메뉴 건너뛰기




Volumn 383, Issue 3, 2004, Pages 439-446

Alternative translation initiation generates a novel isoform of insulin-degrading enzyme targeted to mitochondria

Author keywords

Alzheimer's disease; Diabetes mellitus; Insulin degrading enzyme; Metallopeptidase; Mitochondrion

Indexed keywords

AMINO ACIDS; ELECTRON MICROSCOPY; INSULIN; PROTEINS; ZINC;

EID: 9144260111     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20041081     Document Type: Article
Times cited : (142)

References (53)
  • 1
    • 0031690490 scopus 로고    scopus 로고
    • Insulin degradation: Progress and potential
    • Duckworth, W. C., Bennett, R. G. and Hamel, F. G. (1998) Insulin degradation: progress and potential. Endocr. Rev. 19, 608-624
    • (1998) Endocr. Rev. , vol.19 , pp. 608-624
    • Duckworth, W.C.1    Bennett, R.G.2    Hamel, F.G.3
  • 2
    • 1842367306 scopus 로고    scopus 로고
    • Degradation of amyloid β-protein by a metalloprotease secreted by microglia and other neural and non-neural cells
    • Qiu, W. Q., Ye, Z., Kholodenko, D., Seubert, P. and Selkoe, D. J. (1997) Degradation of amyloid β-protein by a metalloprotease secreted by microglia and other neural and non-neural cells. J. Biol. Chem. 272, 6641-6646
    • (1997) J. Biol. Chem. , vol.272 , pp. 6641-6646
    • Qiu, W.Q.1    Ye, Z.2    Kholodenko, D.3    Seubert, P.4    Selkoe, D.J.5
  • 3
    • 0031550507 scopus 로고    scopus 로고
    • Overexpression of insulin degrading enzyme: Cellular localization and effects on insulin signaling
    • Seta, K. A. and Roth, R. A. (1997) Overexpression of insulin degrading enzyme: cellular localization and effects on insulin signaling. Biochem. Biophys. Res. Commun. 231, 167-171
    • (1997) Biochem. Biophys. Res. Commun. , vol.231 , pp. 167-171
    • Seta, K.A.1    Roth, R.A.2
  • 4
    • 0034161516 scopus 로고    scopus 로고
    • Neurons regulate extracellular levels of amyloid β-protein via proteolysis by insulin-degrading enzyme
    • Vekrellis, K., Ye, Z., Qiu, W. Q., Walsh, D., Hartley, D., Chesneau, V., Rosner, M. R. and Selkoe, D. J. (2000) Neurons regulate extracellular levels of amyloid β-protein via proteolysis by insulin-degrading enzyme. J. Neurosci. 20, 1657-1665
    • (2000) J. Neurosci. , vol.20 , pp. 1657-1665
    • Vekrellis, K.1    Ye, Z.2    Qiu, W.Q.3    Walsh, D.4    Hartley, D.5    Chesneau, V.6    Rosner, M.R.7    Selkoe, D.J.8
  • 5
    • 0030787591 scopus 로고    scopus 로고
    • Insulin-degrading enzyme does not require peroxisomal localization for insulin degradation
    • Chesneau, V., Perlman, R. K., Li, W., Keller, G. A. and Rosner, M. R. (1997) Insulin-degrading enzyme does not require peroxisomal localization for insulin degradation. Endocrinology 138, 3444-3451
    • (1997) Endocrinology , vol.138 , pp. 3444-3451
    • Chesneau, V.1    Perlman, R.K.2    Li, W.3    Keller, G.A.4    Rosner, M.R.5
  • 6
    • 0028176821 scopus 로고
    • Alzheimer's β-amyloid peptide specifically interacts with and is degraded by insulin degrading enzyme
    • Kurochkin, I. V. and Goto, S. (1994) Alzheimer's β-amyloid peptide specifically interacts with and is degraded by insulin degrading enzyme. FEBS Lett. 345, 33-37
    • (1994) FEBS Lett. , vol.345 , pp. 33-37
    • Kurochkin, I.V.1    Goto, S.2
  • 7
