TMP21 regulates Aβ production but does not affect caspase-3, p53, and neprilysin

Biochemical and Biophysical Research Communications

Volumn 371, Issue 1, 2008, Pages 69-74

  Dolcini, Virginia ^a   Dunys, Julie ^a   Sevalle, Jean ^a   Chen, Fusheng ^b,c   Guillot Sestier, Marie Victoire ^a   St George Hyslop, Peter ^b,c   Fraser, Paul E ^b,c   Checler, Frédéric ^a  

^a CNRS   (France)

^b UNIVERSITY OF TORONTO   (Canada)

^c Department of Medical Biophysics ^*  (Canada)

Author keywords

Secretase; Secretase; Caspase 3; HEK293 cell line; Neprilysin; p53; siRNA; TMP21

Indexed keywords

AMYLOID BETA PROTEIN; CASPASE 3; EPSILON SECRETASE; GAMMA SECRETASE; MEMBRANE METALLOENDOPEPTIDASE; PROTEIN; PROTEIN P53; SECRETASE; STAUROSPORINE; TMP21 PROTEIN; AMYLOID BETA PROTEIN[1-40]; MEMBRANE PROTEIN; PEPTIDE FRAGMENT; SMALL INTERFERING RNA; TMP21 PROTEIN, HUMAN;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; EMBRYO; ENZYME ACTIVATION; ENZYME ACTIVITY; HUMAN; HUMAN CELL; MOUSE; NONHUMAN; PHENOTYPE; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PROTEIN INTERACTION; PROTEIN SECRETION; ANIMAL; CELL LINE; DRUG ANTAGONISM; GENETICS; METABOLISM;

AMYLOID BETA-PROTEIN; AMYLOID PRECURSOR PROTEIN SECRETASES; ANIMALS; CASPASE 3; CELL LINE; HUMANS; MEMBRANE PROTEINS; MICE; NEPRILYSIN; PEPTIDE FRAGMENTS; RNA, SMALL INTERFERING; TUMOR SUPPRESSOR PROTEIN P53;

EID: 43049094119     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2008.03.151     Document Type: Article

References (44)

