LMP2-Specific Inhibitors: Chemical Genetic Tools for Proteasome Biology

Chemistry and Biology

Volumn 14, Issue 4, 2007, Pages 419-430

  Bargagna Mohan, Paola ^b   Mohan, Royce ^b  

^a Abby)   (United States)

^b UNIVERSITY OF KENTUCKY   (United States)

Author keywords

CHEMBIOL; MOLIMMUNO

Indexed keywords

CHYMOTRYPSIN; CYSTEINE PROTEINASE; DIHYDROEPONEMYCIN; DRUG DERIVATIVE; LMP 2 PROTEIN; LMP-2 PROTEIN; PROTEASOME; SERINE; UNCLASSIFIED DRUG;

ADENOCARCINOMA; ANIMAL; ARTICLE; CHEMISTRY; DRUG ANTAGONISM; ENZYME ACTIVE SITE; HUMAN; MALE; METABOLISM; MOLECULAR PROBE; MOUSE; NEOVASCULARIZATION (PATHOLOGY); PROSTATE TUMOR; TUMOR CELL LINE;

ADENOCARCINOMA; ANIMALS; CATALYTIC DOMAIN; CELL LINE, TUMOR; CHYMOTRYPSIN; CYSTEINE ENDOPEPTIDASES; HUMANS; MALE; MICE; MOLECULAR PROBES; NEOVASCULARIZATION, PATHOLOGIC; PROSTATIC NEOPLASMS; PROTEASOME ENDOPEPTIDASE COMPLEX; SERINE;

EID: 34247190754     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2007.03.008     Document Type: Article

References (51)

