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Llovera, R.E.; De Tullio, M.; Alonso, L.G.; Leissring, M.A.; Kaufman, S.B.; Roher, A.E.; Gay, G.D.P.; Morelli, L.; Castaño, E.M. "The catalytic domain of insulin-degrading enzyme forms a denaturant-resistant complex with amyloid β peptide: Implications for Alzheimer disease pathogenesis" (2008) Journal of Biological Chemistry. 283(25):17039-17048
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Abstract:

Insulin-degrading enzyme (IDE) is central to the turnover of insulin and degrades amyloid β (Aβ) in the mammalian brain. Biochemical and genetic data support the notion that IDE may play a role in late onset Alzheimer disease (AD), and recent studies suggest an association between AD and diabetes mellitus type 2. Here we show that a natively folded recombinant IDE was capable of forming a stable complex with Aβ that resisted dissociation after treatment with strong denaturants. This interaction was also observed with rat brain IDE and detected in an SDS-soluble fraction from AD cortical tissue. Aβ sequence 17-27, known to be crucial in amyloid assembly, was sufficient to form a stable complex with IDE. Monomeric as opposed to aggregated Aβ was competent to associate irreversibly with IDE following a very slow kinetics (t1/2 ∼ 45 min). Partial denaturation of IDE as well as preincubation with a 10-fold molar excess of insulin prevented complex formation, suggesting that the irreversible interaction of Aβ takes place with at least part of the substrate binding site of the protease. Limited proteolysis showed that Aβ remained bound to a ∼25-kDa N-terminal fragment of IDE in an SDS-resistant manner. Mass spectrometry after in gel digestion of the IDE·Aβ complex showed that peptides derived from the region that includes the catalytic site of IDE were recovered with Aβ. Taken together, these results are suggestive of an unprecedented mechanism of conformation-dependent substrate binding that may perturb Aβ clearance, insulin turnover, and promote AD pathogenesis. © 2008 by The American Society for Biochemistry and Molecular Biology, Inc.

Registro:

Documento: Artículo
Título:The catalytic domain of insulin-degrading enzyme forms a denaturant-resistant complex with amyloid β peptide: Implications for Alzheimer disease pathogenesis
Autor:Llovera, R.E.; De Tullio, M.; Alonso, L.G.; Leissring, M.A.; Kaufman, S.B.; Roher, A.E.; Gay, G.D.P.; Morelli, L.; Castaño, E.M.
Filiación:Fundación Instituto Leloir-Instituto de Investigaciones Bioquímicas de Buenos Aires, Consejo Nacional de Investigaciones Científicas Y Técnicas (CONICET), 435 Av. Patricias Argentinas, Ciudad de Buenos Aires C1405BWE, Argentina
Department of Biomedical Sciences, Scripps Florida, Jupiter, FL 33458, United States
Instituto de Química y Fisicoquímica Biológicas- CONICET, Departamento de Química Biológica, Universidad de Buenos Aires, Buenos Aires, Argentina
Sun Health Research Institute, Sun City, AZ 85351, United States
Palabras clave:Amines; Binding energy; Binding sites; Colloids; Diffusers (optical); Enzymes; Flow interactions; Forming; Gelation; Glycoproteins; High performance liquid chromatography; Hormones; Insulin; Mammals; Mass spectrometry; A stables; After treatments; Alzheimer diseases; Catalytic domains; Catalytic sites; Complex formations; Cortical tissues; Degrading enzymes; Diabetes Mellitus; Genetic datums; Limited proteolyses; Mammalian brains; Molar excesses; Partial denaturations; Rat brains; Soluble fractions; Substrate bindings; Terminal fragments; Integrodifferential equations; amyloid beta protein; dodecyl sulfate sodium; insulinase; recombinant enzyme; Alzheimer disease; amino terminal sequence; article; binding site; complex formation; controlled study; enzyme active site; enzyme denaturation; human; human tissue; nonhuman; pathogenesis; priority journal; protein conformation; protein degradation; protein domain; protein folding; protein protein interaction; rat; animal; biological model; brain; chemistry; enzyme specificity; kinetics; mass spectrometry; metabolism; pathology; protein binding; radiation scattering; Mammalia; Rattus; Alzheimer Disease; Amyloid beta-Protein; Animals; Binding Sites; Brain; Catalytic Domain; Humans; Insulysin; Kinetics; Mass Spectrometry; Models, Biological; Protein Binding; Rats; Scattering, Radiation; Substrate Specificity
Año:2008
Volumen:283
Número:25
Página de inicio:17039
Página de fin:17048
DOI: http://dx.doi.org/10.1074/jbc.M706316200
Título revista:Journal of Biological Chemistry
Título revista abreviado:J. Biol. Chem.
ISSN:00219258
CODEN:JBCHA
CAS:amyloid beta protein, 109770-29-8; dodecyl sulfate sodium, 151-21-3; insulinase, 9013-83-6; Amyloid beta-Protein; Insulysin, EC 3.4.24.56
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00219258_v283_n25_p17039_Llovera