1. F. Chen, H. Hasegawa, G. Schmitt-ulms, T. Kawarai, C. Bohm, T. Katayama, Y. Gu, N. Sanjo, M. Glista, E. Rogaeva, Y. Wakutami, R. Pardossi-Piquard, X. Ruan, A. Tandon, F. Checler, P. Marambaud, K. Hansen, D. Westaway, P. St. George-Hyslop, P. Fraser, TMP21 is a presenilin complex component that modulates γ- but not ε-secretase activities, Nature 440 (2006) 1208-1212.
2. Selkoe D.J. Alzheimer's disease: genes, proteins and therapy. Physiol. Rev. 81 (2001) 741-766
3. Checler F. Processing of the β-amyloid precursor protein and its regulation in Alzheimer's disease. J. Neurochem. 65 (1995) 1431-1444
4. Weidemann A., Eggert S., Reinhard F.B.M., Vogel M., Paliga K., Baier G., Masters C.L., Beyreuther K., and Evin G. A novel ε-cleavage within the transmembrane domain of the Alzheimer amyloid precursor protein demonstrates homology with the Notch processing. Biochemistry 41 (2002) 2825-2835
5. De Strooper B., Saftig P., Craessaerts K., Vanderstichele H., Guhde G., Von Figura K., and Van Leuven F. Deficiency of presenilin 1 inhibits the normal cleavage of amyloid precursor protein. Nature 391 (1998) 387-390
6. Armogida M., Petit A., Vincent B., Scarzello S., Alves da Costa C., and Checler F. Endogenous β-amyloid production in presenilin-deficient embryonic mouse fibroblasts. Nat. Cell. Biol. 3 (2001) 1030-1033
7. Wilson C.A., Doms R.W., and Lee V.M.-Y. Distinct presenilin-dependent and presenilin-independent γ-secretases are responsible for total cellular Aβ production. J. Neurosci. Res. 74 (2003) 361-369
8. Lai M.-T., Crouthamel M.-C., DiMuzio J., Pietrak B.L., Donoviel D.B., Bernstein A., Gardell S.J., Li Y.-M., and Hazuda D. A presenilin-independent aspartyl protease prefers the γ-42 site cleavage. J. Neurochem. 96 (2006) 118-125
9. Takasugi N., Tomita T., Hayashi I., Tsuruoka M., Niimura M., Takahashi Y., Thinakaran G., and Iwatsubo T. The role of presenilin cofactors in the γ-secretase complex. Nature 422 (2003) 438-441
10. Levitan D., Doyle T.G., Brousseau D., Lee M.K., Thinakaran G., Slunt H.H., Sisodia S.S., and Greenwald I. Assessment of normal and mutant human presenilin function in Caenorhabditis elegans. Proc. Natl. Acad. Sci. USA 93 (1996) 14940-14944
11. Zhang D.M., Levitan D., Yu G., Nishimura M., Chen F., Tandon A., Kawarai T., Arawaka S., Supala A., Song Y.Q., Rogaeva E., Liang Y., Holmes E., Milman P., Sato C., Zhang L., and St. George-Hyslop P. Mutation of the conserved N-terminal cysteine (Cys92) of human presenilin1 causes increased A beta secretion in mammalian cells but impaired Notch/lin-12 signalling in C. elegans. Neuroreport 11 (2000) 3227-3230
12. Petit A., Bihel F., Alves da Costa C., Pourquié O., Kraus J.L., and Checler F. New protease inhibitors prevent γ-secretase-mediated Aβ40/42 production without affecting Notch cleavage. Nat. Cell. Biol. 3 (2001) 507-511
13. Chen F., Gu Y., Hasegawa H., Ruan X., Arawaka S., Fraser P., Westaway D., Mount H., and St. George-Hyslop P. Presenilin 1 mutations activate γ-42-secretase but reciprocally inhibit μ-secretase cleavage of APP and S3-cleavage of Notch. J. Biol. Chem. 277 (2002) 36521-36526
14. Blum R., Feick P., Puype M., Vandekerckhove J., Klengel R., Nastainczyk W., and Schulz I. Tmp21 and p24A, two type I proteins enriched in pancreatic microsomal membranes, are members of a protein family involved in vesicular trafficking. J. Biol. Chem. 271 (1996) 17183-17189
15. Cao X., and Südhof T.C. A transcriptively active complex of APP with Fe65 and histone acetyltransferase tip60. Science 293 (2001) 115-120
