Cu, Zn-superoxide dismutase 1 (SOD1) is a novel target of Puromycin-sensitive aminopeptidase (PSA/NPEPPS): PSA/NPEPPS is a possible modifier of amyotrophic lateral sclerosis

Molecular Neurodegeneration

Volumn 6, Issue 1, 2011, Pages

  Ren, Guijie ^a,b   Ma, Zhongcai ^a   Hui, Maria ^c   Kudo, Lili C ^d   Hui, Koon Sea ^c   Karsten, Stanislav L ^a,d,e  

^a UCLA MEDICAL CENTER   (United States)

^b SHANDONG UNIVERSITY   (China)

^c NEW YORK UNIVERSITY SCHOOL OF MEDICINE   (United States)

^d NeuroInDx Inc   (United States)

^e UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

COPPER ZINC SUPEROXIDE DISMUTASE; PEPTIDASE; PUROMYCIN SENSITIVE AMINOPEPTIDASE; TAU PROTEIN; UNCLASSIFIED DRUG;

AMYOTROPHIC LATERAL SCLEROSIS; ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; AUTOPHAGY; CELL LINE; CONTROLLED STUDY; ENZYME METABOLISM; ENZYME REGULATION; ERYTHROCYTE; HUMAN; HUMAN CELL; IMMUNOHISTOCHEMISTRY; IN VITRO STUDY; MALE; MOTONEURON; NERVE DEGENERATION; NEUROBLASTOMA; NEUROPROTECTION; NONHUMAN; PROTEIN DEGRADATION; PROTEIN EXPRESSION; RAT; WESTERN BLOTTING;

MUS MUSCULUS;

EID: 79955673525     PISSN: None     EISSN: 17501326     Source Type: Journal    
DOI: 10.1186/1750-1326-6-29     Document Type: Article

References (38)