1. Deshaies R.J. SCF and Cullin/Ring H2-based ubiquitin ligases. Annu. Rev. Cell Dev. Biol. 15 (1999) 435-467
2. Karin M., and Ben-Neriah Y. Phosphorylation meets ubiquitination: the control of NF-[κ]B activity. Annu. Rev. Immunol. 18 (2000) 621-663
3. Ciechanover A., and Schwartz A.L. Ubiquitin-mediated degradation of cellular proteins in health and disease. Hepatology 35 (2002) 3-6
4. Myung J., Kim K.B., Lindsten K., Dantuma N.P., and Crews C.M. Lack of proteasome active site allostery as revealed by subunit-specific inhibitors. Mol. Cell 7 (2001) 411-420
5. Nazif T., and Bogyo M. Global analysis of proteasomal substrate specificity using positional-scanning libraries of covalent inhibitors. Proc. Natl. Acad. Sci. USA 98 (2001) 2967-2972
6. Loidl G., Groll M., Musiol H.J., Ditzel L., Huber R., and Moroder L. Bifunctional inhibitors of the trypsin-like activity of eukaryotic proteasomes. Chem. Biol. 6 (1999) 197-204
7. Loidl G., Groll M., Musiol H.J., Huber R., and Moroder L. Bivalency as a principle for proteasome inhibition. Proc. Natl. Acad. Sci. USA 96 (1999) 5418-5422
8. Loidl G., Musiol H.J., Groll M., Huber R., and Moroder L. Synthesis of bivalent inhibitors of eucaryotic proteasomes. J. Pept. Sci. 6 (2000) 36-46
9. Myung J., Kim K.B., and Crews C.M. The ubiquitin-proteasome pathway and proteasome inhibitors. Med. Res. Rev. 21 (2001) 245-273
10. Kisselev A.F., Callard A., and Goldberg A.L. Importance of the different proteolytic sites of the proteasome and the efficacy of inhibitors varies with the protein substrate. J. Biol. Chem. 281 (2006) 8582-8590
11. Crawford L.J., Walker B., Ovaa H., Chauhan D., Anderson K.C., Morris T.C., and Irvine A.E. Comparative selectivity and specificity of the proteasome inhibitors BzLLLCOCHO, PS-341, and MG-132. Cancer Res. 66 (2006) 6379-6386
12. Montagut C., Rovira A., and Albanell J. The proteasome: a novel target for anticancer therapy. Clin. Transl. Oncol. 8 (2006) 313-317
13. Chim C.S., Ooi G.C., Loong F., Au A.W., and Lie A.K. Side effects and good effects from new chemotherapeutic agents. Case 3. Bortezomib in primary refractory plasmacytoma. J. Clin. Oncol. 23 (2005) 2426-2428
14. Kloetzel P.M. Antigen processing by the proteasome. Nat. Rev. Mol. Cell Biol. 2 (2001) 179-187
15. Rock K.L., and Goldberg A.L. Degradation of cell proteins and the generation of MHC class I-presented peptides. Annu. Rev. Immunol. 17 (1999) 739-779
16. Fruh K., Gossen M., Wang K., Bujard H., Peterson P.A., and Yang Y. Displacement of housekeeping proteasome subunits by MHC-encoded LMPs: a newly discovered mechanism for modulating the multicatalytic proteinase complex. EMBO J. 13 (1994) 3236-3244
17. Strehl B., Seifert U., Kruger E., Heink S., Kuckelkorn U., and Kloetzel P.M. Interferon-γ, the functional plasticity of the ubiquitin-proteasome system, and MHC class I antigen processing. Immunol. Rev. 207 (2005) 19-30
18. Orlowski R.Z. The ubiquitin proteasome pathway from bench to bedside. Hematology (Am. Soc. Hematol. Educ. Program) (2005) 220-225
19. Voorhees P.M., and Orlowski R.Z. The proteasome and proteasome inhibitors in cancer therapy. Annu. Rev. Pharmacol. Toxicol. 46 (2006) 189-213
20. Casp C.B., She J.X., and McCormack W.T. Genes of the LMP/TAP cluster are associated with the human autoimmune disease vitiligo. Genes Immun. 4 (2003) 492-499
21. Diaz-Hernandez M., Hernandez F., Martin-Aparicio E., Gomez-Ramos P., Moran M.A., Castano J.G., Ferrer I., Avila J., and Lucas J.J. Neuronal induction of the immunoproteasome in Huntington's disease. J. Neurosci. 23 (2003) 11653-11661
22. Piccinini M., Mostert M., Croce S., Baldovino S., Papotti M., and Rinaudo M.T. Interferon-γ-inducible subunits are incorporated in human brain 20S proteasome. J. Neuroimmunol. 135 (2003) 135-140
23. Noda C., Tanahashi N., Shimbara N., Hendil K.B., and Tanaka K. Tissue distribution of constitutive proteasomes, immunoproteasomes, and PA28 in rats. Biochem. Biophys. Res. Commun. 277 (2000) 348-354
24. Mishto M., Bellavista E., Santoro A., Stolzing A., Ligorio C., Nacmias B., Spazzafumo L., Chiappelli M., Licastro F., Sorbi S., et al. Immunoproteasome and LMP2 polymorphism in aged and Alzheimer's disease brains. Neurobiol. Aging 27 (2006) 54-66
25. Zhang H., Sun L., Liang J., Yu W., Zhang Y., Wang Y., Chen Y., Li R., Sun X., and Shang Y. The catalytic subunit of the proteasome is engaged in the entire process of estrogen receptor-regulated transcription. EMBO J. 25 (2006) 4223-4233
26. Singhal S., and Mehta J. Novel therapies in multiple myeloma. Int. J. Hematol. 77 (2003) 226-231
27. Hideshima T., Chauhan D., Podar K., Schlossman R.L., Richardson P., and Anderson K.C. Novel therapies targeting the myeloma cell and its bone marrow microenvironment. Semin. Oncol. 28 (2001) 607-612
28. Hideshima T., Chauhan D., Hayashi T., Akiyama M., Mitsiades N., Mitsiades C., Podar K., Munshi N.C., Richardson P.G., and Anderson K.C. Proteasome inhibitor PS-341 abrogates IL-6 triggered signaling cascades via caspase-dependent downregulation of gp130 in multiple myeloma. Oncogene 22 (2003) 8386-8393
