Dual roles of proteasome in the metabolism of Presenilin 1

Journal of Neurochemistry

Volumn 72, Issue 1, 1999, Pages 255-261

  Honda, Toshiyuki ^b,c,d   Yasutake, Kaori ^a   Nihonmatsu, Naomi ^c   Mercken, Mark ^a   Takahashi, Hiroshi ^a   Murayama, Ohoshi ^c   Murayama, Miyuki ^c   Sato, Kazuki ^a   Omori, Akira ^a   Tsubuki, Satoshi ^b   Saido, Takaomi C ^b   Takashima, Akihiko ^c  

^a MITSUBISHI KASEI INST OF LIFE SCI   (Japan)

^b RIKEN BRAIN SCIENCE INSTITUTE   (Japan)

^c Institute of Physical and Chemical Research   (Japan)

^d MITSUBISHI CHEMICAL CORPORATION   (Japan)

Author keywords

Alzheimer's disease; Presenilin; Proteasome; Proteolytic processing

Indexed keywords

COMPLEMENTARY DNA; PRESENILIN 1; PROTEASOME; PROTEASOME INHIBITOR; SYNTHETIC PEPTIDE;

ALZHEIMER DISEASE; ARTICLE; CONTROLLED STUDY; DEGENERATIVE DISEASE; DEMENTIA; EMBRYO; HUMAN; HUMAN CELL; NEUROBLASTOMA CELL; PRIORITY JOURNAL; PROTEIN CONTENT; PROTEIN DEGRADATION;

ACETYLCYSTEINE; ALZHEIMER DISEASE; AMINO ACID SEQUENCE; BRAIN CHEMISTRY; COUMARINS; CYSTEINE ENDOPEPTIDASES; CYSTEINE PROTEINASE INHIBITORS; GLYCOPROTEINS; HUMANS; KIDNEY; MEMBRANE PROTEINS; MOLECULAR SEQUENCE DATA; MULTIENZYME COMPLEXES; MUTATION; NEUROBLASTOMA; PEPTIDE FRAGMENTS; PRECIPITIN TESTS; PRESENILIN-1; PROTEASOME ENDOPEPTIDASE COMPLEX; SERINE PROTEINASE INHIBITORS; SULFONES; TRYPSIN INHIBITORS; TUMOR CELLS, CULTURED;

EID: 0032925297     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1999.0720255.x     Document Type: Article

References (36)