1. Unraveling the mechanisms involved in motor neuron degeneration in ALS. LI Bruijn TM Miller DW Cleveland, Annu Rev Neurosci 2004 27 723 749 10.1146/annurev.neuro.27.070203.144244 15217349 (Pubitemid 39050419)
2. Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. DR Rosen T Siddique D Patterson DA Figlewicz P Sapp A Hentati D Donaldson J Goto JP O'Regan HX Deng,, et al. Nature 1993 362 59 62 10.1038/362059a0 8446170 (Pubitemid 23087289)
3. Current hypotheses for the underlying biology of amyotrophic lateral sclerosis. JD Rothstein, Ann Neurol 2009 65 Suppl 1 3 S9 19191304
4. Genetic studies of amyotrophic lateral sclerosis: controversies and perspectives. A Beleza-Meireles A Al-Chalabi, Amyotroph Lateral Scler 2009 10 1 14 10.1080/17482960802585469 19110986
5. Recent advances in the genetics of amyotrophic lateral sclerosis. PN Valdmanis H Daoud PA Dion GA Rouleau, Curr Neurol Neurosci Rep 2009 9 198 205 10.1007/s11910-009-0030-9 19348708
6. Aggregation of copper-zinc superoxide dismutase in familial and sporadic ALS. M Chattopadhyay JS Valentine, Antioxid Redox Signal 2009 11 1603 1614 10.1089/ars.2009.2536 19271992
7. How do ALS-associated mutations in superoxide dismutase 1 promote aggregation of the protein? BF Shaw JS Valentine, Trends Biochem Sci 2007 32 78 85 10.1016/j.tibs.2006.12.005 17208444 (Pubitemid 46199198)
8. Intense superoxide dismutase-1 immunoreactivity in intracytoplasmic hyaline inclusions of familial amyotrophic lateral sclerosis with posterior column involvement. N Shibata A Hirano M Kobayashi T Siddique HX Deng WY Hung T Kato K Asayama, J Neuropathol Exp Neurol 1996 55 481 490 10.1097/00005072- 199604000-00011 8786408 (Pubitemid 26112102)
9. High molecular weight complexes of mutant superoxide dismutase 1: age-dependent and tissue-specific accumulation. J Wang G Xu DR Borchelt, Neurobiol Dis 2002 9 139 148 10.1006/nbdi.2001.0471 11895367 (Pubitemid 34261210)
10. New consensus research on neuropathological aspects of familial amyotrophic lateral sclerosis with superoxide dismutase 1 (SOD1) gene mutations: inclusions containing SOD1 in neurons and astrocytes. S Kato M Takikawa K Nakashima A Hirano DW Cleveland H Kusaka N Shibata M Kato I Nakano E Ohama, Amyotroph Lateral Scler Other Motor Neuron Disord 2000 1 163 184 10.1080/14660820050515160 11464950
11. Wild-type and mutant SOD1 share an aberrant conformation and a common pathogenic pathway in ALS. DA Bosco G Morfini NM Karabacak Y Song F Gros-Louis P Pasinelli H Goolsby BA Fontaine N Lemay D McKenna-Yasek,, et al. Nat Neurosci 2010 13 1396 1403 10.1038/nn.2660 20953194
12. Novel antibodies reveal inclusions containing non-native SOD1 in sporadic ALS patients. K Forsberg PA Jonsson PM Andersen D Bergemalm KS Graffmo M Hultdin J Jacobsson R Rosquist SL Marklund T Brannstrom, PLoS One 2010 5 11552 10.1371/journal.pone.0011552 20644736
13. Protein aggregation diseases: pathogenicity and therapeutic perspectives. A Aguzzi T O'Connor, Nat Rev Drug Discov 2010 9 237 248 10.1038/nrd3050 20190788
14. Tau-mediated neurodegeneration in Alzheimer's disease and related disorders. C Ballatore VM Lee JQ Trojanowski, Nat Rev Neurosci 2007 8 663 672 17684513 (Pubitemid 47283144)
15. Mechanisms of tau-induced neurodegeneration. K Iqbal F Liu CX Gong C Alonso Adel I Grundke-Iqbal, Acta Neuropathol 2009 118 53 69 10.1007/s00401-009-0486-3 19184068
16. Tau pathophysiology in neurodegeneration: a tangled issue. TL Spires-Jones WH Stoothoff A de Calignon PB Jones BT Hyman, Trends Neurosci 2009 32 150 159 10.1016/j.tins.2008.11.007 19162340
17. Common molecular signature in SOD1 for both sporadic and familial amyotrophic lateral sclerosis. A Gruzman WL Wood E Alpert MD Prasad RG Miller JD Rothstein R Bowser R Hamilton TD Wood DW Cleveland,, et al. Proc Natl Acad Sci USA 2007 104 12524 12529 10.1073/pnas.0705044104 17636119 (Pubitemid 47206171)
18. Sporadic amyotrophic lateral sclerosis with dementia and Cu/Zn superoxide dismutase-positive Lewy body-like inclusions. S Matsumoto H Kusaka H Ito N Shibata T Asayama T Imai, Clin Neuropathol 1996 15 41 46 8998856 (Pubitemid 26022736)
19. Cu/Zn superoxide dismutase-like immunoreactivity in Lewy body-like inclusions of sporadic amyotrophic lateral sclerosis. N Shibata A Hirano M Kobayashi S Sasaki T Kato S Matsumoto Z Shiozawa T Komori A Ikemoto T Umahara,, et al. Neurosci Lett 1994 179 149 152 10.1016/0304-3940(94)90956-3 7845611 (Pubitemid 24298580)
