Heparinase thromboelastography compared with activated coagulation time for protamine titration after cardiopulmonary bypass.

OBJECTIVE: The present study is a comparison of two point-of-care (POC) tests as endpoints of protamine titration after CPB. The authors hypothesized that using the heparinase-kaolin thromboelastography (TEG-HK) R-time difference would more readily identify residual heparin necessitating additional protamine than when using activated coagulation time (ACT). The primary endpoint was the between-group difference in protamine dose. Whether this approach would lessen postoperative bleeding and sequelae also was investigated. DESIGN: Single center, blinded, prospective, randomized study. SETTING: University teaching hospital. PARTICIPANTS: Eighty-two adult patients for on-pump coronary artery bypass and/or valve surgery. INTERVENTIONS: Patients were randomized. In the ACT group, protamine was titrated until ACT did not exceed baseline by more than 10%. In the TEG group, a TEG-HK R-time difference less than 20% was targeted. Protamine was repeated to achieve the endpoints. Clinicians in the ACT group were blinded to TEG data and vice versa. MEASUREMENTS AND MAIN RESULTS: There was no between-group difference in total protamine dose (3.9 ± 0.6 and 4.2 ± 0.7; 95% CI of the difference between means: -0.544 to 0.008 mg/kg; p = 0.057) or protamine:heparin ratios (1.3:1 and 1.4:1; 95% CI of the difference between means: -0.05 to 0.03 mg/mg; p = 0.653). In the ACT group, 17% of patients required a second protamine dose, and in the TEG group, 24% of patients required a second protamine dose. No between-group differences in the postoperative transfusion requirements or intensive care unit length of stay were demonstrated. CONCLUSION: No difference was identified in protamine dosing using either ACT or TEG-HK R-time difference as endpoints. Heparinase TEG may be useful for monitoring heparin reversal.

On the non-linear attachment characteristics of blood to bacterial cellulose/kaolin biomaterials.

In this communication, we report a non-linear variation in the strength of blood attachment to bacterial cellulose/kaolin biomaterials as the fractions of bacterial cellulose to kaolin are increased. The changes observed for attachment strength are elucidated following both experimental and numerical investigations on both the biomaterial and the blood-biomaterial interface. Our research reveals that the non-linear strength of attachment of blood is related to topographical characteristics on the surface of the biomaterial, the maleability of the biomaterial and the intermolecular strength of attraction between clotted blood proteins (fibrinogen) with the cellulose/kaolin components of the biomaterial.

Studies of the mechanisms of bradykinin generation in hereditary angioedema plasma.

BACKGROUND: Factor XII-dependent bradykinin formation is thought to be responsible for the swelling associated with the various forms of C1 inhibitor deficiency, and complement activation is augmented during attacks of swelling. OBJECTIVES: To further elucidate the interactions of the kinin-forming cascade that lead to complement activation during attacks of swelling and to determine whether fibrinolysis is augmented as well. METHODS: We compared spontaneous and kaolin-induced activation of normal plasma with the plasma of patients with hereditary angioedema. RESULTS: Hereditary angioedema plasma demonstrated augmented factor XII activation, production of factor XIIf, prekallikrein activation, and high-molecular-weight kininogen cleavage, and, as a result, bradykinin formation was markedly increased. Baseline levels of C4a and plasmin-alpha 2 antiplasmin complexes increased, and, on activation with kaolin, levels increased further. CONCLUSIONS: All parameters indicative of activation of the bradykinin-forming cascade are activated in hereditary angioedema plasma vs normal plasma. Production of factor XIIf, demonstrated for the first time in whole plasma, may be responsible for C1 activation based on C4a production. The factor XII-dependent fibrinolytic cascade is also activated.