Heterozygosity for the proteasomal Psmc1 ATPase is insufficient to cause neuropathology in mouse brain, but causes cell cycle defects in mouse embryonic fibroblasts

Neuroscience Letters

Volumn 521, Issue 2, 2012, Pages 130-135

  Rezvani, Nooshin ^a   Elkharaz, Jamal ^b   Lawler, Karen ^b   Mee, Maureen ^b   Mayer, R John ^b   Bedford, Lynn ^b  

^a BAYLOR COLLEGE OF MEDICINE   (United States)

^b UNIVERSITY OF NOTTINGHAM   (United Kingdom)

Author keywords

26S proteasome; Cell cycle; Heterozygosity; Lewy body; Neurodegeneration; Ubiquitin proteasome system

Indexed keywords

ADENOSINE TRIPHOSPHATASE; LYSINE; POLYUBIQUITIN; PROTEIN P21; PSMC1 PROTEIN; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; BRAIN; CONTROLLED STUDY; EMBRYO; EMBRYONIC FIBROBLAST; FIBROBLAST; G2 PHASE CELL CYCLE CHECKPOINT; GENOTYPE; HETEROZYGOSITY; IMMUNOHISTOCHEMISTRY; M PHASE CELL CYCLE CHECKPOINT; MOUSE; NEUROPATHOLOGY; NONHUMAN; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN EXPRESSION; WILD TYPE;

ADENOSINE TRIPHOSPHATASES; ANIMALS; BRAIN; CELLS, CULTURED; FIBROBLASTS; G2 PHASE CELL CYCLE CHECKPOINTS; HETEROZYGOTE; M PHASE CELL CYCLE CHECKPOINTS; MICE; MICE, KNOCKOUT; PRIMARY CELL CULTURE; PROTEASOME ENDOPEPTIDASE COMPLEX;

EID: 84863084445     PISSN: 03043940     EISSN: 18727972     Source Type: Journal    
DOI: 10.1016/j.neulet.2012.05.070     Document Type: Article

References (48)

