Histidine-rich Glycoprotein (HRG) Tokushima 2: Novel HRG Deficiency, Molecular and Cellular Characterization

Toshio Shigekiyo; Hidemasa Yoshida; Yasuhiko Kanagawa; Koichi Satoh; Sadao Wakabayashi; Toshio Matsumoto; Takehiko Koide

doi:10.1055/s-0037-1614086

Thrombosis and Haemostasis, Inhaltsverzeichnis

Thromb Haemost 2000; 84(04): 675-679
DOI: 10.1055/s-0037-1614086

Review Article

Schattauer GmbH

Histidine-rich Glycoprotein (HRG) Tokushima 2: Novel HRG Deficiency, Molecular and Cellular Characterization

Toshio Shigekiyo

¹From the First Department of Internal Medicine, School of Medicine, The University of Tokushima, Tokushima

,

Hidemasa Yoshida

³Department of Life Science, Faculty of Science, Himeji Institute of Technology, Hyogo, Japan

,

Yasuhiko Kanagawa

¹From the First Department of Internal Medicine, School of Medicine, The University of Tokushima, Tokushima

,

Koichi Satoh

²Department of Neurological Surgery, School of Medicine, The University of Tokushima, Tokushima

,

Sadao Wakabayashi

³Department of Life Science, Faculty of Science, Himeji Institute of Technology, Hyogo, Japan

,

Toshio Matsumoto

¹From the First Department of Internal Medicine, School of Medicine, The University of Tokushima, Tokushima

,

Takehiko Koide

³Department of Life Science, Faculty of Science, Himeji Institute of Technology, Hyogo, Japan

› Institutsangaben

Abstract

Summary

The proband, a 76-year-old woman, suffered from dural arteriovenous fistula. Her plasma histidine-rich glycoprotein (HRG) level was 50% of the normal level. A low level of plasma HRG was also found in her third daughter. A single nucleotide substitution of T to C was found at nucleotide position 11,438 in exon 6 of the HRG gene from the proband, converting Cys223 to Arg in the second cystatin-like domain. The same mutation was also identified in her third daughter, but not in the other four family members having normal HRG levels or in 50 unrelated healthy Japanese individuals. Expression studies in BHK cells showed that substantial intracellular degradation of the mutant occurred and only about 40% of the recombinant HRG mutant was secreted. These results indicate that congenital HRG deficiency caused by a substitution of Cys223 to Arg is hereditary in this family.

Key words

Congenital histidine-rich glycoprotein deficiency - histidine-rich glycoprotein - thrombosis