20. Oxidized/misfolded superoxide dismutase-1: the cause of all amyotrophic lateral sclerosis? E Kabashi PN Valdmanis P Dion GA Rouleau, Ann Neurol 2007 62 553 559 10.1002/ana.21319 18074357
21. Allele-specific RNAi selectively silences mutant SOD1 and achieves significant therapeutic benefit in vivo. X Xia H Zhou Y Huang Z Xu, Neurobiol Dis 2006 23 578 586 10.1016/j.nbd.2006.04.019 16857362 (Pubitemid 44234094)
22. A genomic screen for modifiers of tauopathy identifies puromycin-sensitive aminopeptidase as an inhibitor of tau-induced neurodegeneration. SL Karsten TK Sang LT Gehman S Chatterjee J Liu GM Lawless S Sengupta RW Berry J Pomakian HS Oh,, et al. Neuron 2006 51 549 560 10.1016/j.neuron.2006.07.019 16950154 (Pubitemid 44314079)
23. Degradation of tau protein by puromycin-sensitive aminopeptidase in vitro. S Sengupta PM Horowitz SL Karsten GR Jackson DH Geschwind Y Fu RW Berry LI Binder, Biochemistry 2006 45 15111 15119 10.1021/bi061830d 17154549 (Pubitemid 44937024)
24. Involvement of puromycin-sensitive aminopeptidase in proteolysis of tau protein in cultured cells, and attenuated proteolysis of frontotemporal dementia and parkinsonism linked to chromosome 17 (FTDP-17) mutant tau. K Yanagi T Tanaka K Kato G Sadik T Morihara T Kudo M Takeda, Psychogeriatrics 2009 9 157 166 10.1111/j.1479-8301.2010.00307.x 20377816
25. Puromycin-sensitive aminopeptidase is the major peptidase responsible for digesting polyglutamine sequences released by proteasomes during protein degradation. N Bhutani P Venkatraman AL Goldberg, EMBO J 2007 6 1385 1396 (Pubitemid 46398712)
26. Puromycin-sensitive aminopeptidase protects against aggregation-prone proteins via autophagy. FM Menzies R Hourez S Imarisio M Raspe O Sadiq D Chandraratna C O'Kane KL Rock E Reits AL Goldberg,, et al. Hum Mol Genet 2010 19 4573 4586 10.1093/hmg/ddq385 20829225
27. Immunocytochemistry and quantification of protein colocalization in cultured neurons. MW Glynn AK McAllister, Nat Protoc 2006 1 1287 1296 10.1038/nprot.2006.220 17406413
28. Modulation of polyglutamine-induced cell death by genes identified by expression profiling. H Kita J Carmichael J Swartz S Muro A Wyttenbach K Matsubara DC Rubinsztein K Kato, Hum Mol Genet 2002 11 2279 2287 10.1093/hmg/11.19.2279 12217956
29. Puromycin-sensitive aminopeptidase (PSA/NPEPPS) impedes development of neuropathology in hPSA/TAUP301L double-transgenic mice. LC Kudo L Parfenova G Ren N Vi M Hui Z Ma K Lau M Gray F Bardag-Gorce M Wiedau-Pazos,, et al. Hum Mol Genet 2011 20 1820 33 10.1093/hmg/ddr065 21320871
30. An automatic continuous-flow aminopeptidase detector and its applications. KS Hui M Hui, Anal Biochem 1996 242 271 273 10.1006/abio.1996.0464 8937573 (Pubitemid 26386825)
31. Proteinases and peptidases. KS Hui A Lajtha, Neuromethods New Jersey: Humana Press, Boulton AA, Baker GB, Yu PH, 1 1986 V 421 450
32. A novel neuron-specific aminopeptidase in rat brain synaptosomes. Its identification, purification, and characterization. KS Hui M Saito M Hui, J Biol Chem 1998 273 31053 31060 10.1074/jbc.273.47.31053 9813004 (Pubitemid 28533112)
33. Motor neuron degeneration in mice that express a human Cu, Zn superoxide dismutase mutation. ME Gurney H Pu AY Chiu MC Dal Canto CY Polchow DD Alexander J Caliendo A Hentati YW Kwon HX Deng,, et al. Science 1994 264 1772 1775 10.1126/science.8209258 8209258 (Pubitemid 24227760)
34. Transgenic mice with increased Cu/Zn-superoxide dismutase activity: animal model of dosage effects in Down syndrome. CJ Epstein KB Avraham M Lovett S Smith O Elroy-Stein G Rotman C Bry Y Groner, Proc Natl Acad Sci USA 1987 84 8044 8048 10.1073/pnas.84.22.8044 2960971
35. Lack of evidence of monomer/misfolded superoxide dismutase-1 in sporadic amyotrophic lateral sclerosis. HN Liu T Sanelli P Horne EP Pioro MJ Strong E Rogaeva J Bilbao L Zinman J Robertson, Ann Neurol 2009 66 75 80 10.1002/ana.21704 19670443
36. Amyotrophic lateral sclerosis is a non-amyloid disease in which extensive misfolding of SOD1 is unique to the familial form. A Kerman HN Liu S Croul J Bilbao E Rogaeva L Zinman J Robertson A Chakrabartty, Acta Neuropathol 2010 119 335 344 10.1007/s00401-010-0646-5 20111867
37. Bringing SOD1 into the fold. S Barmada S Finkbeiner, Nat Neurosci 2010 13 1303 1304 10.1038/nn1110-1303 20975748
38. Integrative gene-tissue microarray-based approach for identification of human disease biomarkers: application to amyotrophic lateral sclerosis. LC Kudo L Parfenova N Vi K Lau J Pomakian P Valdmanis GA Rouleau HV Vinters M Wiedau-Pazos SL Karsten, Hum Mol Genet 2010 19 3233 3253 10.1093/hmg/ddq232 20530642