    • 0031044352 scopus 로고    scopus 로고
    • Degradation of Alzheimer's β-amyloid protein by human and rat brain peptidases: Involvement of insulin-degrading enzyme
    • McDermott, J. R. and Gibson, A. M. (1997) Degradation of Alzheimer's β-amyloid protein by human and rat brain peptidases: involvement of insulin-degrading enzyme. Neurochem. Res. 22, 49-56
    • (1997) Neurochem. Res. , vol.22 , pp. 49-56
    • McDermott, J.R.1    Gibson, A.M.2
  • 11
    • 0346101885 scopus 로고    scopus 로고
    • Enhanced proteolysis of β-amyloid in APP transgenic mice prevents plaque formation, secondary pathology, and premature death
    • Leissring, M. A., Farris, W., Chang, A. Y., Walsh, D. M., Wu, X., Sun, X., Frosch, M. P. and Selkoe, D. J. (2003) Enhanced proteolysis of β-amyloid in APP transgenic mice prevents plaque formation, secondary pathology, and premature death. Neuron 40, 1087-1093
    • (2003) Neuron , vol.40 , pp. 1087-1093
    • Leissring, M.A.1    Farris, W.2    Chang, A.Y.3    Walsh, D.M.4    Wu, X.5    Sun, X.6    Frosch, M.P.7    Selkoe, D.J.8
  • 14
    • 0038519618 scopus 로고    scopus 로고
    • Insulin degrading enzyme (IDE) genetic variants and risk of Alzheimer's disease: Evidence of effect modification by apolipoprotein E (APOE)
    • Edland, S. D., Wavrant-De Vriese, F., Compton, D., Smith, G. E., Ivnik, R., Boeve, B. F., Tangalos, E. G. and Petersen, R. C. (2003) Insulin degrading enzyme (IDE) genetic variants and risk of Alzheimer's disease: evidence of effect modification by apolipoprotein E (APOE). Neurosci. Lett. 345, 21-24
    • (2003) Neurosci. Lett. , vol.345 , pp. 21-24
    • Edland, S.D.1    Wavrant-De Vriese, F.2    Compton, D.3    Smith, G.E.4    Ivnik, R.5    Boeve, B.F.6    Tangalos, E.G.7    Petersen, R.C.8
  • 15
  • 16
    • 0033764737 scopus 로고    scopus 로고
    • The Finland-United States investigation of non-insulin-dependent diabetes mellitus genetics (FUSION) study. I. An autosomal genome scan for genes that predispose to type 2 diabetes
    • Ghosh, S., Watanabe, R. M., Valle, T. T., Hauser, E. R., Magnuson, V. L., Langefeld, C. D., Ally, D. S., Mohlke, K. L., Silander, K., Kohtamaki, K. et al. (2000) The Finland-United States investigation of non-insulin-dependent diabetes mellitus genetics (FUSION) study. I. An autosomal genome scan for genes that predispose to type 2 diabetes. Am. J. Hum. Genet 67, 1174-1185
    • (2000) Am. J. Hum. Genet. , vol.67 , pp. 1174-1185
    • Ghosh, S.1    Watanabe, R.M.2    Valle, T.T.3    Hauser, E.R.4    Magnuson, V.L.5    Langefeld, C.D.6    Ally, D.S.7    Mohlke, K.L.8    Silander, K.9    Kohtamaki, K.10
  • 21
    • 0027991714 scopus 로고
    • Hyperinsulinaemia and Alzheimer's disease
    • Razay, G. and Wilcock, G. K. (1994) Hyperinsulinaemia and Alzheimer's disease. Age Ageing 23, 396-399
    • (1994) Age Ageing , vol.23 , pp. 396-399
    • Razay, G.1    Wilcock, G.K.2
  • 23
    • 0017066391 scopus 로고
    • Production of spontaneous diabetic rats by repetition of selective breeding
    • Goto, Y., Kakizaki, M. and Masaki, N. (1976) Production of spontaneous diabetic rats by repetition of selective breeding. Tohoku J. Exp. Med. 119, 85-90
    • (1976) Tohoku J. Exp. Med. , vol.119 , pp. 85-90
    • Goto, Y.1    Kakizaki, M.2    Masaki, N.3
  • 25