16. Baek S.H., Ohgi K.A., Rose D.W., Koo E.H., Glass C.K., and Rosenfeld M.G. Exchange of N-CoR corepressor and Tip60 coactivator complexes links gene expression by NF-κB and β-amyloid precursor protein. Cell 110 (2002) 55-67
17. von Rotz R.C., Kohli B.M., Bosset J., Meier M., Suzuki T., Nitsch R.M., and Konietzko U. The APP intracellular domain forms nuclear multiprotein complexes and regulates the transcription of its own precursor. J. Cell Sci. 117 (2004) 4435-4448
18. Pardossi-Piquard R., Petit A., Kawarai T., Sunyach C., Alves da Costa C., Vincent B., Ring S., D'Adamio L., Shen J., Müller U., St. George-Hyslop P., and Checler F. Presenilin-dependent transcriptional control of the Aβ-degrading enzyme neprilysin by intracellular domains of βAPP and APLP. Neuron 46 (2005) 541-554
19. Zhang Y.W., Wang R., Liu Q., Zhang H., Liao F.F., and Xu H. Presenilin/gamma-secretase-dependent processing of beta-amyloid precursor protein regulates EGF receptor expression. Proc. Natl. Acad. Sci. USA 104 (2007) 10613-10618
20. Alves da Costa C., Sunyach C., Pardossi-Piquard R., Sevalle J., Vincent B., Boyer N., Kawarai T., Girardot N., St. George Hyslop P., and Checler F. Presenilin-dependent γ-secretase-mediated control of p53-associated cell death in Alzheimer's disease. J. Neurosci. 26 (2006) 6377-6385
21. Ancolio K., Dumanchin C., Barelli H., Warter J.M., Brice A., Campion D., Frébourg T., and Checler F. Unusual phenotypic alteration of β amyloid precursor protein (βAPP) maturation by a new Val->Met βAPP-770 mutation responsible for probable early-onset Alzheimer's disease. Proc. Natl. Acad. Sci. USA 96 (1999) 4119-4124
22. Alves da Costa C., Paitel E., Mattson M.P., Amson R., Telerman A., Ancolio K., and Checler F. Wild-type and mutated presenilin-2 trigger p53-dependent apoptosis and down-regulate presenilin-1 expression in HEK293 human cells and in murine neurons. Proc. Natl. Acad. Sci. USA 99 (2002) 4043-4048
23. Dunys J., Kawarai T., Sevalle J., Dolcini V., St. George-Hyslop P., Alves da Costa C., and Checler F. p53-dependent Aph-1 and Pen-2 anti-apoptotic phenotype requires the integrity of the gamma -secretase complex but is independent of its activity. J. Biol. Chem. 282 (2007) 10516-10525
24. Chevallier N., Jiracek J., Vincent B., Baur C.P., Spillantini M.G., Goedert M., Dive V., and Checler F. Examination of the role of endopeptidase 3.4.24.15 in Aβ secretion by human transfected cells. Br. J. Pharmacol. 121 (1997) 556-562
25. Barelli H., Lebeau A., Vizzavona J., Delaere P., Chevallier N., Drouot C., Marambaud P., Ancolio K., Buxbaum J.D., Khorkova O., Heroux J., Sahasrabudhe S., Martinez J., Warter J.-M., Mohr M., and Checler F. Characterization of new polyclonal antibodies specific for 40 and 42 aminoacid-long amyloid β peptides: their use to examine the cell biology of presenilins and the immunohistochemistry of sporadic Alzheimer's disease and cerebral amyloid angiopathy cases. Mol. Med. 3 (1997) 695-707
26. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-259
27. Gu Y., Sanjo N., Chen F., Hasegawa H., Petit A., Ruan X., Li W., Shier C., Kawarai T., Schmitt-Ulms G., Westaway D., George-Hyslop P.St., and Fraser F.W. The presenilin proteins are components of multiple membrane-bound complexes which have different biological activities. J. Biol. Chem. 279 (2004) 31329-31336
28. Evin G., Canterford L.D., Hoke D.E., Sharples R.A., Culvenor J.G., and Masters C.L. Transition-state analogue g-secretase inhibitors stabilize a 9OO KDa presenilin/nicastrin complex. Biochemistry 44 (2005) 4332-4341
29. Sato T., Diehl T.S., Narayanan S., Funamoto S., Ihara Y., De Strooper B., Steiner H., Haass C., and Wolfe M.S. Active {gamma}-secretase complexes contain only one of each component. J. Biol. Chem. 282 (2007) 33985-33993
