Proteasome degradation of protein C and plasmin inhibitor mutants

Thrombosis and Haemostasis

Volumn 100, Issue 3, 2008, Pages 405-412

  Nishio, Miwako ^a   Koyama, Takatoshi ^a   Nakahara, Masako ^b   Egawa, Nagisa ^a   Hirosawa, Shinsaku ^a  

^a TOKYO MEDICAL AND DENTAL UNIVERSITY   (Japan)

^b KITASATO UNIVERSITY   (Japan)

Author keywords

Endoplasmic reticulum associated degradation; N linked glycosylation; Plasmin inhibitor; Proteasome inhibitor; Protein C

Indexed keywords

BORTEZOMIB; CALRETICULIN; DOXYCYCLINE; GLUCOSE REGULATED PROTEIN 78; GLUCOSE REGULATED PROTEIN 94; LACTACYSTIN; MANNOSE; PLASMIN INHIBITOR; PROTEASOME; PROTEIN C; TUNICAMYCIN;

ANIMAL CELL; ARTICLE; AUTOPHAGY; CONTROLLED STUDY; ENDOPLASMIC RETICULUM; GENE MUTATION; GENE OVEREXPRESSION; GLYCOSYLATION; IMMUNOBLOTTING; IMMUNOPRECIPITATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN C DEFICIENCY; PROTEIN DEGRADATION; PROTEIN FOLDING; UBIQUITINATION;

ANIMALS; CALRETICULIN; CHO CELLS; CRICETINAE; CRICETULUS; ENDOPLASMIC RETICULUM; HEAT-SHOCK PROTEINS; HSP70 HEAT-SHOCK PROTEINS; HUMANS; JURKAT CELLS; MEMBRANE PROTEINS; MICE; MOLECULAR CHAPERONES; MUTATION; PLASMIN; PROTEASE INHIBITORS; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN C;

EID: 51349129642     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1160/TH08-04-0252     Document Type: Article

References (37)