Referencias:

  • Morelli, L., Llovera, R., Ibendhal, S., Castaño, E.M., (2002) Neurochem. Res, 27, pp. 1387-1399
  • Harper, J.D., Lansbury Jr., P.T., (1997) Annu. Rev. Biochem, 66, pp. 385-407
  • Iwata, N., Tsubuki, S., Takaki, Y., Shirotani, K., Lu, B., Gerard, N.P., Gerard, C., Saido, T.C., (2001) Science, 292, pp. 1550-1552
  • Farris, W., Mansourian, S., Chang, Y., Lindsley, L., Eckman, E.A., Frosch, M.P., Eckman, C.B., Guenette, S., (2003) Proc. Natl. Acad. Sci. U. S. A, 100, pp. 4162-4167
  • Miller, B.C., Eckman, E.A., Sambamurti, K., Dobbs, N., Chow, K.M., Eckman, C.B., Hersh, L.B., Thiele, D.L., (2003) Proc. Natl. Acad. Sci. U. S. A, 100, pp. 6221-6226
  • Eckman, E.A., Watson, M., Marlow, L., Sambamurti, K., Eckman, C.B., (2003) J. Biol. Chem, 278, pp. 2081-2084
  • Leissring, M.A., Farris, W., Chang, A.Y., Walsh, D.M., Wu, X., Sun, X., Frosch, M.P., Selkoe, D.J., (2003) Neuron, 40, pp. 1087-1093
  • Roth, R., (2004) Handbook of Proteolytic Enzymes, pp. 868-876. , Barrett, A. J, Rawlings, N. D, and Woessner, J. F, eds pp, Elsevier Academic Press, New York
  • Qiu, W.Q., Walsh, D.M., Ye, Z., Vekrellis, K., Zhang, J., Podlisny, M.B., Rosner, M.R., Selkoe, D.J., (1998) J. Biol. Chem, 273, pp. 32730-32738
  • Sudoh, S., Frosch, M.P., Wolf, B.A., (2002) Biochemistry, 41, pp. 1091-1099
  • Kurochkin, I.V., (2001) Trends Biochem. Sci, 26, pp. 421-425
  • Morelli, L., Llovera, R., Gonzalez, S.A., Affranchino, J.L., Prelli, F., Frangione, B., Ghiso, J., Castaño, E.M., (2003) J. Biol. Chem, 278, pp. 23221-23226
  • Morelli, L., Llovera, R.E., Alonso, L.G., Frangione, B., de Prat Gay, G., Ghiso, J., Castaño, E.M., (2005) Biochem. Biophys. Res. Commun, 332, pp. 808-816
  • Shen, Y., Joachimiak, A., Rosner, M.R., Tang, W.J., (2006) Nature, 443, pp. 870-887
  • Vepsalainen, S., Parkinson, M., Helisalmi, S., Mannermaa, A., Soininen, H., Tanzi, R., Bertram, L., Hiltunen, M., (2007) J. Med. Genet, 44, pp. 606-608
  • Qiu, W.Q., Folstein, M.F., (2006) Neurobiol. Aging, 27, pp. 190-198
  • Luchsinger, J.A., Tang, M.X., Shea, S., Mayeux, R., (2004) Neurology, 63, pp. 1187-1192
  • Pérez, A., Morelli, L., Cresto, J.C., Castaño, E.M., (2000) Neurochem. Res, 25, pp. 247-255
  • Cook, D.G., Leverenz, J.B., McMillan, P.J., Kulstad, J.J., Ericksen, S., Roth, R.A., Schellenberg, G.D., Craft, S., (2003) Am. J. Pathol, 162, pp. 313-319
  • Morelli, L., Llovera, R.E., Mathov, I., Lue, L., Frangione, B., Ghiso, J., Castaño, E.M., (2004) J. Biol. Chem, 279, pp. 56004-56013
  • Shinall, H., Song, E.S., Hersh, L.B., (2005) Biochemistry, 44, pp. 15345-15350
  • Caccamo, A., Oddo, S., Sugarman, M.C., Akbari, Y., LaFerla, F.M., (2005) Neurobiol. Aging, 26, pp. 645-654
  • Castaño, E.M., Prelli, F., Soto, C., Beavis, R., Matsubara, E., Shoji, M., Frangione, B., (1996) J. Biol. Chem, 271, pp. 32185-32191
  • Wood, S.J., Maleeff, B., Hart, T., Wetzel, R., (1996) J. Mol. Biol, 256, pp. 870-877
  • Saric, T., Muller, D., Seitz, H.J., Pavelic, K., (2003) Mol. Cell. Endocrinol, 204, pp. 11-20
  • Wisniewski, H.M., Wen, G.Y., Kim, K.S., (1989) Acta Neuropathol. (Berl.), 78, pp. 22-27
  • Harigaya, Y., Shoji, M., Kawarabayashi, T., Kanai, M., Nakamura, T., Iizuka, T., Igeta, Y., Hirai, S., (1995) Biochem. Biophys. Res. Commun, 211, pp. 1015-1022
