Purification and separation of the 20S immunoproteasome from the constitutive proteasome and identification of the subunits by LC–MS

Protein Expression and Purification

Volumn 87, Issue 2, 2013, Pages 100-110

  Dechavanne, Vincent ^a   Vilbois, Francis ^a   Glez, Loic ^a   Antonsson, Bruno ^a  

^a MERCK SERONO S A   (Switzerland)

Author keywords

Constitutive proteasome; Immunoproteasome; Liquid Chromatography Mass Spectrometry (LC MS); Proteasome characterization; Proteasome purification

Indexed keywords

CASPASE; CHYMOTRYPSIN; PROTEASOME; TRYPSIN;

ARTICLE; CHEMICAL PHENOMENA; CHEMISTRY; HUMAN; ISOLATION AND PURIFICATION; LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; METABOLISM; METHODOLOGY; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN SUBUNIT; TUMOR CELL LINE; WESTERN BLOTTING;

BLOTTING, WESTERN; CASPASES; CELL LINE, TUMOR; CHROMATOGRAPHY, LIQUID; CHYMOTRYPSIN; ELECTROPHORESIS, POLYACRYLAMIDE GEL; HUMANS; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; MASS SPECTROMETRY; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN SUBUNITS; TRYPSIN;

MLCS; MLOWN;

EID: 84870294017     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2012.10.009     Document Type: Article

References (32)

