Preoperative haemostasis testing does not predict requirement of blood products in cardiac surgery.

OBJECTIVE: Standard haemostasis screening tests are performed to reveal unknown congenital or acquired disturbances of plasma and/or platelet haemostasis. Since their diagnostic efficacy is often low, routinely performed haemostasis testing has been questioned. We investigated whether preoperatively assessed haemostasis testing can be used to predict the requirement of blood products. METHODS: We retrospectively assessed haemostasis parameters including platelet function testing by PFA 100 as well as the numbers of red blood cell (RBC) concentrates, fresh frozen plasmas (FFPs), and platelet concentrates (PCs) that were given peri-operatively and during the first two postoperative days in 2,831 cardiac surgery patients. Logistic regression analyses were used to select those parameters, which could predict blood product requirement. RESULTS: Of our study cohort, 56.5% needed RBCs, 15% FFPs, and 5% PCs. The need for RBCs was associated with significantly altered pre-operative values of most haemostasis parameters. However, by the use of logistic regression analysis fibrinogen was the only haemostasis parameter that was independently associated with the use of RBCs (odds ratio 1.56; 95% CI: 1.27-1.91; P <0.001). The predictive value of other parameters such as age, body weight, haemoglobin, and haematocrit was however much higher in comparison to fibrinogen (odds ratios: 1.92-3.50; P <0.001). It was not possible to develop a score based on haemostasis parameters to accurately identify patients at risk for RBC use. Moreover, we were unable to estimate the need for FFPs and PCs using preoperative haemostasis testing. CONCLUSIONS: Our data demonstrate that preoperatively performed haemostasis testing is not predictive in estimating the need for blood products in cardiac surgery patients.

Immunoglobulin preparations from hepatitis C antibody-positive plasma donors: influence on diagnosis and risk of infection in heart transplant recipients.

All heart transplant patients in our clinic received intravenous immunoglobulins as a prophylaxis against cytomegalovirus infections or reactivations. Serum was sampled from 160 heart transplant patients within 4 months after surgery. In 98 samples (61%) hepatitis C virus (HCV)-specific antibodies could be detected by a "second generation" enzyme immunoassay. Of these HCV antibody-positive patients 89 were tested for a second time. At this time, 5-11 months later, in 66 patients (74%) the HCV antibody had disappeared. In the 23 still positively reacting patients, immunoglobulins were given in the last 6 months before serum sampling. Nine commercial immunoglobulin preparations were tested for HCV-specific antibodies and the presence of HCV RNA. Seven preparations were anti-HCV positive with titres in the range of 64-256, whereas reverse transcription and polymerase chain reaction did not detect HCV RNA in any immunoglobulin preparation. Passive antibody transfer rather than a HCV infection is the cause of HCV antibody detection in our patients. The presence of HCV antibodies in high concentrations in commercial immunoglobulin preparations may only be explained by an extremely high proportion of anti-HCV-positive single donations in the plasma pools used for immunoglobulin production. The passive HCV antibody transmission prevents anti-HCV serological monitoring of patients treated with these preparations. Additionally, there are reports on the transmission of hepatitis non-A, non-B via immunoglobulin preparations. Therefore, we recommend an anti-HCV screening of plasma donors.

Synthesis of hepatic glycosaminoglycans in the early stages of galactosamine hepatitis: a rapid decline of heparan sulfate is followed by elevation of chondroitin sulfate and dermatan sulfate.

Administration of a single dose of D-galactosamine to rats causes time-dependent, biphasic changes of total glycosaminoglycan synthesis in liver. A rapidly occurring inhibition is followed by a significantly enhanced (greater than 2 fold) production of 35S-labeled glycosaminoglycans in later stages of injury. Degree and duration of the inhibitory phase are dose-dependent; 50% inhibition is reached at 80 mg/kg and maximum inhibition (nearly 80%) at about 300 mg/kg body weight 2 h after injection of D-galactosamine. The hepatotoxin impairs preferentially the production of heparan sulfate, whereas that of chondroitin sulfate and dermatan sulfate is diminished only slightly and for a rather short period of time. The synthesis of the latter, however, is more stimulated than that of heparan sulfate in later stages of injury. The specific radioactivity of 35S-labeled 3'-phosphoadenosine-5'-phosphosulfate (PAPS) did not change significantly during the course of acute liver damage. Glycosaminoglycan synthesis in regenerating liver was nearly unaffected by D-galactosamine. Uridine at the dose applied partially reversed D-galactosamine-inhibited synthesis of proteoheparan sulfate. In accordance with the labeling studies the content of glucosamine-containing glycosaminoglycans in treated liver decreased, whereas that of galactosamine-containing glycosaminoglycans slightly increased, resulting in a nearly 50% reduction of the glucosamine/galactosamine ratio 5 h after administration of D-galactosamine. Ion exchange chromatographic studies of 35S-labeled specific types of glycosaminoglycans from normal and galactosamine-injured liver revealed only minor structural differences.

Metabolic and structural studies on serum- and liver-glycosaminoglycans in normal and liver-injured rats.

The incorporation of [35S]sulfate into total and specific types of serum glycosaminoglycans was studied in rats with acute, subacute or chronic liver injury (liver cirrhosis), and compared with that of normal rats. The macromolecular (protein-bound) nature of serum glycosaminoglycans in normal and diseased animals was also analysed. The results show a strong increase in rate and extent of [35S]sulfate incorporation into total serum glycosaminoglycans for acutely but a decrease for subacutely and chronically liver damaged rats. The time-course of distribution of label between serum chondroitin sulfate and dermatan sulfate exhibits significant changes in liver-injured animals, in particular a relatively high proportion of dermatan [35S]sulfate in rats with cirrhotic livers. In comparison with serum glycosaminoglycans the labeling profile of glycosaminoglycans in the cirrhotic liver was quite different (heparan sulfate:dermatan sulfate:chondroitin sulfate = 1:0.34:0.09) and changed only insignificantly during a 1 h labeling period. The protein-bound moiety of serum glycosaminoglycans was not affected by liver disease; but the elution profile of chondroitin [35S]sulfate from Dowex 1 X 2 for treated rats was altered, thus indicating a structural modification of its carbohydrate chain.