Transfusion-related acute lung injury (TRALI): A Canadian blood services research and development symposium.

Since the first description of transfusion-related acute lung injury (TRALI) more than 2 decades ago, we have only recently begun to learn how this disorder may occur and how to prevent it. Scientists from around the world have made great strides in identifying the possible causes of this condition. Blood banks and transfusion services have risen to the challenges of prevention. Recent introduction of restricting most plasma products to those obtained from male donors only has greatly reduced the incidence of TRALI worldwide. Scientists have recently identified the gene and protein for the human neutrophil antigen-3a associated with most mortality due to TRALI, and this presents an opportunity for a screening assay to prevent future TRALI-associated deaths. Finally, animal models of TRALI have provided insight into the possible mechanisms of this disorder and can be used to explore potential treatment modalities.

Evaluation of platelet gel characteristics using thrombin produced by the thrombin processing device: a comparative study.

PURPOSE: Autologous platelet gels can be prepared using the patient's own platelet-rich plasma and thrombin produced by the Thrombin Processing Device (Thermogenesis Corp, Rancho Cordova, CA). As the Thrombin Processing Device thrombin contains a residual amount of ethanol, the purpose of this study was to investigate the effect of the Thrombin Processing Device thrombin on growth factor release from platelet gels, and the effect on cell viability and cell proliferation. MATERIALS AND METHODS: Platelet gels were prepared using Thrombin Processing Device-produced human thrombin at platelet-rich plasma to thrombin ratios of 3.3 to 1 and 7 to 1. Commercially available bovine thrombin was used as control. The content of the growth factors, platelet-derived growth factor beta polypeptide, and transforming growth factor beta, were assessed in both the clot and supernatant. The influence of different concentrations of ethanol on cell viability was assessed by flow cytometry and cell proliferation was assessed by (3)H-thymidine incorporation. RESULTS: Using a ratio of 3.3 to 1, the supernatant of the platelet gel produced with Thrombin Processing Device thrombin had a lower growth factor content compared with bovine thrombin but was similar when prepared using a ratio of platelet-rich plasma to thrombin of 7 to 1. Supernatants from the platelet gels did not affect the viability of human macrophage line cells or a fibroblast cell line. When the different platelet gels or their supernatants were tested for their ability to stimulate cell proliferation, similar rates of proliferation were observed. CONCLUSIONS: These data suggest that residual ethanol in the Thrombin Processing Device-produced thrombin does not affect any of the tested parameters and has similar characteristics as commercially available bovine thrombin.

Stability of human thrombin produced from 11 ml of plasma using the thrombin processing device.

Autologous thrombin can be produced by activating the patient's own plasma. By adding calcium chloride (CaCl2) to the anticoagulated plasma, the coagulation cascade will be initiated, and active thrombin will be produced. However, thrombin obtained by this method degrades very quickly and is not practical for use during surgery. The aim of this study was to investigate the stability of the thrombin produced using the thrombin processing device (TPD; Thermogenesis Corporation). The TPD consists of a tubular chamber containing a negatively charged surface for activation. Plasma (11 ml) and reagent (CaCl2 and ethanol, 3.75 ml) were added to the TPD, and active thrombin was harvested after a 20-minute incubation. The production of thrombin was done at 18 degrees C (64 degrees F), 24 degrees C (75 degrees F), and 27 degrees C (81 degrees F) (n = 4/group). The produced thrombin was stored at the production temperature, 4 degrees C (39 degrees F), and 35 degrees C (95 degrees F). The thrombin activity was assessed by time to clot formation, using a fibrinogen concentrate as substrate, after 2, 4, and 6 hours of storage. Thrombin produced at 18 degrees C had clot times of less than 5 seconds for 2 hours (4.42 +/- 1.3 seconds) when stored at 4 degrees C, but 4 hours (4.1 +/- 1.3 seconds) when stored at 35 degrees C. In contrast, when thrombin was produced at 24 degrees C, the clot times were 4.3 +/- 0.7 and 4.6 +/- 1.6 seconds at 4 degrees C and 35 degrees C, respectively, for up to 6 hours. Similar results were obtained for thrombin produced at 27 degrees C. Active thrombin produced by the TPD is dependent on both the production temperature and the storage temperature. Autologous human thrombin with a stability of up to 6 hours can be obtained using the TPD when produced at 24 degrees C or 27 degrees C and stored at 4 degrees C.