    • 1642290835 scopus 로고    scopus 로고
    • Partial loss-of-function mutations in insulin-degrading enzyme that induce diabetes also impair degradation of amyloid β-protein
    • Farris, W., Mansourian, S., Leissring, M. A., Eckman, E. A., Bertram, L., Eckman, C., Tanzi, R. E. and Selkoe, D. J. (2004) Partial loss-of-function mutations in insulin-degrading enzyme that induce diabetes also impair degradation of amyloid β-protein. Am. J. Pathol. 164, 1424-1434
    • (2004) Am. J. Pathol. , vol.164 , pp. 1424-1434
    • Farris, W.1    Mansourian, S.2    Leissring, M.A.3    Eckman, E.A.4    Bertram, L.5    Eckman, C.6    Tanzi, R.E.7    Selkoe, D.J.8
  • 27
    • 0023245015 scopus 로고
    • The human pyruvate dehydrogenase complex. Isolation of cDNA clones for the E1α subunit, sequence analysis, and characterization of the mRNA
    • Dahl, H. H., Hunt, S. M., Hutchison, W. M. and Brown, G. K. (1987) The human pyruvate dehydrogenase complex. Isolation of cDNA clones for the E1α subunit, sequence analysis, and characterization of the mRNA. J. Biol. Chem. 262, 7398-7403
    • (1987) J. Biol. Chem. , vol.262 , pp. 7398-7403
    • Dahl, H.H.1    Hunt, S.M.2    Hutchison, W.M.3    Brown, G.K.4
  • 28
    • 0028587344 scopus 로고
    • Identification of zinc ligands of the insulin-degrading enzyme
    • Perlman, R. K. and Rosner, M. R. (1994) Identification of zinc ligands of the insulin-degrading enzyme. J. Biol. Chem. 269, 33140-33145
    • (1994) J. Biol. Chem. , vol.269 , pp. 33140-33145
    • Perlman, R.K.1    Rosner, M.R.2
  • 29
    • 0034045482 scopus 로고    scopus 로고
    • Functional human insulin-degrading enzyme can be expressed in bacteria
    • Chesneau, V. and Rosner, M. R. (2000) Functional human insulin-degrading enzyme can be expressed in bacteria. Protein Expr. Purif. 19, 91-98
    • (2000) Protein Expr. Purif. , vol.19 , pp. 91-98
    • Chesneau, V.1    Rosner, M.R.2
  • 30
    • 0022552131 scopus 로고
    • Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes
    • Kozak, M. (1986) Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes. Cell 44, 283-292
    • (1986) Cell , vol.44 , pp. 283-292
    • Kozak, M.1
  • 31
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen, H., Engelbrecht, J., Brunak, S. and von Heijne, G. (1997) Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng. 10, 1-6
    • (1997) Protein Eng. , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    Von Heijne, G.4
  • 32
    • 0032972509 scopus 로고    scopus 로고
    • PSORT: A program for detecting sorting signals in proteins and predicting their subcellular localization
    • Nakai, K. and Horton, P. (1999) PSORT: a program for detecting sorting signals in proteins and predicting their subcellular localization. Trends Biochem. Sci. 24, 34-36
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 34-36
    • Nakai, K.1    Horton, P.2
  • 33
    • 0029915525 scopus 로고    scopus 로고
    • Computational method to predict mitochondrially imported proteins and their targeting sequences
    • Claros, M. G. and Vincens, P. (1996) Computational method to predict mitochondrially imported proteins and their targeting sequences. Eur. J. Biochem. 241, 779-786
    • (1996) Eur. J. Biochem. , vol.241 , pp. 779-786
    • Claros, M.G.1    Vincens, P.2
  • 34
