiopulmonary bypass increases plasma bradykinin concentrations. Immunopharmacology 1999; 43: 145-7.
16 Chenoweth DE, Cooper SW, Hugli TE, Stewart RW, Blackstone EH, Kirklin JW. Complement activation during cardiopulmonary bypass: evidence for generation of C3a and C5a anaphylatoxins. N Engl J Med 1981; 304: 497-503.
17 Royston D, Bidstrup BP, Taylor KM, Sapsford RN. Effect of aprotinin on need for blood transfusion after repeat open-heart surgery. Lancet 1987; 2: 1289-91.
18 Davis R, Whittington R. Aprotinin: a review of its pharmacology and therapeutic efficacy in reducing blood loss associated with cardiac surgery. Drugs 1995; 49: 954-83.
19 Levi M, Cromheecke ME, de Jonge E, Prins MH, de Mol BJM, Briët E, Büller HR. Pharmacological strategies to decrease excessive blood loss in cardiac surgery: a meta-analysis of clinically relevant endpoints. Lancet 1999; 354: 1940-7.
20 Wong BI, McLean RF, Fremes SE, Deemar KA, Harrington EM, Christakis GT, Goldman BS. Aprotinin and tranexamic acid for high transfusion risk cardiac surgery. Ann Thorac Surg 2000; 69: 808-16.