1. Coux, O., Tanaka, K., Goldberg, A.L., Structure and functions of the 20S and 26S proteasomes. Annu. Rev. Biochem. 65 (1996), 801–847.
2. Tanaka, K., Yoshimura, T., Kumatori, A., Ichihara, A., Ikai, A., Nishigai, M., Kameyama, K., Takagi, T., Proteasomes (multi-protease complexes) as 20S ring-shaped particles in a variety of eukaryotic cells. J. Biol. Chem. 263 (1988), 16209–16217.
3. Finley, D., Ubiquitin chained and crosslinked. Nat. Cell Biol. 4 (2002), E121–E123.
4. Voges, D., Zwickl, P., Baumeister, W., The 26S proteasome: a molecular machine designed for controlled proteolysis. Annu. Rev. Biochem. 68 (1999), 1015–1018.
5. Demartino, G.N., Gillette, T.G., Proteasomes: machines for all reasons. Nat. Cell Biol. 129 (2007), 659–662.
6. Groll, M., Ditzel, L., Löwe, J., Stock, D., Bochtler, M., Bartunik, H.D., Huber, R., Structure of 20S proteasome from yeast at 2.4 A resolution. Nature 386 (1997), 437–438.
7. Zwickl, P., Kleinz, J., Baumeister, W., Critical elements in proteasome assembly. Nat. Struct. Biol. 1 (1994), 765–770.
8. Osmulski, P.A., Gaczynska, M., Atomic force microscopy reveals two conformations of the 20S proteasome from fission yeast. J. Biol. Chem. 275 (2000), 13171–13174.
9. Kania, M.A., Demartino, G.N., Baumeister, W., Goldberg, A.L., The proteasome subunit, C2, contains an important site for binding of the PA28 (11S) activator. Eur. J. Biochem. 236 (1996), 510–516.
10. Glickman, M.H., Rubin, D.M., Coux, O., Wefes, I., Pfeifer, G., Cjeka, Z., Baumeister, W., Fried, V.A., Finley, D., A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3. Nat. Cell Biol. 94 (1998), 615–623.
11. Braun, B.C., Glickman, M., Kraft, R., Dahlmann, B., Kloetzel, P.M., Finley, D., Schmidt, M., The base of the proteasome regulatory particle exhibits chaperone-like activity. Nat. Cell Biol. 1 (1999), 221–226.
12. Strickland, E., Hakala, K., Thomas, P.J., DeMartino, G.N., Recognition of misfolding proteins by PA700, the regulatory subcomplex of the 26S proteasome. J. Biol. Chem. 275 (2000), 5565–5572.
13. Hirano, Y., Hendil, K.B., Yashiroda, H., Iemura, S., Nagane, R., Hioki, Y., Natsume, T., Tanaka, K., Murata, S., A heterodimeric complex that promotes the assembly of mammalian 20S proteasomes. Nature 437 (2005), 1381–1385.
14. Brown, M.G., Monaco, J.J., Biochemical purification of distinct protesome subsets. Enzyme Protein 47 (1993), 343–353.
15. Akiyama, K., Kagawa, S., Tamura, T., Shimbara, N., Takashina, M., Kristensen, P., Hendil, K.B., Tanaka, K., Ichihara, A., Replacement subunits X and Y by LMP7 and LMP2 induced by interferon-gamma for acquirement of the functional diversity responsible for antigen processing. FEBS Lett. 343 (1994), 85–88.
16. Gaczynska, M., Rock, K.L., Goldberg, A.L., Gamma-interferon and expression of MHC genes regulate peptide hydrolysis by proteasomes. Nature 365 (1993), 264–267.
17. Driscoll, J., Brown, M.G., Finley, D., Monaco, J.J., MHC-linked LMP gene products specifically alter peptidase activities of the proteasome. Nature 365 (1993), 211–212.
18. Monaco, J.J., Nandi, D., The genetics of proteasomes and antigen processing. Annu. Rev. Genet. 29 (1995), 729–754.
19. Nandi, D., Marusina, K., Monaco, J.J., How do endogenous proteins become peptides and reach the endoplasmic reticulum. Curr. Topics Microbiol. Immunol. 232 (1998), 15–47.
20. Shah, S.A., Potter, M.W., Callery, M.P., Ubiquitin proteasome pathway: implications and advances in cancer therapy. Surg. Oncol. 10 (2001), 43–52.
21. Sánchez-Serrano, I., Success in translational research: lessons from the development of bortezomib. Nat. Rev. Drug Discov. 5 (2006), 107–114.
22. Feling, R.H., Buchanan, G.O., Mincer, T.J., Kauffman, C.A., Jensen, P.R., Fenical, W., Salinosporamide A: a highly cytotoxic proteasome inhibitor from a novel microbial source, a marine bacterium of the new genus salinospora. Angew. Chem. Int. Ed. Engl. 42 (2003), 355–357.
23. Bross, P.F., Kane, R., Farrell, A.T., Abraham, S., Benson, K., Brower, M.E., Bradley, S., Gobburu, J.V., Goheer, A., Lee, S.L., Leighton, J., Liang, C.Y., Lostritto, R.T., McGuinn, W.D., Morse, D.E., Rahman, A., Rosario, L.A., Verbois, S.L., Williams, G., Wang, Y.C., Pazdur, R., Approval summary for bortezomib for injection in the treatment of multiple myeloma. Clin. Cancer Res. 10 (2004), 3954–3964.
24. Tenzer, S., Schild, H., Methods assays of proteasome-dependent cleavage products. Mol. Biol. 301 (2005), 97–115.
25. Eleuteri, A.M., Angeletti, M., Lupidi, G., Tacconi, R., Bini, L., Fioretti, E., Isolation and characterization of bovine thymus multicatalytic proteinase complex. Protein Expr. Purif. 18 (2000), 160–168.
26. Groettrup, M., Ruppert, T., Kuehn, L., Seeger, M., Standera, S., Koszinowski, U., Kloetzel, P.M., The interferon-gamma-inducible 11S regulator (PA28) and the LMP2/LMP7 subunits govern the peptide production by the 20S proteasome in vitro. J. Biol. Chem. 270 (1995), 23808–23815.
27. Orlowski, M., Michaud, C., Pituitary multicatalytic proteinase complex. Biochemistry 28 (1989), 9270–9278.
28. Sacchetta, P., Battista, P., Santarone, S., Di Cola, D., Purification of human erythrocyte proteolytic enzyme responsible for degradation of oxidant-damaged hemoglobin. Biochim. Biophys. Acta 1037 (1990), 337–343.
29. Bauer, M.W., Bauer, S.H., Kelly, R.M., Purification and characterization of a proteasome from the hyperthermophilic archaeon Pyrococcus furiosus. Appl. Environ. Microbiol. 63 (1997), 1160–1164.
30. Chapiro, J., Claverol, S., Piette, F., Ma, W., Stroobant, V., Guillaume, B., Gairin, J.E., Morel, S., Burlet-Schiltz, O., Monsarrat, B., Boon, T., Van den Eynde, B.J., Destructive cleavage of antigenic peptides either by the immunoproteasome or by the standard proteasome results in differential antigen presentation. J. Immunol. 176 (2006), 1053–1061.
31. Boes, B., Hengel, H., Ruppert, T., Multhaup, G., Koszinowski, U.H., Kloetzel, P.M., Interferon gamma stimulation modulates the proteolytic activity and cleavage site preference of 20S mouse proteasomes. J. Exp. Med. 179 (1994), 901–909.
32. Wang, X., Chen, C.F., Baker, P.R., Chen, P.L., Kaiser, P., Huang, L., Mass spectrometric characterization of the affinity-purified human 26S proteasome complex. Biochemistry 46 (2007), 3553–3565.