    • 0034697980 scopus 로고    scopus 로고
    • Predicting subcellular localization of proteins based on their N-terminal amino acid sequence
    • Emanuelsson, O., Nielsen, H., Brunak, S. and von Heijne, G. (2000) Predicting subcellular localization of proteins based on their N-terminal amino acid sequence. J. Mol. Biol. 300, 1005-1016
    • (2000) J. Mol. Biol. , vol.300 , pp. 1005-1016
    • Emanuelsson, O.1    Nielsen, H.2    Brunak, S.3    Von Heijne, G.4
  • 36
    • 0036828801 scopus 로고    scopus 로고
    • Isolation and identification of a novel mitochondrial metalloprotease (PreP) that degrades targeting presequences in plants
    • Stahl, A., Moberg, P., Ytterberg, J., Panfilov, O., Brockenhuus Von Lowenhielm, H., Nilsson, F. and Glaser, E. (2002) Isolation and identification of a novel mitochondrial metalloprotease (PreP) that degrades targeting presequences in plants. J. Biol. Chem. 277, 41931-41939
    • (2002) J. Biol. Chem. , vol.277 , pp. 41931-41939
    • Stahl, A.1    Moberg, P.2    Ytterberg, J.3    Panfilov, O.4    Brockenhuus Von Lowenhielm, H.5    Nilsson, F.6    Glaser, E.7
  • 38
    • 0034551718 scopus 로고    scopus 로고
    • Insulysin hydrolyzes amyloid beta peptides to products that are neither neurotoxic nor deposit on amyloid plaques
    • Mukherjee, A., Song, E., Kihiko-Ehmann, M., Goodman, Jr, J. P., Pyrek, J. S., Estus, S. and Hersh, L. B. (2000) Insulysin hydrolyzes amyloid beta peptides to products that are neither neurotoxic nor deposit on amyloid plaques. J. Neurosci. 20, 8745-8749
    • (2000) J. Neurosci. , vol.20 , pp. 8745-8749
    • Mukherjee, A.1    Song, E.2    Kihiko-Ehmann, M.3    Goodman Jr., J.P.4    Pyrek, J.S.5    Estus, S.6    Hersh, L.B.7
  • 39
    • 0141621234 scopus 로고    scopus 로고
    • Kinetics of amyloid β-protein degradation determined by novel fluorescence- and fluorescence polarization-based assays
    • Leissring, M. A., Lu, A., Condron, M. M., Teplow, D. B., Stein, R. L., Farris, W. and Selkoe, D. J. (2003) Kinetics of amyloid β-protein degradation determined by novel fluorescence- and fluorescence polarization-based assays. J. Biol. Chem. 278, 37314-37320
    • (2003) J. Biol. Chem. , vol.278 , pp. 37314-37320
    • Leissring, M.A.1    Lu, A.2    Condron, M.M.3    Teplow, D.B.4    Stein, R.L.5    Farris, W.6    Selkoe, D.J.7
  • 40
    • 0030950637 scopus 로고    scopus 로고
    • Targeting of endopeptidase 24.16 to different subcellular compartments by alternative promoter usage
    • Kato, A., Sugiura, N., Saruta, Y., Hosoiri, T., Yasue, H. and Hirose, S. (1997) Targeting of endopeptidase 24.16 to different subcellular compartments by alternative promoter usage. J. Biol. Chem. 272, 15313-15322
    • (1997) J. Biol. Chem. , vol.272 , pp. 15313-15322
    • Kato, A.1    Sugiura, N.2    Saruta, Y.3    Hosoiri, T.4    Yasue, H.5    Hirose, S.6
  • 41
    • 0035824654 scopus 로고    scopus 로고
    • Mitochondrial and cytosolic isoforms of yeast fumarase are derivatives of a single translation product and have identical amino termini
    • Sass, E., Blachinsky, E., Karniely, S. and Pines, O. (2001) Mitochondrial and cytosolic isoforms of yeast fumarase are derivatives of a single translation product and have identical amino termini. J. Biol. Chem. 276, 46111-46117
    • (2001) J. Biol. Chem. , vol.276 , pp. 46111-46117