  • Bernstein, H.G., Ansorge, S., Riederer, P., Reiser, M., Frolich, L., Bogerts, B., (1999) Neurosci. Lett, 263, pp. 161-164
  • Gorevic, P.D., Castaño, E.M., Sarma, R., Frangione, B., (1987) Biochem. Biophys. Res. Commun, 147, pp. 854-862
  • Liu, R., Yuan, B., Emadi, S., Zameer, A., Schulz, P., McAllister, C., Lyubchenko, Y., Sierks, M.R., (2004) Biochemistry, 43, pp. 6959-6967
  • Shii, K., Yokono, K., Baba, S., Roth, R.A., (1986) Diabetes, 35, pp. 675-683
  • Safavi, A., Miller, B.C., Cottam, L., Hersh, L.B., (1996) Biochemistry, 35, pp. 14318-14325
  • Strittmatter, W.J., Saunders, A.M., Schmechel, D., Pericak-Vance, M., Enghild, J., Salvesen, G.S., Roses, A.D., (1993) Proc. Natl. Acad. Sci. U. S. A, 90, pp. 1977-1981
  • Munson, G.W., Roher, A.E., Kuo, Y.M., Gilligan, S.M., Reardon, C.A., Getz, G.S., LaDu, M.J., (2000) Biochemistry, 39, pp. 16119-16124
  • Hughes, S.R., Khorkova, O., Goyal, S., Knaeblein, J., Heroux, J., Riedel, N.G., Sahasrabudhe, S., (1998) Proc. Natl. Acad. Sci. U. S. A, 95, pp. 3275-3280
  • Schwarzman, A.L., Gregori, L., Vitek, M.P., Lyubski, S., Strittmatter, W.J., Enghilde, J.J., Bhasin, R., Goldgaber, D., (1994) Proc. Natl. Acad. Sci. U. S. A, 91, pp. 8368-8372
  • Chauhan, V.P., Ray, I., Chauhan, A., Wisniewski, H.M., (1999) Biochem. Biophys. Res. Commun, 258, pp. 241-246
  • Wang, H.Y., Lee, D.H., D'Andrea, M.R., Peterson, P.A., Shank, R.P., Reitz, A.B., (2000) J. Biol. Chem, 275, pp. 5626-5632
  • Hilbich, C., Kisters-Woike, B., Reed, J., Masters, C.L., Beyreuther, K., (1992) J. Mol. Biol, 228, pp. 460-473
  • Soto, C., Sigurdsson, E.M., Morelli, L., Kumar, R.A., Castaño, E.M., Frangione, B., (1998) Nat. Med, 4, pp. 822-826
  • Zhang, S., Iwata, K., Lachenmann, M.J., Peng, J.W., Li, S., Stimson, E.R., Lu, Y., Lee, J.P., (2000) J. Struct. Biol, 130, pp. 130-141
  • Luhrs, T., Ritter, C., Adrian, M., Riek-Loher, D., Bohrmann, B., Dobeli, H., Schubert, D., Riek, R., (2005) Proc. Natl. Acad. Sci. U. S. A, 102, pp. 17342-17347
  • Lesne, S., Koh, M.T., Kotilinek, L., Kayed, R., Glabe, C.G., Yang, A., Gallagher, M., Ashe, K.H., (2006) Nature, 440, pp. 352-357
  • O'Nuallain, B., Williams, A.D., Westermark, P., Wetzel, R., (2004) J. Biol. Chem, 279, pp. 17490-17499
  • Auld, D.S., (2004) Handbook of Proteolytic Enzymes, pp. 268-289. , Barrett, A. J, Rawlings, N. D, and Woessner, J. F, eds pp, Elsevier Academic Press, New York
  • Makarova, K.S., Grishin, N.V., (1999) Protein Sci, 8, pp. 2537-2540
  • Oefner, C., D'Arcy, A., Hennig, M., Winkler, F.K., Dale, G.E., (2000) J. Mol. Biol, 296, pp. 341-349
  • Wang, R., Zhang, Y.W., Zhang, X., Liu, R., Zhang, X., Hong, S., Xia, K., Xu, H., (2006) FASEB J, 20, pp. 1275-1287
  • Leissring, M.A., Lu, A., Condron, M.M., Teplow, D.B., Stein, R.L., Farris, W., Selkoe, D.J., (2003) J. Biol. Chem, 278, pp. 37314-37320
  • O' Nuallain, B., Shivaprasad, S., Kheterpal, I., Wetzel, R., (2005) Biochemistry, 44, pp. 12709-12718
  • Chen, Y.R., Glabe, C.G., (2006) J. Biol. Chem, 281, pp. 24414-24422
  • Esch, F.S., Keim, P.S., Beattie, E.C., Blacher, R.W., Culwell, A.R., Oltersdorf, T., McClure, D., Ward, P.J., (1990) Science, 248, pp. 1122-1124
  • Gowing, E., Roher, A.E., Woods, A.S., Cotter, R.J., Chaney, M., Little, S.P., Ball, M.J., (1994) J. Biol. Chem, 269, pp. 10987-10990