1. Adams J. The development of proteasome inhibitors as anticancer drugs. Cancer Cell 2004, 5:417-421.
2. Ahmed Z., Sheng H., Xu Y.F., Lin W.L., Innes A.E., Gass J., Yu X., Wuertzer C.A., Hou H., Chiba S., Yamanouchi K., Leissring M., Petrucelli L., Nishihara M., Hutton M.L., McGowan E., Dickson D.W., Lewis J. Accelerated lipofuscinosis and ubiquitination in granulin knockout mice suggest a role for progranulin in successful aging. American Journal of Pathology 2010, 177:311-324.
3. Baiz D., Pozzato G., Dapas B., Farra R., Scaggiante B., Grassi M., Uxa L., Giansante C., Zennaro C., Guarnieri G., Grassi G. Bortezomib arrests the proliferation of hepatocellular carcinoma cells HepG2 and JHH6 by differentially affecting E2F1, p21 and p27 levels. Biochimie 2009, 91:373-382.
4. Bedford L., Hay D., Devoy A., Paine S., Powe D.G., Seth R., Gray T., Topham I., Fone K., Rezvani N., Mee M., Soane T., Layfield R., Sheppard P.W., Ebendal T., Usoskin D., Lowe J., Mayer R.J. Depletion of 26S proteasomes in mouse brain neurons causes neurodegeneration and Lewy-like inclusions resembling human pale bodies. Journal of Neuroscience 2008, 28:8189-8198.
5. Blagosklonny M.V., Wu G.S., Omura S., el-Deiry W.S. Proteasome-dependent regulation of p21WAF1/CIP1 expression. Biochemical and Biophysical Research Communications 1996, 227:564-569.
6. Brijbassi S., Amtul Z., Newbigging S., Westaway D., St George-Hyslop P., Rozmahel R.F. Excess of nicastrin in brain results in heterozygosity having no effect on endogenous APP processing and amyloid peptide levels in vivo. Neurobiology of Disease 2007, 25:291-296.
7. Chen L., Thiruchelvam M.J., Madura K., Richfield E.K. Proteasome dysfunction in aged human alpha-synuclein transgenic mice. Neurobiology of Disease 2006, 23:120-126.
8. Ciechanover A. Intracellular protein degradation: from a vague idea thru the lysosome and the ubiquitin-proteasome system and onto human diseases and drug targeting. Experimental Biology and Medical Science (Maywood) 2006, 231:1197-1211.
9. Cook C., Petrucelli L. A critical evaluation of the ubiquitin-proteasome system in Parkinson's disease. Biochimica et Biophysica Acta 2009, 1792:664-675.
10. Dahlmann B. Role of proteasomes in disease. BMC Biochemistry 2007, 8(Suppl. 1):S3.
11. Dawson T.M., Dawson V.L. The role of parkin in familial and sporadic Parkinson's disease. Movement Disorders 2010, 25(Suppl. 1):S32-S39.
12. Dickson D.W., Wertkin A., Kress Y., Ksiezak-Reding H., Yen S.H. Ubiquitin immunoreactive structures in normal human brains. Distribution and developmental aspects. Laboratory Investigation 1990, 63:87-99.
13. Ebrahimi-Fakhari D., Cantuti-Castelvetri I., Fan Z., Rockenstein E., Masliah E., Hyman B.T., McLean P.J., Unni V.K. Distinct roles in vivo for the ubiquitin-proteasome system and the autophagy-lysosomal pathway in the degradation of alpha-synuclein. Journal of Neuroscience 2011, 31:14508-14520.
14. Emmanouilidou E., Stefanis L., Vekrellis K. Cell-produced alpha-synuclein oligomers are targeted to, and impair the 26S proteasome. Neurobiology of Aging 2010, 31:953-968.
15. Escobar M., Velez M., Belalcazar A., Santos E.S., Raez L.E. The role of proteasome inhibition in nonsmall cell lung cancer. Journal of Biomedical and Biotechnology 2011, 2011:806506.
16. Fornai F., Schluter O.M., Lenzi P., Gesi M., Ruffoli R., Ferrucci M., Lazzeri G., Busceti C.L., Pontarelli F., Battaglia G., Pellegrini A., Nicoletti F., Ruggieri S., Paparelli A., Sudhof T.C. Parkinson-like syndrome induced by continuous MPTP infusion: convergent roles of the ubiquitin-proteasome system and alpha-synuclein. Proceedings of the National Academy of Sciences of the United States of America 2005, 102:3413-3418.
17. Geng F., Wenzel S., Tansey W.P. Ubiquitin and proteasomes in transcription. Annual Review of Biochemistry 2012, 81:177-201.
18. Glotzer M., Murray A.W., Kirschner M.W. Cyclin is degraded by the ubiquitin pathway. Nature 1991, 349:132-138.
19. Goldberg A.L. Protein degradation and protection against misfolded or damaged proteins. Nature 2003, 426:895-899.
20. Gray D.A., Tsirigotis M., Woulfe J. Ubiquitin, proteasomes, and the aging brain. Science of Aging Knowledge Environment 2003, 2003:RE6.
21. Gu Z., Steinmetz L.M., Gu X., Scharfe C., Davis R.W., Li W.H. Role of duplicate genes in genetic robustness against null mutations. Nature 2003, 421:63-66.
22. Hamazaki J., Sasaki K., Kawahara H., Hisanaga S., Tanaka K., Murata S. Rpn10-mediated degradation of ubiquitinated proteins is essential for mouse development. Molecular and Cellular Biology 2007, 27:6629-6638.
23. Hanna J., Finley D. A proteasome for all occasions. FEBS Letters 2007, 581:2854-2861.
24. Hartman J.L.t., Garvik B., Hartwell L. Principles for the buffering of genetic variation. Science (New York, NY) 2001, 291:1001-1004.