30. Edbauer D., Winkler E., Regula J.T., Pesold B., Steiner H., and Haass C. Reconstitution of γ-secretase activity. Nat. Cell Biol. 5 (2003) 486-488
31. Kimberly W.T., LaVoie M.J., Ostaszewski B.L., Ye W., Wolfe M.S., and Selkoe D.J. γ-secretase is a membrane protein complex comprised of presenilin, nicastrin, aph-1 and pen-2. Proc. Natl. Acad. Sci. USA 100 (2003) 6382-6387
32. Passer B., Pellegrini L., Russo C., Siegel R.M., Lenardio M.J., Schettini G., Bachmann M., Tabaton M., and D'Adamio L. Generation of an apoptotic intracellular peptide by γ-secretase cleavage of Alzheimer's amyloid β protein precursor. J. Alzheimer's Dis. 2 (2000) 289-301
33. Pardossi-Piquard R., Dunys J., Yu G., St. George-Hyslop P., Alves da Costa C., and Checler F. Neprilysin activity and expression are controlled by nicastrin. J. Neurochem. 97 (2006) 1052-1056
34. Gu Y., Misonou H., Sato T., Dohmae N., Takio K., and Ihara Y. Distinct intramembrane cleavages of the β-amyloid precursor protein family resembling γ-secretase-like cleavage of Notch. J. Biol. Chem. 276 (2001) 35235-35238
35. Sastre M., Steiner H., Fuchs K., Capell A., Multhaup G., Condron M.M., Teplow D.B., and Haass C. Presenilin dependent γ-secretase processing of β-amyloid precursor protein at a site corresponding to the S3 cleavage of Notch. EMBO Rep. 2 (2001) 835-841
36. Kume H., Maruyama K., and Kametani F. Intracellular domain generation of amyloid precursor protein by ε-cleavage depends on C-terminal fragment by a-secretase cleavage. Int. J. Mol. Med. 13 (2004) 121-125
37. Lefranc-Jullien S., Sunyach C., and Checler F. APPε, the ε-secretase-derived N-terminal product of the β-amyloid precursor protein, behaves as a type I protein and undergoes α-, β- and γ-secretase cleavages. J. Neurochem. 97 (2006) 807-817
38. Sato T., Dohmae N., Qi Y., Kakuda N., Misonou H., Mitsumori R., Maruyama K., Koo E.H., Haass C., Takio K., Morishima-Kawashima M., Ishiura S., and Ihara Y. Potential link between amyloid β-protein 42 and C-terminal fragment γ49-99 of β-amyloid precursor protein. J. Biol. Chem. 278 (2003) 20294-20301
39. Funamoto S., Morishima-Kawashima M., Tanimura Y., Hirotani N., Saido T.C., and Ihara M. Truncated carboxyl-terminal fragments of β-amyloid precursor protein are processed to amyloid β-proteins 40 and 42. Biochemistry 43 (2004) 13532-13540
40. Kulic L., Walter J., Multhaup G., Teplow D.B., Baumeister R., Romig H., Capell A., Steiner H., and Haass C. Separation of presenilin function in amyloid β-peptide generation and endoproteolysis of Notch. Proc. Natl. Acad. Sci. USA 97 (2000) 5913-5918
41. Moelhmann T., Winkler E., Xia X., Edbauer D., Murrell J., Capell A., Kaether C., Zheng H., Ghetti B., Haass C., and Steiner H. Presenilin-1 mutations of leucine 166 equally affect the generation of the notch and APP intracellular domains independent of their effect on Aβ42 production. Proc. Natl. Acad. Sci. USA 99 (2002) 8025-8030
42. Weggen S., Eriksen J.L., Das P., Sagi S.A., Wang R., Pietzik C.U., Findlay K.A., Smith T.E., Murphy M.P., Bulter T., Kang D.E., Marquez-Sterling N., Golde T.E., and Koo E.H. A subset of NSAIDs lower amyloidogenic Ab42 independently of cyclooxygenase activity. Nature 414 (2001) 212-216
43. Netzer W.J., Dou F., Cai D., Veach D., Jean S., Li Y., Bornmann W.G., Clarkson B., Xu H., and Greengard P. Gleevec inhibits β-amyloid production but not Notch cleavage. Proc. Natl. Acad. Sci. USA 100 (2003) 12444-12449
44. Phiel C.J., Wilson C.A., Lee V.M.-Y., and Klein P.S. GSK-3α regulates production of Alzheimer's disease amyloid-β peptides. Nature 423 (2003) 435-439