1. Alzheimer's Disease Collaborative Group (1995) The structure of the presenilin 1 (S 182) gene and identification of six novel mutations in early onset AD families. Nat. Genet. 11, 219-222.
2. Borchelt D. R., Thinakaran G., Eckman C. B., Lee M. K., Davenport F., Ratovitsky T., Prada C. M., Kim G., Seekins S., Yager D., Slunt H. H., Wang R., Seeger M., Levey A. I., Candy S. E., Copeland N. G., Jenkins N. A., Price D. L., Younkin S. G., and Sisodia S. S. (1996) Familial Alzheimer's disease-linked presenilin 1 variants elevate Aβ1-42/1-40 ratio in vitro and in vivo. Neuron 17, 1005-1013.
3. Brodsky J. L. and McCraken A. A. (1997) ER-associated and proteasome-mediated protein degradation: how two topologically restricted events came together. Trends Cell Biol 7, 151-156.
4. Citron M., Westaway D., Xia W., Carlson G., Diehl T., Levesque G., Johnson-Wood K., Lee M., Seubert P., Davis A.. Kholodenko D., Motter R., Sherrington R., Perry B., Yao H., Strome R., Lieberburg I., Rommens J., Kim S., Schenk D., Fraser P., St. George Hyslop P., and Selkoe D. J. (1997) Mutant presenilins of Alzheimer's disease increase production of 42-residue amyloid β-protein in both transfected cells and transgenic mice. Nat. Med. 3, 67-72.
5. Duff K., Eckman C., Zehr C., Yu X., Prada C. M., Perez-tur J., Hutton M., Buee L., Harigaya Y., Yager D., Morgan D., Gordon M. N., Holcomb L. Refolo L., Zenk B., Hardy J., and Younkin S. (1996) Increased amyloid-β42(43) in brains of mice expressing mutant presenilin 1. Nature 383, 710-713.
6. Fan C. M. and Maniatis T. (1991) Generation of p50 subunit of NF-κ-B by processing of p105 through an ATP-dependent pathway. Nature 354, 395-398.
7. Fraser P. E., Levesque G., Yu G., Mills L. R., Thirlwell J., Frantseva M., Gandy S. E., Seeger M., Carlen P. L., and St. George-Hyslop P. (1998) Presenilin 1 is actively degraded by the 26S proteasome. Neurobiol. Aging 19, S19-S21.
8. Kim D. W., Uetsuki T., Kaziro Y., Yamaguchi N., and Sugano S. (1990) Use of the human elongation factor 1α promoter as a versatile and efficient expression system. Gene 91, 217-223.
9. Kim T. W., Pettingell W. H., Hallmark O. G., Moir R. D., Wasco W., and Tanzi R. E. (1997) Endoproteolytic cleavage and proteasomal degradation of presenilin 2 in transfected cells. J. Biol. Chem. 272, 11006-11010.
10. Kopito R. R. (1997) ER quality control: the cytoplasmic connection. Cell 88, 427-430.
11. Lemere C. A., Lopera F., Kosik K. S., Lendon C. L., Ossa J., Saido T. C., Yamaguchi H., Ruiz A., Martinez A., Madrigal L., Hincapie L., Arango J. C., Anthony D. C., Koo E. H., Goate A. M., Selkoe D. J., and Arango J. C. (1996) The E280A presenilin 1 Alzheimer mutation produces increased Aβ42 deposition and severe cerebellar pathology. Nat. Med. 2, 1146-1150.
12. Levy-Lahad E., Wasco W., Poorkaj P., Romano D. M., Oshima J., Pettingell W. H., Yu C. E., Jondro P. D., Schmidt S. D., Wang K., Crowley A. C., Fu Y.-H., Guenette S. Y., Galas D., Nemens E., Wijsman E. M., Bird T. D., Schellenberg G. D., and Tanzi R. E. (1995a) Candidate gene for the chromosome 1 familial Alzheimer's disease locus. Science 269, 973-977.
13. Levy-Lahad E., Wijsman E. M., Nemens E., Anderson L., Goddard K. A., Weber J. L., Bird T. D., and Schellenberg G. D. (1995b) A familial Alzheimer's disease locus on chromosome 1. Science 269, 970-973.
14. Marambaud P., Chevallier N., Barelli H., Wilk S., and Checler F. (1997a) Proteasome contributes to the α-secretase pathway of amyloid precursor protein in human cells. J. Neurochem. 68, 698-703.
15. Marambaud P., Lopez-Perez E., Wilk S., and Checler F. (1997b) Constitutive and protein kinase C-regulated secretory cleavage of Alzheimer's β-amyloid precursor protein: different control of early and late events by the proteasome. J. Neurochem. 69, 2500-2505.
16. Marambaud P., Ancolio K., Lopez-Perez E., and Checler F. (1998) Proteasome inhibitors prevent the degradation of familial Alzheimer's disease-linked presenilin 1 and potentiate A beta 42 recovery from human cells. Mol. Med. 4, 147-157.
17. Martins R. N., Turner B. A., Carroll R. T., Sweeney D., Kim K. S., Wisniewski H. M., Blass J. P., Gibson G. E., and Gandy S. (1995) High levels of amyloid-β protein from S182 (Glu246) familial Alzheimer's cells. Neuroreport 7, 217-220.
18. McDermott J. R. and Gibson A. M. (1991) The activity of the high-Mr multicatalytic protease in normal brain and brain from Alzheimer's disease patients. Neurosci. Res. Commun. 8, 185-190.
19. Mercken M., Takahashi H., Honda T., Sato K., Murayama M., Nakazato Y., Noguchi K., Imahori K., and Takashima A. (1996) Characterization of human presenilin 1 using N-terminal specific monoclonal antibodies: evidence that Alzheimer mutations affect proteolytic processing. FEBS Lett. 389, 297-303.
20. Muller S. and Schwartz L. M. (1995) Ubiquitin in homeostasis, development and disease. Bioessays 17, 677-684.