25. Hutter G., Rieken M., Pastore A., Weigert O., Zimmermann Y., Weinkauf M., Hiddemann W., Dreyling M. The proteasome inhibitor bortezomib targets cell cycle and apoptosis and acts synergistically in a sequence-dependent way with chemotherapeutic agents in mantle cell lymphoma. Annals of Hematology 2012, 91:847-856.
26. Iseki E., Li F., Odawara T., Kosaka K. Hippocampal pathology in diffuse Lewy body disease using ubiquitin immunohistochemistry. Journal of the Neurological Sciences 1997, 149:165-169.
27. Iseki E., Odawara T., Li F., Kosaka K., Nishimura T., Akiyama H., Ikeda K. Age-related ubiquitin-positive granular structures in non-demented subjects and neurodegenerative disorders. Journal of the Neurological Sciences 1996, 142:25-29.
28. Kodadek T. No Splicing, no dicing: non-proteolytic roles of the ubiquitin-proteasome system in transcription. The Journal of biological chemistry 2010, 285:2221-2226.
29. Ling Y.H., Liebes L., Jiang J.D., Holland J.F., Elliott P.J., Adams J., Muggia F.M., Perez-Soler R. Mechanisms of proteasome inhibitor PS-341-induced G(2)-M-phase arrest and apoptosis in human non-small cell lung cancer cell lines. Clinical Cancer Research 2003, 9:1145-1154.
30. Lowe J., Blanchard A., Morrell K., Lennox G., Reynolds L., Billett M., Landon M., Mayer R.J. Ubiquitin is a common factor in intermediate filament inclusion bodies of diverse type in man, including those of Parkinson's disease, Pick's disease, and Alzheimer's disease as well as Rosenthal fibres in cerebellar astrocytomas, cytoplasmic bodies in muscle, and mallory bodies in alcoholic liver disease. The Journal of Pathology 1988, 155:9-15.
31. Maki C.G., Huibregtse J.M., Howley P.M. In vivo ubiquitination and proteasome-mediated degradation of p53(1). Cancer Research 1996, 56:2649-2654.
32. Montagut C., Rovira A., Albanell J. The proteasome: a novel target for anticancer therapy. Clinical and Translational Oncology 2006, 8:313-317.
33. Nakayama K.I., Nakayama K. Ubiquitin ligases: cell-cycle control and cancer. Nature Reviews Cancer 2006, 6:369-381.
34. Paine S., Bedford L., Thorpe J.R., Mayer R.J., Cavey J.R., Bajaj N., Sheppard P.W., Lowe J., Layfield R. Immunoreactivity to Lys63-linked polyubiquitin is a feature of neurodegeneration. Neuroscience Letters 2009, 460:205-208.
35. Riederer B.M., Leuba G., Vernay A., Riederer I.M. The role of the ubiquitin proteasome system in Alzheimer's disease. Experimental Biology and Medical Science (Maywood) 2011, 236:268-276.
36. Rosenzweig R., Osmulski P.A., Gaczynska M., Glickman M.H. The central unit within the 19S regulatory particle of the proteasome. Nature Structural and Molecular Biology 2008, 15:573-580.
37. Ross C.A., Pickart C.M. The ubiquitin-proteasome pathway in Parkinson's disease and other neurodegenerative diseases. Trends in Cell Biology 2004, 14:703-711.
38. Rubin D.M., Glickman M.H., Larsen C.N., Dhruvakumar S., Finley D. Active site mutants in the six regulatory particle ATPases reveal multiple roles for ATP in the proteasome. The EMBO Journal 1998, 17:4909-4919.
39. Sakao Y., Kawai T., Takeuchi O., Copeland N.G., Gilbert D.J., Jenkins N.A., Takeda K., Akira S. Mouse proteasomal ATPases Psmc3 and Psmc4: genomic organization and gene targeting. Genomics 2000, 67:1-7.
40. Shimada A., Keino H., Kawamura N., Chiba Y., Hosokawa M. Limbic structures are prone to age-related impairments in proteasome activity and neuronal ubiquitinated inclusions in SAMP10 mouse: a model of cerebral degeneration. Neuropathology and Applied Neurobiology 2008, 34:33-51.
41. Sterz J., Jakob C., Kuckelkorn U., Heider U., Mieth M., Kleeberg L., Kaiser M., Kloetzel P.M., Sezer O., von Metzler I. BSc2118 is a novel proteasome inhibitor with activity against multiple myeloma. European Journal of Haematology 2010, 85:99-107.
42. Tai H.C., Schuman E.M. Ubiquitin, the proteasome and protein degradation in neuronal function and dysfunction. Nature Reviews Neuroscience 2008, 9:826-838.
43. Tseng B.P., Green K.N., Chan J.L., Blurton-Jones M., LaFerla F.M. Abeta inhibits the proteasome and enhances amyloid and tau accumulation. Neurobiology of Aging 2008, 29:1607-1618.
44. Veitia R.A. Exploring the etiology of haploinsufficiency. Bioessays 2002, 24:175-184.
45. Vernace V.A., Schmidt-Glenewinkel T., Figueiredo-Pereira M.E. Aging and regulated protein degradation: who has the UPPer hand?. Aging Cell 2007, 6:599-606.
46. Wills J., Credle J., Oaks A.W., Duka V., Lee J.H., Jones J., Sidhu A. Paraquat, but not maneb, induces synucleinopathy and tauopathy in striata of mice through inhibition of proteasomal and autophagic pathways. PLoS One 2012, 7:e30745.
47. Zeng B.Y., Medhurst A.D., Jackson M., Rose S., Jenner P. Proteasomal activity in brain differs between species and brain regions and changes with age. Mechanisms of Ageing and Development 2005, 126:760-766.
48. Zhang N.Y., Tang Z., Liu C.W. Alpha-synuclein protofibrils inhibit 26 S proteasome-mediated protein degradation: understanding the cytotoxicity of protein protofibrils in neurodegenerative disease pathogenesis. The Journal of Biological Chemistry 2008, 283:20288-20298.