29. Hideshima T., and Anderson K.C. Molecular mechanisms of novel therapeutic approaches for multiple myeloma. Nat. Rev. Cancer 2 (2002) 927-937
30. Altun M., Galardy P.J., Shringarpure R., Hideshima T., LeBlanc R., Anderson K.C., Ploegh H.L., and Kessler B.M. Effects of PS-341 on the activity and composition of proteasomes in multiple myeloma cells. Cancer Res. 65 (2005) 7896-7901
31. Meng L., Kwok B.H., Sin N., and Crews C.M. Eponemycin exerts its antitumor effect through the inhibition of proteasome function. Cancer Res. 59 (1999) 2798-2801
32. Meng L., Mohan R., Kwok B.H., Elofsson M., Sin N., and Crews C.M. Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo antiinflammatory activity. Proc. Natl. Acad. Sci. USA 96 (1999) 10403-10408
33. Kim K.B., Myung J., Sin N., and Crews C.M. Proteasome inhibition by the natural products epoxomicin and dihydroeponemycin: insights into specificity and potency. Bioorg. Med. Chem. Lett. 9 (1999) 3335-3340
34. Kuttler C., Nussbaum A.K., Dick T.P., Rammensee H.G., Schild H., and Hadeler K.P. An algorithm for the prediction of proteasomal cleavages. J. Mol. Biol. 298 (2000) 417-429
35. Ho A., Cyrus K., and Kim K.B. Towards immunoproteasome-specific inhibitors: an improved synthesis of dihydroeponemycin. Eur. J. Org. Chem. 2005 (2005) 4829-4834
36. Groll M., Kim K.B., Kairies N., Huber R., and Crews C.M. Crystal structure of epoxomicin: 20S proteasome reveals a molecular basis for selectivity of a′,b′-epoxyketone proteasome inhibitors. J. Am. Chem. Soc. 122 (2000) 1237-1238
37. Lowe J., Stock D., Jap B., Zwickl P., Baumeister W., and Huber R. Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 Å resolution. Science 268 (1995) 533-539
38. Groll M., Ditzel L., Lowe J., Stock D., Bochtler M., Bartunik H.D., and Huber R. Structure of 20S proteasome from yeast at 2.4 Å resolution. Nature 386 (1997) 463-471
39. Eleuteri A.M., Kohanski R.A., Cardozo C., and Orlowski M. Bovine spleen multicatalytic proteinase complex (proteasome). Replacement of X, Y, and Z subunits by LMP7, LMP2, and MECL1 and changes in properties and specificity. J. Biol. Chem. 272 (1997) 11824-11831
40. Cardozo C., and Kohanski R.A. Altered properties of the branched chain amino acid-preferring activity contribute to increased cleavages after branched chain residues by the "immunoproteasome". J. Biol. Chem. 273 (1998) 16764-16770
41. Craiu A., Gaczynska M., Akopian T., Gramm C.F., Fenteany G., Goldberg A.L., and Rock K.L. Lactacystin and clasto-lactacystin β-lactone modify multiple proteasome β-subunits and inhibit intracellular protein degradation and major histocompatibility complex class I antigen presentation. J. Biol. Chem. 272 (1997) 13437-13445
42. Reidlinger J., Pike A.M., Savory P.J., Murray R.Z., and Rivett A.J. Catalytic properties of 26 S and 20 S proteasomes and radiolabeling of MB1, LMP7, and C7 subunits associated with trypsin-like and chymotrypsin-like activities. J. Biol. Chem. 272 (1997) 24899-24905
43. Cardozo C., Eleuteri A.M., and Orlowski M. Differences in catalytic activities and subunit pattern of multicatalytic proteinase complexes (proteasomes) isolated from bovine pituitary, lung, and liver. Changes in LMP7 and the component necessary for expression of the chymotrypsin-like activity. J. Biol. Chem. 270 (1995) 22645-22651
44. Salzmann U., Kral S., Braun B., Standera S., Schmidt M., Kloetzel P.M., and Sijts A. Mutational analysis of subunit i β2 (MECL-1) demonstrates conservation of cleavage specificity between yeast and mammalian proteasomes. FEBS Lett. 454 (1999) 11-15
45. Basler M., Moebius J., Elenich L., Groettrup M., and Monaco J.J. An altered T cell repertoire in MECL-1-deficient mice. J. Immunol. 176 (2006) 6665-6672
46. Mohan R., Hammers H.J., Bargagna-Mohan P., Zhan X.H., Herbstritt C.J., Ruiz A., Zhang L., Hanson A.D., Conner B.P., Rougas J., and Pribluda V.S. Withaferin A is a potent inhibitor of angiogenesis. Angiogenesis 7 (2004) 115-122
47. Korff T., and Augustin H.G. Integration of endothelial cells in multicellular spheroids prevents apoptosis and induces differentiation. J. Cell Biol. 143 (1998) 1341-1352
48. Bargagna-Mohan P., Ravindranath P.P., and Mohan R. Small molecule anti-angiogenic probes of the ubiquitin proteasome pathway: potential application to choroidal neovascularization. Invest. Ophthalmol. Vis. Sci. 47 (2006) 4138-4145
49. Griffin T.A., Nandi D., Cruz M., Fehling H.J., Kaer L.V., Monaco J.J., and Colbert R.A. Immunoproteasome assembly: cooperative incorporation of interferon γ (IFN-γ)-inducible subunits. J. Exp. Med. 187 (1998) 97-104
50. Kingsbury D.J., Griffin T.A., and Colbert R.A. Novel propeptide function in 20 S proteasome assembly influences beta subunit composition. J. Biol. Chem. 275 (2000) 24156-24162
51. De M., Jayarapu K., Elenich L., Monaco J.J., Colbert R.A., and Griffin T.A. Beta 2 subunit propeptides influence cooperative proteasome assembly. J. Biol. Chem. 278 (2003) 6153-6159