Antithrombin Murcia (K241E) causing antithrombin deficiency: A possible role for altered glycosylation

Haematologica

Volumn 95, Issue 8, 2010, Pages 1358-1365

  Martínez Martínez, Irene ^a   Ordóñez, Adriana ^a   Navarro Fernández, José ^b   Pérez Lara, Ángel ^b   Gutiérrez Gallego, Ricardo ^c,d   Giraldo, Rafael ^e   Martínez, Constantino ^a   Llop, Esther ^c   Vicente, Vicente ^a   Corral, Javier ^a  

^a HOSPITAL UNIVERSITARIO MORALES MESEGUER   (Spain)

^b UNIVERSITY OF MURCIA   (Spain)

^c HOSPITAL DEL MAR   (Spain)

^d UNIVERSITAT POMPEU FABRA   (Spain)

^e CENTRO DE INVESTIGACIONES BIOLÓGICAS   (Spain)

Author keywords

Antithrombin; Glycosylation; Heparin

Indexed keywords

ANTICOAGULANT AGENT; ANTITHROMBIN; ANTITHROMBIN MURCIA; BLOOD CLOTTING FACTOR 5 LEIDEN; DNA; HEPARIN; PHOSPHOLIPID ANTIBODY; PROTEIN C; PROTEIN S; PROTEINASE; PROTHROMBIN; RNA; SERINE PROTEINASE INHIBITOR; UNCLASSIFIED DRUG;

ADULT; ANTICOAGULATION; ANTITHROMBIN DEFICIENCY; ARTICLE; BINDING AFFINITY; BINDING SITE; BIOCHEMISTRY; BLOOD SAMPLING; CASE REPORT; DEEP VEIN THROMBOSIS; FAMILY STUDY; FEMALE; FUCOSYLATION; GENE DELETION; GENE MUTATION; GENETIC VARIABILITY; GLYCOBIOLOGY; GLYCOSYLATION; HUMAN; HUMAN CELL; MALE; MASS SPECTROMETRY; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; MISSENSE MUTATION; MOLECULAR WEIGHT; NONSENSE MUTATION; PATHOGENESIS; PLEIOTROPY; POLYMERASE CHAIN REACTION; PROTEOMICS; RISK ASSESSMENT; RNA STABILITY; THROMBOSIS; WILD TYPE;

ADULT; AMINO ACID SUBSTITUTION; ANTITHROMBIN III; ANTITHROMBIN III DEFICIENCY; BASE SEQUENCE; BLOTTING, WESTERN; FEMALE; GENETIC PREDISPOSITION TO DISEASE; GLYCOSYLATION; HUMANS; MALE; MODELS, MOLECULAR; MUTATION; PEDIGREE; PROTEIN CONFORMATION;

EID: 77956032246     PISSN: 03906078     EISSN: 15928721     Source Type: Journal    
DOI: 10.3324/haematol.2009.015487     Document Type: Article

References (27)

