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Gene Review

THBD  -  thrombomodulin

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Disease relevance of THBD

  • The decrease in thrombomodulin was twice as great compared with the general decline in total protein synthesis in hypoxia [1].
  • Finally, to gain insight into the role of this coiled coil in the infectious potential of BLV in vivo, the mutated TM genes were introduced in an infectious and pathogenic molecular clone and injected into sheep [2].
  • Many retroviruses, including bovine leukemia virus (BLV), contain a highly conserved region located about 40 amino acids downstream from the fusion peptide within the sequence of the external domain of the transmembrane (TM) protein [2].
  • These results indicate that CSA produces a time- and dose-dependent reduction in thrombomodulin activity of cultured endothelial cells, downregulating the protein C anticoagulant pathway, thereby increasing the risk of thrombosis [3].
  • The recombinant TM protein of JDV also reacted with antibody from the JDV infected cattle and with the BIV antisera [4].

High impact information on THBD


Chemical compound and disease context of THBD


Biological context of THBD


Anatomical context of THBD

  • The sensitivity of TM mRNA expression by flow was found to be specific to endothelium, since it was not observed in BSM cells exposed to steady laminar shear stress of 15 dynes/cm2 [14].
  • We have explored the role of fluid shear stress, imparted on the luminal surface of the endothelial cell as a result of blood flow, on the expression of TM mRNA and protein in both bovine aortic endothelial (BAE) and bovine smooth muscle (BSM) cells in an in vitro system [14].
  • We conclude that TM at the blood-brain barrier is likely to be an important physiologic anticoagulant in brain microcirculation [15].
  • Incubation of brain capillaries with retinoic acid (10 mumol/L) and dibutyryl cAMP (3 mmol/L) resulted in a 4-fold increase in TM mRNA at 4 and 8 hours, respectively, followed by an increase in protein C activation [15].
  • cAMP influence on transcription of thrombomodulin is dependent on de novo synthesis of a protein intermediate: evidence for cohesive regulation of myogenic proteins in vascular smooth muscle [16].

Associations of THBD with chemical compounds


Other interactions of THBD


Analytical, diagnostic and therapeutic context of THBD

  • At PO2 approximately 14 mm Hg thrombomodulin antigen and functional activity on the cell surface were diminished by 80-90%, and Northern blots demonstrated suppression of thrombomodulin mRNA [1].
  • Both surface expressed TM (antigen and activity), and the total TM pool (measured by radioimmunoassay and activity in detergent extracts) dropped to less than or equal to 20% of control values within 12 hours of TNF treatment [9].
  • In addition, it appeared that the integrity of the TM coiled coil structure is essential for envelope protein multimerization, as analyzed by metrizamide gradient centrifugation [2].
  • We then used quantitative-competitive PCR to compare thrombomodulin expression in endothelial monocultures and astrocyte-endothelial cocultures after 1 and 7 days of culture [13].
  • There was no significant difference in thrombomodulin mRNA expression for cocultures versus monocultures after 1 day [13].


