Antithrombin: A bloody important serpin

Advances in Experimental Medicine and Biology

Volumn 425, Issue , 1997, Pages 17-33

  Björk, Ingemar ^a   Olson, Steven T ^b  

^a SWEDISH UNIVERSITY OF AGRICULTURAL SCIENCES   (Sweden)

^b UNIVERSITY OF ILLINOIS AT CHICAGO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANTITHROMBIN; BLOOD CLOTTING FACTOR 10A; GLYCOSAMINOGLYCAN; HEPARAN SULFATE; HEPARIN; SERINE PROTEINASE INHIBITOR; THROMBIN;

ANTITHROMBIN DEFICIENCY; ARTICLE; BLOOD CLOTTING; CHEMICAL STRUCTURE; CONFORMATIONAL TRANSITION; ENZYME INACTIVATION; ENZYME INHIBITOR INTERACTION; HEMOSTASIS; MAST CELL; PRIORITY JOURNAL; PROTEINASE INHIBITION; VEIN THROMBOSIS;

EID: 0031455114     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4615-5391-5_3     Document Type: Article

References (17)

1. 1-proteinase inhibitor. Biochem. Biophys. Res. Commun. 95: 864-871.
2. 1-Antitrypsin and the serpins: variation and countervariation. Trends Biochem. Sci. 10: 20-24.
3. Huber, R. and Carrell, R.W. (1989) Implications of the three-dimensional structure of alpha I-antitrypsin for structure and function of serpins. Biochemistry 28: 8951-8966.
4. 1-antitrypsin and antithrombin III. pp. 43-54, In "The Physiological Inhibitors of Blood Coagulation and Fibrinolysis" (Eds., Collen, D., Wiman, B. and Verstraete, M.), Elsevier/North-Holland, Amsterdam.
5. Bock, S.C., Wion, K.L., Vehar, G.A. and Lawn, R.M. (1982) Cloning and expression of the cDNA for human antithrombin III. Nucleic Acids Res. 10: 8113-8125.
6. Prochownik, E.V., Markham, A.F. and Orkin, S.H. (1983) Isolation of a cDNA clone for human antithrombin III. J. Biol. Chem. 258: 8389-8394.
7. Chandra, T., Stackhouse, R., Kidd, V.J. and Woo, S.L. (1983) Isolation and sequence characterization of a cDNA clone of human antithrombin III. Proc. Natl. Acad. Sci. U. S. A. 80: 1845-1848.
8. Carlson, T.H. and Atencio, A.C. (1982) Isolation and partial characterization of two distinct types of antithrombin III from rabbit. Thromb. Res. 27: 23-34.
9. Peterson, C.B. and Blackburn, M.N. (1985) Isolation and characterization of an antithrombin III variant with reduced carbohydrate content and enhanced heparin binding. J. Biol. Chem. 260: 610-615.
10. Brennan, S.O., George, P.M. and Jordan, R.E. (1987) Physiological variant of antithrombin-III lacks carbohydrate sidechain at Asn 135. FEBS Lett. 219: 431-436.
11. Picard, V., Ersdal-Badju, E. and Bock, S.C. (1995) Partial glycosylation of antithrombin III asparagine-135 is caused by the serine in the third position of its N-glycosylation consensus sequence and is responsible for production of the β-antithrombin III isoform with enhanced heparin affinity. Biochemistry 34: 8433-8440.
12. Franzén, L.E., Svensson, S. and Larm, O. (1980) Structural studies on the carbohydrate portion of human antithrombin III. J. Biol. Chem. 255: 5090-5093.
13. Mizuochi, T., Fujii, J., Kurachi, K. and Kobata, A. (1980) Structural studies of the carbohydrate moiety of human antithrombin III. Arch. Biochem. Biophys. 203: 458-465.
14. Stephens, A.W., Siddiqui, A. and Hirs, C.H. (1987) Expression of functionally active human antithrombin III. Proc. Natl. Acad. Sci. U. S. A. 84: 3886-3890.
15. ZettlmeissI, G., Conradt, H.S., Nimtz, M. and Karges, H.E. (1989) Characterization of recombinant human antithrombin III synthesized in Chinese hamster ovary cells. J. Biol. Chem. 264: 21153-21159.
16. Gillespie, L.S., Hillesland, K.K. and Knauer, D.J. (1991) Expression of biologically active human antithrombin III by recombinant baculovirus in Spodoptera frugiperda cells. J. Biol. Chem. 266: 3995-4001.
17. Ersdal-Badju, E., Lu, A., Peng, X., Picard, V., Zendehrouh, P., Turk, B., Björk, I., Olson, S.T. and Bock, S.C. (1995) Elimination of glycosylation heterogeneity affecting heparin affinity of recombinant human antithrombin III by expression of a β-like variant in baculovirus-infected insect cells. Biochem. J. 310: 323-330.