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Antithrombin is a member of the serpin family of natural anticoagulant proteins that inhibits the serine proteases thrombin, factor Xa, and factor VIIa. Hepatic synthesis of antithrombin may be impaired by chronic liver disease; however, it remains unknown how the levels of circulating antithrombin are maintained. To determine whether the second synthesis of antithrombin is occurring in the diseased liver, we assessed antithrombin levels in five groups of patients with chronic liver disease. The patients were classified into four groups on the basis of the severity of their liver disease and shown to have similar levels of antithrombin in the liver. The groups included were normal subjects (n = 8), patients with chronic hepatitis (n = 12), patients with cirrhosis (n = 4), and patients with portal hypertension (n = 8). Immunoprecipitation of [35S]cysteine-labeled antithrombin from serum revealed that most of the antithrombin secreted into the circulation was synthesized in the liver (80% to 85% in normal subjects). However, the immunoprecipitated antithrombin had a lower molar ratio of protease inhibitory activity to antithrombin than that in normal subjects; thus, the antithrombin in chronic liver disease is less effective at inhibiting thrombin and factor Xa and converting protein C. The second synthesis of antithrombin in the diseased liver does not compensate for the reduced thrombin inhibition. We conclude that the levels of circulating antithrombin are maintained by the second synthesis in the diseased liver, and thrombin inhibition is reduced because of the low antithrombin levels.Sir,

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