  1. Hypoxia modulates the barrier and coagulant function of cultured bovine endothelium. Increased monolayer permeability and induction of procoagulant properties. Ogawa, S., Gerlach, H., Esposito, C., Pasagian-Macaulay, A., Brett, J., Stern, D. J. Clin. Invest. (1990) [Pubmed]
  2. Conservative mutations in the immunosuppressive region of the bovine leukemia virus transmembrane protein affect fusion but not infectivity in vivo. Gatot, J.S., Callebaut, I., Mornon, J.P., Portetelle, D., Burny, A., Kerkhofs, P., Kettmann, R., Willems, L. J. Biol. Chem. (1998) [Pubmed]
  3. Decrease in endothelial cell-dependent protein C activation induced by thrombomodulin by treatment with cyclosporine. Garcia-Maldonado, M., Kaufman, C.E., Comp, P.C. Transplantation (1991) [Pubmed]
  4. Recombinant Jembrana disease virus proteins as antigens for the detection of antibody to bovine lentiviruses. Burkala, E.J., Narayani, I., Hartaningsih, N., Kertayadnya, G., Berryman, D.I., Wilcox, G.E. J. Virol. Methods (1998) [Pubmed]
  5. Endothelial receptor-mediated binding of glucose-modified albumin is associated with increased monolayer permeability and modulation of cell surface coagulant properties. Esposito, C., Gerlach, H., Brett, J., Stern, D., Vlassara, H. J. Exp. Med. (1989) [Pubmed]
  6. Solution structure of the smallest cofactor-active fragment of thrombomodulin. Wood, M.J., Sampoli Benitez, B.A., Komives, E.A. Nat. Struct. Biol. (2000) [Pubmed]
  7. Characterization of a thrombomodulin cDNA reveals structural similarity to the low density lipoprotein receptor. Jackman, R.W., Beeler, D.L., VanDeWater, L., Rosenberg, R.D. Proc. Natl. Acad. Sci. U.S.A. (1986) [Pubmed]
  8. Bovine leukemia virus gp30 transmembrane (TM) protein is not tyrosine phosphorylated: examining potential interactions with host tyrosine-mediated signaling. Hamilton, V.T., Stone, D.M., Pritchard, S.M., Cantor, G.H. Virus Res. (2002) [Pubmed]
  9. Tumor necrosis factor leads to the internalization and degradation of thrombomodulin from the surface of bovine aortic endothelial cells in culture. Moore, K.L., Esmon, C.T., Esmon, N.L. Blood (1989) [Pubmed]
  10. The active site of the thrombin-thrombomodulin complex. A fluorescence energy transfer measurement of its distance above the membrane surface. Lu, R.L., Esmon, N.L., Esmon, C.T., Johnson, A.E. J. Biol. Chem. (1989) [Pubmed]
  11. The effect of bovine thrombomodulin on the specificity of bovine thrombin. Jakubowski, H.V., Kline, M.D., Owen, W.G. J. Biol. Chem. (1986) [Pubmed]
  12. Thrombomodulin blocks the ability of thrombin to activate platelets. Esmon, N.L., Carroll, R.C., Esmon, C.T. J. Biol. Chem. (1983) [Pubmed]
  13. Regulation of brain capillary endothelial thrombomodulin mRNA expression. Tran, N.D., Wong, V.L., Schreiber, S.S., Bready, J.V., Fisher, M. Stroke (1996) [Pubmed]
  14. Endothelial expression of thrombomodulin is reversibly regulated by fluid shear stress. Malek, A.M., Jackman, R., Rosenberg, R.D., Izumo, S. Circ. Res. (1994) [Pubmed]
  15. Thrombomodulin expression in bovine brain capillaries. Anticoagulant function of the blood-brain barrier, regional differences, and regulatory mechanisms. Wang, L., Tran, N.D., Kittaka, M., Fisher, M.J., Schreiber, S.S., Zlokovic, B.V. Arterioscler. Thromb. Vasc. Biol. (1997) [Pubmed]
  16. cAMP influence on transcription of thrombomodulin is dependent on de novo synthesis of a protein intermediate: evidence for cohesive regulation of myogenic proteins in vascular smooth muscle. Traynor, A.E., Cundiff, D.L., Soff, G.A. J. Lab. Clin. Med. (1995) [Pubmed]
  17. Reconstitution of rabbit thrombomodulin into phospholipid vesicles. Galvin, J.B., Kurosawa, S., Moore, K., Esmon, C.T., Esmon, N.L. J. Biol. Chem. (1987) [Pubmed]
  18. Formation of activated protein C and inactivation of cell-bound thrombin by antithrombin III at the surface of cultured vascular endothelial cells--a comparative study of two anticoagulant mechanisms. Delvos, U., Meusel, P., Preissner, K.T., Müller-Berghaus, G. Thromb. Haemost. (1987) [Pubmed]
  19. Chelerythrine, a selective protein kinase C inhibitor, counteracts pyrogen-induced expression of tissue factor without effect on thrombomodulin down-regulation in endothelial cells. Herbert, J.M., Savi, P., Laplace, M.C., Dumas, A., Dol, F. Thromb. Res. (1993) [Pubmed]
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