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  • Title: Receptor-mediated endocytosis of thrombin-antithrombin III complex by the human monocytoid cell line U937.
    Author: Takeya H, Hamada T, Kume M, Suzuki K.
    Journal: Biochem Biophys Res Commun; 1994 May 16; 200(3):1334-40. PubMed ID: 8185584.
    Abstract:
    Receptor-mediated endocytosis of thrombin-antithrombin III (TAT) complex was characterized with the monocytoid cell line U937. At 4 degrees C, U937 cells bound TAT but not antithrombin III in a rapid, specific, saturable, and reversible manner. [125I]TAT binding to U937 cells was not inhibited by antithrombin III and hardly by thrombin, but 75% inhibited by a 50 molar excess of the unlabeled TAT. There were about 79,000 binding sites/cell (Kd = 68 nM). The TAT receptor on U937 cells may be distinct from the serpin-enzyme complex (SEC) receptor, since a synthetic peptide corresponding to the recognition sequence of SEC receptor did not compete with TAT binding to the cells. Receptor-bound TAT was internalized into the cells after switching the temperature from 4 to 37 degrees C and thereafter degraded in lysosomes.
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