21. Murayama O., Honda T., Mercken M., Murayama M., Yasutake K., Nihonmatsu N., Nakazato Y., Michel G., Song S., Sato K., Takahashi H., and Takashima A. (1997) Different effects of Alzheimerassociated mutations of presenilin 1 on its processing. Neurosci. Lett. 229, 61-64.
22. Omura S., Fujimoto T., Otoguro K., Matsuzaki K., Moriguchi R., Tanaka H., and Sasaki Y. (1991) Lactacystin, a novel microbial metabolite, induces neuritogenesis of neuroblastoma cells. J. Antibiot. (Tokyo) 44, 113-116.
23. Palombella V. J., Rando O. J., Goldberg A. L., and Maniatis T. (1994) The ubiquitin-proteasome pathway is required for processing the NF-κBl precursor protein and the activation of NF-κB. Cell 78, 773-785.
24. Podlisny M. B., Citron M., Amarante P., Sherrington R., Xia W., Zhang J., Diehl T., Levesque G., Fraser P., Haass C., Koo E. H., Seubert P., St. George-Hyslop P., Teplow D. B., and Selkoe D. J. (1997) Presenilin proteins undergo heterogeneous endoproteolysis between Thr291 and Ala299 and occur as stable N-and C-terminal fragments in normal and Alzheimer brain tissue. Neurobiol. Dis. 3, 325-337.
25. Rogaev E. I., Sherrington R., Rogaeva E. A., Levesque G., Ikeda M., Liang Y., Chi H., Lin C., Holman K., Tsuda T., Mar L., Sorbi S., Nacmias B., Piacentini S., Amaducci L., Chumakov I., Cohen D., Lannfelt L., Fraser P. E., Rommens J. M., and St. George-Hyslop P. H. (1995) Familial Alzheimer's disease in kindreds with missense mutations in gene on chromosome 1 related to the Alzheimer's disease type 3 gene. Nature 376, 775-778.
26. Scheuner D., Eckman C., Jensen M., Song X., Citron M., Suzuki N., Bird T. D., Hardy J., Hutton M., Kukull W., Larson E., Levy-Lahad E., Viitanen M., Peskind E., Poorkaj P., Schellenberg G., Tanzi R., Wasco W., Lannfelt L., Selkoe D., and Younkin S. (1996) Secreted amyloid β-protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease. Nat. Med. 2, 864-870.
27. Seeger M., Nordstedt C., Petanceska S., Kovacs D. M., Gouras G. K., Hahne S., Fraser P., Levesque L., Czernik A. J., St. George-Hyslop P. S., Sisodia S. S., Thinakaran G., Tanzi R. E., Greengard P., and Gandy S. (1997) Evidence for phosphorylation and oligomeric assembly of presenilin 1. Proc. Natl. Acad. Sci. USA 94, 5090-5094.
28. Sherrington R., Rogaev E. I., Liang Y., Rogaeva E. A., Levesque G., Ikeda M., Chi H., Lin C., Li G., Holman K., Tsuda T., Mar L., Foncin J.-F., Bruni A. C., Montesi M. P., Sorbi S., Rainero I., Pinessi L., Nee L., Chumakov I., Pollen D., Brookes A., Sanseau P., Polinsky R. J., Wasco W., Da Silva H. A. R., Haines J. L., Pericak-Vance M. A., Tanzi R. E., Roses A. D., Fraser P. E., Rommens J. M., and St. George-Hyslop P. H. (1995) Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease. Nature 375, 754-760.
29. Takashima A., Sato M., Mercken M., Tanaka S., Kondo S., Honda T., Sato K., Murayama M., Noguchi K., Nakazato Y., and Takahashi H. (1996) Localization of Alzheimer-associated presenilin 1 in transfected COS-7 cells. Biochem. Biophys. Res. Commun. 227, 423-426.
30. Thinakaran G., Borchelt D. R., Lee M. K., Slunt H. H., Spitzer L., Kim G., Ratovitsky T., Davenport F., Nordstedt C., Seeger M., Hardy J., Levey A. I., Gandy S. E., Jenkins N. A., Copeland N. G., Price D. L., and Sisodia S. S. (1996) Endoproteolysis of presenilin 1 and accumulation of processed derivatives in vivo. Neuron 17, 181-190.
31. Tomita T., Maruyama K., Saido T. C., Kume H., Shinozaki K., Tokuhiro S., Capell A., Walter J., Grunberg J., Haass C., Iwatsubo T., and Obata K. (1997) The presenilin 2 mutation (N141I) linked to familial Alzheimer disease (Volga German families) increases the secretion of amyloid β protein ending at the 42nd (or 43rd) residue. Proc. Natl. Acad. Sci. USA 94, 2025-2030.
32. Walter J., Capell A., Grunberg J., Pesold B., Schindzielorz A., Prior R., Podlisny M. B., Fraser P., Hyslop P. S., Selkoe D. J., and Haass C. (1996) The Alzheimer's disease-associated presenilins are differentially phosphorylated proteins located predominantly within the endoplasmic reticulum. Mol. Med. 2, 673-691.
33. Walter J., Grunberg J., Capell A., Pesold B., Schindzielorz A., Citron M., Mendla K., George-Hyslop P. S., Multhaup G., Selkoe D. J., and Haass C. (1997) Proteolytic processing of the Alzheimer disease-associated presenilin-1 generates an in vivo substrate for protein kinase C. Proc. Natl. Acad. Sci. USA 94, 5349-5354.
34. Wisniewski T., Dowjat W. K., Permanne B., Palha J., Kumar A., Gallo G., and Frangione B. (1997) Presenilin-1 is associated with Alzheimer's disease amyloid. Am. J. Pathol. 151, 601-610.
35. Xia W., Zhang J., Kholodenko D., Citron M., Podlisny M. B., Teplow D. B., Haass C., Seubert P., Koo E. H., and Selkoe D. J. (1997) Enhanced production and oligomerization of the 42-residue amyloid β-protein by Chinese hamster ovary cells stably expressing mutant presenilins. J. Biol. Chem. 272, 7977-7982.
36. Yamazaki T., Haass C., Saido T. C., Omura S., and Ihara Y. (1997) Specific increase in amyloid β-protein 42 secretion ratio by calpain inhibition. Biochemistry 36, 8377-8383.