1. Dahlbäck B. Progress in the understanding of the protein C anticoagulant pathway. Int J Hematol 2004; 79: 109-116.
2. Reitsma PH. Protein C deficiency: from gene defects to disease. Thromb Haemost 1997; 78: 344-350.
3. Rossi E, Za T, Ciminello A, Leone G, et al. The risk of symptomatic pulmonary embolism due to proximal deep venous thrombosis differs in patients with different types of inherited thrombophilia. Thromb Haemost 2008; 99: 1030-1034.
4. 2- plasmin inhibitor from human plasma. A novel proteinase inhibitor which inhibits activator-induced clot lysis. J Biol Chem 1976; 251: 5956-5965.
5. 2-antiplasmin. Blood 1982; 59: 1246-1251.
6. El-Maarri O, Singer H, Klein C, et al. Lack of F8 mRNA: a novel mechanism leading to hemophilia A. Blood 2006; 107: 2759-2765.
7. Kornfeld R, Kornfeld S. Assembly of asparagine-linked oligosaccharides. Annu Rev Biochem 1985; 54: 631-664.
8. 2 in calf thyroid cells. A possible recognition signal in the processing of glycoproteins. J Biol Chem 1983; 258: 8260-8265.
9. Knittler MR, Dirks S, Haas IG. Molecular chaperones involved in protein degradation in the endoplasmic reticulum: quantitative interaction of the heat shock cognate protein BiP with partially folded immunoglobulin light chains that are degraded in the endoplasmic reticulum. Proc Natl Acad Sci USA 1995; 92: 1764-1768.
10. 1- antitrypsin by human ER mannosidase I. J Biol Chem 2003; 278: 26287-26294.
11. Mizushima N, Levine B, Cuervo AM, Klionsky DJ. Autophagy fights disease through cellular self-digestion. Nature 2008; 451: 1069-1075.
12. Webb JL, Ravikumar B, Atkins J, et al. α-Synuclein is degraded by both autophagy and the proteasome. J Biol Chem 2003; 278: 25009-25013.
13. 1-antitrypsin Z are propagated in the absence of autophagic activity. J Biol Chem 2006; 281: 4467-4476.
14. Nakahara M, Koyama T, Nakazawa F, et al. Gradually glycosylated protein C mutants (Arg178Gln and Cys331Arg) are degraded by proteasome after mannose trimming. Thromb Haemost 2004; 92: 1284-1290.
15. 2-plasmin inhibitor for degradation by the proteasome. J Biol Chem 2000; 275: 4981-4987.
16. Sugahara Y, Miura O, Hirosawa S, et al. Compound heterozygous protein C deficiency caused by two mutations, Arg-178 to Gln and Cys-331 to Arg, leading to impaired secretion of mutant protein C. Thromb Haemost 1994; 72: 814-818.
17. Reitsma PH, Bernardi F, Doig RG, et al. Protein C deficiency: a database of mutations, 1995 update. On behalf of the Subcommittee on Plasma Coagulation Inhibitors of the Scientific and Standardization Committee of the ISTH. Thromb Haemost 1995; 73: 876-889.
18. Yoshinaga H, Nakahara M, Koyama T, et al. A single thymine nucleotide deletion responsible for congenital deficiency of plasmin inhibitor. Thromb Haemost 2002; 88: 144-148.
19. 2-PI-Okinawa). Deletion of Glu137 by a trinucleotide deletion blocks intracellular transport. J Biol Chem 1989; 264: 18213-18219.
20. Miyake S, Sellers WR, Safran M, et al. Cells degrade a novel inhibitor of differentiation with E1A-like properties upon exiting the cell cycle. Mol Cell Biol 2000; 20: 8889-8902.
21. Hosokawa N, Hara Y, Mizushima N. Generation of cell lines with tetracycline-regulated autophagy and a role for autophagy in controlling cell size. FEBS Lett 2007; 581: 2623-2629.
22. Chen WJ, Lin JK. Induction of G1 arrest and apoptosis in human jurkat T cells by pentagalloylglucose through inhibiting proteasome activity and elevating p27Kip1, p21Cip1/WAF1, and Bax proteins. J Biol Chem 2004; 279: 13496-13505.
23. de Virgilio M, Kitzmuller C, Schwaiger E, et al. Degradation of a short-lived glycoprotein from the lumen of the endoplasmic reticulum: the role of N-linked glycans and the unfolded protein response. Mol Biol Cell 1999; 10: 4059-4073.
24. el Battari A, Forget P, Fouchier F, et al. Effect of inhibiting N-glycosylation or oligosaccharide processing on vasoactive intestinal peptide receptor binding activity and structure. Biochem J 1991; 278: 527-533.
25. Travers KJ, Patil CK, Wodicka L, et al. Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation. Cell 2000; 101: 249-258.
26. Mor-Cohen R, Rosenberg N, Peretz H, et al. Disulfide bond disruption by a β3-Cys549Arg mutation in six Jordanian families with Glanzmann thrombasthenia causes diminished production of constitutively active αIIbβ3. Thromb Haemost 2007; 98: 1257-1265.
27. Williams DB. Calnexin leads glycoproteins into the fold. Glycoconj J 1995; 12: iii-iv.
28. Hammond C, Braakman I, Helenius A. Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control. Proc Natl Acad Sci USA 1994; 91: 913-917.
29. Hochrainer K, Lipp J. Ubiquitylation within signaling pathways in- and outside of inflammation. Thromb Haemost 2007; 97: 370-377.
30. Newman RM, Mobascher A, Mangold U, et al. Antizyme targets cyclin D1 for degradation. A novel mechanism for cell growth repression. J Biol Chem 2004; 279: 41504-41511.
31. Grune T, Merker K, Sandig G, et al. Selective degradation of oxidatively modified protein substrates by the proteasome. Biochem Biophys Res Commun 2003; 305: 709-718.
32. Rajkumar SV, Richardson PG, Hideshima T, et al. Proteasome inhibition as a novel therapeutic target in human cancer. J Clin Oncol 2005; 23: 630-639.
33. Zhang L, Zhang ZG, Liu X, et al. Treatment of embolic stroke in rats with bortezomib and recombinant human tissue plasminogen activator. Thromb Haemost 2006; 95: 166-173.
34. Hara T, Nakamura K, Matsui M, et al. Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice. Nature 2006; 441: 885-889.
35. Kruse KB, Dear A, Kaltenbrun ER, et al. Mutant fibrinogen cleared from the endoplasmic reticulum via endoplasmic reticulum-associated protein degradation and autophagy: an explanation for liver disease. Am J Pathol 2006; 168: 1299-1308; quiz 1404-1405.
36. Fujita E, Kouroku Y, Isoai A, et al. Two endoplasmic reticulum-associated degradation (ERAD) systems for the novel variant of the mutant dysferlin: ubiquitin/proteasome ERAD(I) and autophagy/lysosome ERAD(II). Hum Mol Genet 2007; 16: 618-629.
37. Ding WX, Yin XM. Sorting, recognition and activation of the misfolded protein degradation pathways through macroautophagy and the proteasome. Autophagy 2008; 4: 1-10.