Biotechnological traps for the reduction of inflammation due to cardiopulmonary bypass operations

Cardiopulmonary bypass induces a systemic inflammatory response (SIR), characterized by the activation of cellular and humoral elements, with concomitant release of neutrophil elastase and matrix-metallo proteinases. In the present study, the protease release during extracorporeal circulation in 28...

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Bibliographic Details
Published in:Biomaterials 2006-07, Vol.27 (20), p.3855-3862
Main Authors: Grano, Valentina, Salamino, Franca, Melloni, Edon, Minafra, Roberto, Regola, Eliana, Diano, Nadia, Nicolucci, Carla, Attanasio, Angelina, Nappi, Gianantonio, Cotrufo, Maurizio, Maresca, Lucio, De Santo, Natale Gaspare, Mita, Damiano Gustavo
Format: Article
Language:English
Subjects:
Animals
Biotechnology
Blood flow
Cardiopulmonary Bypass - adverse effects
Cell activation
Enzyme Inhibitors - chemistry
Enzyme Inhibitors - therapeutic use
Extracorporeal circulation
Female
Humans
Inflammation
Inflammation - etiology
Inflammation - therapy
Membranes, Artificial
Middle Aged
Molecular Structure
Peptide Hydrolases - blood
Surface grafting
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Summary:Cardiopulmonary bypass induces a systemic inflammatory response (SIR), characterized by the activation of cellular and humoral elements, with concomitant release of neutrophil elastase and matrix-metallo proteinases. In the present study, the protease release during extracorporeal circulation in 28 patients undergoing cardiac surgical operations was monitored using casein zymography. A peak in protease activity was found in all patients at the end of cardiopulmonary bypass. Plasma samples of patients were allowed to interact with different traps obtained by immobilizing different protease inhibitors on specific carriers. α 1-Antitpypsin, Bovine Pancreatic Trypsin Inhibitor, Elastatinal or Leupeptin were used as inhibitors and were covalently immobilized by diazotization or by condensation. A reduction in the proteolytic activity of the plasma samples was observed after interaction with the different traps. The most efficient traps, i.e. the ones displaying greatest power to inhibit protease activity, were those obtained by immobilizing Bovine Pancreatic Trypsin Inhibitor and Leupeptin. The biocompatibility of traps was also tested. Results show that protease activity in blood can be decreased by our protease traps.
ISSN:0142-9612
1878-5905
DOI:10.1016/j.biomaterials.2006.02.029