Biochemical Properties | transmembrane proteoglycan
receptor of thrombinl; cofactor of thrombin-catalyzed
activation of protein C, and inhibits the procoagulant functions of thrombin; protein is very stable and compact
because of several disulphur bridges; The long extracellular domain at the
NH2-terminal part includes: a lectin-like domain
necessary for TM endocytosis, a domain with 6
EGF-like repeats, among which the last three are
necessary for protein C activation by thrombin, and a
serine-threonine rich domain, putative sites of glycosylation
responsible for the binding of a trisulphated
chondroitin-sulphate, of importance in Plasmodium
falciparum malaria; contains a hydrophobic
transmembrane domain of 23 amino acids and a short
intracytoplasmic tail probably associated with endocytosis
and degradation. |
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Bibliography | 1. Esmon, C. T. (1995) Thrombomodulin as a model of molecular mechanisms that modulate protease specificity and function at the vessel surface. FASEB J. 9, 946–955. 2. Bourin, M. C., Lundgren-Akerlund, E., and Lindahl, U. (1990) Isolation and characterization of the glycosaminoglycan component of rabbit thrombomodulin proteoglycan. J. Biol. Chem. 265, 15424–15431. 3. Conway, E. M., Pollefeyt, S., Collen, D., and Steiner-Mosonyi, M. (1997) The amino terminal lectin-like domain of thrombomodulin is required for constitutive endocytosis. Blood 89, 652–661. 4. Gysin, J., Pouvelle, B., Le Tonquèze, M., Edelman, L., and Boffa, M. C. (1997) Chondroitin sulfate of thrombomodulin is an adhesion receptor for Plasmodium falciparum-infected erythrocytes. Mol. Biochem. Parasitol. 88, 267–271. 5. Boffa, M. C., Jackman, R. W., Peyri, N., Boffa, J. F., and George, B. (1991) Thrombomodulin in the central nervous system. Nouv. Rev. Fr. Hematol. 33, 423–429. 6. Boffa, M. C., Burke, B., and Haudenschild, C. C. (1987) Preservation of thrombomodulin antigen on vascular and extravascular surfaces. J. Histochem. Cytochem. 35, 1267–1276. 7. Pruna, A., Peyri, N., Berard, M., and Boffa, M. C. (1997) Thrombomodulin is synthesized by human mesangial cells. Kidney Int. 51, 687–693. |