Volltext

Referenzen

References
1 Heimburger N, Haupt H, Kranz T, Baudner S. Human serum proteins with a high affinity for carboxymethylcellulose. II. Physicochemical and immunological characterization of a histidine-rich 3.8 S α₂ glycoprotein (CM protein I). Hoppe Seyler’s Z Physiol Chem 1972; 353: 1133-40.
2 Koide T, Foster D, Yoshitake S, Davie EW. Amino acid sequence of human histidine-rich glycoprotein derived from the nucleotide of its cDNA. Biochemistry 1986; 25: 2220-5.
3 Wakabayashi S, Takahashi K, Koide T. Structural characterization of the gene for human histidine-rich glycoprotein. Reinvestigation of the 5’-terminal region of cDNA and search for the liver specific promotor in the gene. J Biochem 1999; 125: 522-30.
4 Hennis BC, Frants RR, Bakker E, Vossen RHAM, van der Poort EW, Blonden LA, Cox S, Kham PM, Spur NK, Kluft C. Evidence for the absence of intron H of the histidine-rich glycoprotein (HRG) gene: Genetic mapping and in situ localization of HRG to chromosome 3q28-29. Genomics 1994; 19: 195-7.
5 Leung LLK, Harpel PC, Nachman RL, Rabellino EM. Histidine-rich glycoprotein is present in human platelets and is released following thrombin stimulation. Blood 1983; 62: 1016-21.
6 Lijnen HR, Collen D. Turnover of histidine-rich glycoprotein during heparin administration in man. Thromb Res 1983; 30: 671-6.
7 Morgan WT. Human serum histidine-rich glycoprotein. I. Interaction with heme, metal ions and organic ligands. Biochim Biophys Acta 1978; 535: 319-33.
8 Lijnen HR, Hoylaerts M, Collen D. Heparin binding properties of human histidine-rich glycoprotein. Mechanism and role in the neutralization of heparin in plasma. J Biol Chem 1983; 258: 3803-8.
9 Leung LLK. Interaction of histidine-rich glycoproterin with fibrinogen and fibrin. J Clin Invest 1986; 77: 1305-11.
10 Halkier T, Anderson H, Vestergaard A, Magnusson S. Bovine histidinerich glycoprotein is a substrate for bovine plasma factor XIIIa. Biochem Biophys Res Commun 1994; 200: 78-82.
11 Lijnen HR, Hoylaerts M, Collen D. Isolation and characterization of a human plasma protein with affinity for the lysine binding sites in plasminogen. Role in the regulation of fibrinolysis and identification as histidine-rich glycoprotein. J Biol Chem 1980; 255: 10214-22.
12 Leung LLK, Nachman RL, Harpel PC. Complex formation of platelet thrombospondin with histidine-rich glycoprotein. J Clin Invest 1984; 73: 5-12.
13 Chang NS, Lew RW, Rummage JK, Mole JE. Regulation of complement functional efficiency by histidine-rich glycoprotein. Blood 1992; 79: 2973-80.
14 Lerch PG, Nydegger UE, Kuyas C, Haeberli A. Histidine-rich glycoprotein binding to activated human platelets. Br J Haematol 1988; 70: 219-24.
15 Saigo K, Shatsky M, Levitt LJ, Leung LLK. Interaction of histidinerich glycoprotein with human T lymphocytes. J Biol Chem 1989; 264: 8249-53.
16 Leung L. Histidine-rich glycoprotein: An abundant plasma protein in search of a function. J Lab Clin Med 1993; 121: 630-1.
17 Zehnder JL, Leung L. Histidine-rich glycoprotein: Is there a role in hemostasis or immune function?. J Lab Clin Med 1995; 125: 682-3.
18 Shigekiyo T, Ohshima T, Oka H, Tomonari A, Azuma H, Saito S. Congenital histidine-rich glycoprotein deficiency. Thromb Haemost 1993; 70: 263-5.
19 Shigekiyo T, Yoshida H, Matsumoto K, Azuma H, Wakabayashi S, Saito S, Fujikawa K, Koide K. HRG Tokushima: Molecular and cellular characterization of histidine-rich glycoprotein (HRG) deficiency. Blood 1998; 91: 128-33.
20 Souto JC, Gari M, Falkon L, Fontcuberta J. A new case of hereditary histidine-rich glycoprotein deficiency with familial thrombophilia. Thromb Haemost 1996; 75: 374-5.
21 Laurell CB. Quantitative estimation of proteins by electrophoresis in agarose gel containing antibodies. Anal Biochem 1966; 15: 45-52.
22 Lijnen HR, Jacobs G, Collen D. Histidine-rich glycoprotein in a normal and a clinical population. Thromb Res 1981; 22: 519-23.
23 Hennis BC, van Boheemen PA, Wakabayashi S, Koide T, Hoffmann JJML, Kievit P, Dooijewaard G, Jansen JG, Kluft C. Identification and genetic analysis of a common molecular variant of histidine-rich glycoprotein with a difference of 2KD in apparent molecular weight. Thromb Haemost 1995; 74: 1491-6.
24 Hennis BC, Boomsma DI, van Boheemen PA, Engesser L, Kievit P, Dooijewaard G, Jansen JG, Kluft C. An amino acid polymorphism in histidinerich glycoprotein (HRG) explains 59% of the variance in plasma HRG levels. Thromb Haemost 1995; 74: 1497-500.
25 Mullan S. Fistulas and vascular malformations of the dura and dural sinuses. In: Brain Surgery. Complication Avoidance and Management, vol 2. Apuzzo MLJ, Todd EM, Wells Jr. THW. eds. New York: Churchill Livingstone; 1993: 1117-41.
26 Lewis AI, Tomsick TA, Tew Jr JM. Carotid-cavernous fistulas and intracavernous aneurysms. In: Neurosurgery, vol II. Wilkins RH, Rengachary SS. eds. New York: McGRAW-HILL; 1996: 2529-39.
27 De Stefano V, Finazzi G, Mannucci PM. Inherited thrombophilia: Pathogenesis, clinical syndromes, and management. Blood 1996; 87: 3531-44.
28 Silverstein RL, Nachman RL, Leung LLK, Harpel PC. Activation of immobilized plasminogen by tissue activator. Multimolecular Complex Formation. J Biol Chem 1985; 260: 10346-52.
29 Borza DB, Morgan WT. Acceleration of plasminogen activation by tissue plasminogen activator on surface-bound histidine-proline-rich glycoprotein. J Biol Chem 1997; 272: 5718-26.
30 Sørensen CB, Krogh-Pedersen H, Petersen TE. Determination of the disulphide bridge arrangement of bovine histidine-rich glycoprotein. FEBS Lett 1993; 328: 285-90.
31 Borza DB, Tatum FM, Morgan WT. Domain structure and conformation of histidine-proline-rich glycoprotein. Biochemistry 1996; 35: 1925-34.
32 Ward CL, Omura S, Kopito RR. Degradation of CFTR by the ubiquitinproteasome pathway. Cell 1995; 83: 121-7.
33 Wiertz EJHJ, Tortorella D, Bogyo M, Yu J, Mothes W, Jones TR, Rapoport TA, Ploegh HL. Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction. Nature 1996; 384: 432-8.
34 Oda K, Ikehara Y, Omura S. Lactacystin, an inhibitor of the proteasome, blocks the degradation of a mutant precursor of glycosylphosphatidylinositol-linked protein in a pre-Golgi. Biochem Biophys Res Commun 1996; 219: 800-5.
35 Werner ED, Brodsky JL, McCracken AA. Proteasome-dependent endoplasmic reticulum-associated protein degradation: an unconventional route to a familiar fate. Pro Natl Acad Sci 1996; 93: 13797-801.
36 Tokunaga F, Shirotani H, Hara K, Kozuki D, Omura S, Koide T. Intracellular degradation of secretion defect-type mutants of antithrombin is inhibited by proteasomal inhibitors. FEBS Lett 1997; 412: 65-9.
37 Tokunaga F, Wakabayashi S, Koide T. Warfarin causes the degradation of protein C precursor in the endoplasmic reticulum. Biochemistry 1995; 34: 1163-70.