Citas:

---------- APA ----------
Llovera, R.E., De Tullio, M., Alonso, L.G., Leissring, M.A., Kaufman, S.B., Roher, A.E., Gay, G.D.P.,..., Castaño, E.M. (2008) . The catalytic domain of insulin-degrading enzyme forms a denaturant-resistant complex with amyloid β peptide: Implications for Alzheimer disease pathogenesis. Journal of Biological Chemistry, 283(25), 17039-17048.
http://dx.doi.org/10.1074/jbc.M706316200
---------- CHICAGO ----------
Llovera, R.E., De Tullio, M., Alonso, L.G., Leissring, M.A., Kaufman, S.B., Roher, A.E., et al. "The catalytic domain of insulin-degrading enzyme forms a denaturant-resistant complex with amyloid β peptide: Implications for Alzheimer disease pathogenesis" . Journal of Biological Chemistry 283, no. 25 (2008) : 17039-17048.
http://dx.doi.org/10.1074/jbc.M706316200
---------- MLA ----------
Llovera, R.E., De Tullio, M., Alonso, L.G., Leissring, M.A., Kaufman, S.B., Roher, A.E., et al. "The catalytic domain of insulin-degrading enzyme forms a denaturant-resistant complex with amyloid β peptide: Implications for Alzheimer disease pathogenesis" . Journal of Biological Chemistry, vol. 283, no. 25, 2008, pp. 17039-17048.
http://dx.doi.org/10.1074/jbc.M706316200
---------- VANCOUVER ----------
Llovera, R.E., De Tullio, M., Alonso, L.G., Leissring, M.A., Kaufman, S.B., Roher, A.E., et al. The catalytic domain of insulin-degrading enzyme forms a denaturant-resistant complex with amyloid β peptide: Implications for Alzheimer disease pathogenesis. J. Biol. Chem. 2008;283(25):17039-17048.
http://dx.doi.org/10.1074/jbc.M706316200