1. Quinsey NS, Greedy AL, Bottomley SP, Whisstock JC, Pike RN. Antithrombin: in control of coagulation. Int J Biochem Cell Biol. 2004;36(3):386-9.
2. Cooper DN, Ball EV, Stenson PD, Phillips AD, Howells K, Mort ME, Thomas NST. The Human Gene Mutation Database. http://www.hgmd.cf.ac.uk/ac/gene.php?gene=SERPINC1. 2009
3. Lane DA, Bayston T, Olds RJ, Fitches AC, Cooper DN, Miller DS, Jochmans K, Perry DJ, Okajima K, Thein SL, Emmerich J. Antithrombin mutation database: 2nd (1997) update. Thromb Haemost. 1997; 77(1):197-211.
4. Corral J, Vicente V, Carrell RW. Thrombosis as a conformational disease. Haematologica. 2005;90(2):238-46.
5. Olson ST, Björk I, Bock SC. Identification of critical molecular interactions mediating heparin activation of antithrombin. Trends Cardiovasc Med. 2002;12(5):198-205.
6. Johnson DJ, Langdown J, Li W, Luis SA, Baglin TP, Huntington JA. Crystal structure of monomeric native antithrombin reveals a novel reactive center loop conformation. J Biol Chem. 2006;281(46):35478-86.
7. Langdown J, Belzar KJ, Savoir WJ, Baglin TP, Huntington JA. The critical role of hinge-region expulsion in the induced-fit heparin binding mechanism of antithrombin. J Mol Biol. 2009;386(5):1278-89.
8. Corral J, Huntington JA, Gonzalez-Conejero R, Mushunje A, Navarro M, Marco P, et al. Mutations in the shutter region of antithrombin result in formation of disulfide-linked dimers and severe venous thrombosis. J Thromb Haemost. 2004;2(6):931-9.
9. Corral J, Rivera J, Martínez C, Gónzalez-Conejero R, Miñano A, Vicente V. Detection of conformational transformation of antithrombin in blood with crossed immunoelectrophoresis: new application for a classical method. J Lab Clin Med. 2003; 142(5):298-305.
10. Mushunje A, Evans G, Brennan SO, Carrell RW, Zhou A. Latent antithrombin and its detection, formation and turnover in the circulation. J Thromb Haemost. 2004; 2(12):2170-7.
11. Shevchenko A, Wilm M, Vorm O, Mann M. Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal Chem. 1996;68(5):850-8.
12. Mushunje A, Zhou A, Carrell RW, Huntington JA. Heparin-induced substrate behavior of antithrombin Cambridge II. Blood. 2003;102(12):4028-34.
13. Guex N, Peitsch MC. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modelling. Electrophoresis. 1997;18(15):2714-23.
14. Baker NA, Sept D, Joseph S, Holst MJ, McCammon JA. Electrostatics of nanosystems: application to microtubules and the ribosome. Proc Natl Acad Sci USA. 2001; 98(8):10037-41.
15. Sanner MF. Python: a programming language for software integration and development. J Mol Graphics Mod. 1999;17(1):57-61.
16. Picard V, Ersdal-Badju E, Bock SC. 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 b-antithrombin III isoform with enhanced heparin affinity. Biochemistry. 1995;34(26):8433-40.
17. McCoy AJ, Pei XY, Skinner R, Abrahams JP, Carrell RW. Structure of beta-antithrombin and the effect of glycosylation on antithrombin's heparin affinity and activity. J Mol Biol. 2003;326(3):823-33.
18. Muller R, Marchetti M, Kratzmeier M, Elgass H, Kuschell M, Zenker A, Allmaier G. Comparison of planar SDS-PAGE, CGEon-the-chip and MALDI-TOF mass spectrometry for the analysis of the enzymatic de-N-glycosylation of antithrombin III and coagulation factor IX with PNGase F. Anal Bioanal Chem. 2007;389(6):1859-68.
19. Garone L, Edmunds T, Hanson E, Bernasconi R, Huntington JA, Meagher JL, et al. Antithrombin-heparin affinity reduced by fucosylation of carbohydrate at asparagine 155. Biochemistry. 1996;35(27): 8881-9.
20. Björk I, Ylinenjärvi K, Olson ST, Hermentin P, Conradt HS, Zettlmeissl G. Decreased affinity of recombinant antithrombin for heparin due to increased glycosylation. Biochem J. 1992;286(Pt 3):793-800.
21. Olson ST, Frances-Chmura AM, Swanson R, Björk I, Zettlmeissl G. Effect of individual carbohydrate chains of recombinant antithrombin on heparin affinity and on the generation of glycoforms differing in heparin affinity. Arch Biochem Biophys. 1997;341(2):212-21.
22. Demelbauer UM, Plematl A, Kremser L, Allmaier G, Josic D, Rizzi A. Characterization of glyco isoforms in plasma-derived human antithrombin by online capillary zone electrophoresis-electrospray ionization-quadrupole ion trap-mass spectrometry of the intact glycoproteins. Electrophoresis. 2004;25(13):2026-32.
23. Olds RJ, Lane DA, Boisclair M, Sas G, Bock SC, Thein SL. Antithrombin Budapest 3. An antithrombin variant with reduced heparin affinity resulting from the substitution L99F. FEBS Lett. 1992;300(3):241-6.
24. Lane DA, Olds RJ, Conard J, Boisclair M, Bock SC, Hultin M, et al. Pleiotropic effects of antithrombin strand 1C substitution mutations. J Clin Invest. 1992;90(6):2422-33.
25. Fan B, Crews BC, Turko IV, Choay J, Zettlmeissl G, Gettins P. Heterogeneity of recombinant human antithrombin III expressed in baby hamster kidney cells. Effect of glycosylation differences on heparin binding and structure. J Biol Chem. 1993;268(23):17588-96.
26. Pousset D, Piller V, Bureaud N, Monsigny M, Piller F. Increased a2,6 Sialylation of NGlycans in a Transgenic Mouse Model of Hepatocellular Carcinoma. Cancer Res. 1997;57(19):4249-56.
27. Schachter H. Biosynthetic controls that determine the branching and microheterogeneity of protein-bound oligosaccharides. Biochem Cell Biol. 1986;64(3):163-81.