    • Sass, E.1    Blachinsky, E.2    Karniely, S.3    Pines, O.4
  • 42
    • 0036797556 scopus 로고    scopus 로고
    • The metalloendopeptidase nardilysin (NRDc) is potently inhibited by heparin-binding epidermal growth factor-like growth factor (HB-EGF)
    • Hospital, V., Nishi, E., Klagsbrun, M., Cohen, P., Seidah, N. G. and Prat, A. (2002) The metalloendopeptidase nardilysin (NRDc) is potently inhibited by heparin-binding epidermal growth factor-like growth factor (HB-EGF). Biochem. J. 367, 229-238
    • (2002) Biochem. J. , vol.367 , pp. 229-238
    • Hospital, V.1    Nishi, E.2    Klagsbrun, M.3    Cohen, P.4    Seidah, N.G.5    Prat, A.6
  • 43
    • 0028030514 scopus 로고
    • N-arginine dibasic convertase (NRD convertase): A newcomer to the family of processing endopeptidases. An overview
    • Chesneau, V., Pierotti, A. R., Prat, A., Gaudoux, F., Foulon, T. and Cohen, P. (1994) N-arginine dibasic convertase (NRD convertase): a newcomer to the family of processing endopeptidases. An overview. Biochimie 76, 234-240
    • (1994) Biochimie , vol.76 , pp. 234-240
    • Chesneau, V.1    Pierotti, A.R.2    Prat, A.3    Gaudoux, F.4    Foulon, T.5    Cohen, P.6
  • 44
    • 0022576497 scopus 로고
    • A metalloprotease involved in the processing of mitochondrial precursor proteins
    • Miura, S., Amaya, Y. and Mori, M. (1986) A metalloprotease involved in the processing of mitochondrial precursor proteins. Biochem. Biophys. Res. Commun. 134, 1151-1159
    • (1986) Biochem. Biophys. Res. Commun. , vol.134 , pp. 1151-1159
    • Miura, S.1    Amaya, Y.2    Mori, M.3
  • 45
    • 0030867866 scopus 로고    scopus 로고
    • Crystal structure of the cytochrome bc1 complex from bovine heart mitochondria
    • Xia, D., Yu, C. A., Kim, H., Xia, J. Z., Kachurin, A. M., Zhang, L., Yu, L. and Deisenhofer, J. (1997) Crystal structure of the cytochrome bc1 complex from bovine heart mitochondria. Science 277, 60-66
    • (1997) Science , vol.277 , pp. 60-66
    • Xia, D.1    Yu, C.A.2    Kim, H.3    Xia, J.Z.4    Kachurin, A.M.5    Zhang, L.6    Yu, L.7    Deisenhofer, J.8
  • 46
    • 0031763979 scopus 로고    scopus 로고
    • Regulation of multicatalytic enzyme activity by insulin and the insulin-degrading enzyme
    • Hamel, F. G., Bennett, R. G. and Duckworth, W. C. (1998) Regulation of multicatalytic enzyme activity by insulin and the insulin-degrading enzyme. Endocrinology 139, 4061-4066
    • (1998) Endocrinology , vol.139 , pp. 4061-4066
    • Hamel, F.G.1    Bennett, R.G.2    Duckworth, W.C.3
  • 47
    • 0027983795 scopus 로고
    • Androgen and glucocorticoid receptors interact with insulin degrading enzyme
    • Kupfer, S. R., Wilson, E. M. and French, F. S. (1994) Androgen and glucocorticoid receptors interact with insulin degrading enzyme. J. Biol. Chem. 269, 20622-20628
    • (1994) J. Biol. Chem. , vol.269 , pp. 20622-20628
    • Kupfer, S.R.1    Wilson, E.M.2    French, F.S.3
  • 48
    • 0028879135 scopus 로고
    • Role of yeast insulin-degrading enzyme homologs in propheromone processing and bud site selection
    • Adames, N., Blundell, K., Ashby, M. N. and Boone, C. (1995) Role of yeast insulin-degrading enzyme homologs in propheromone processing and bud site selection. Science 270, 464-467
    • (1995) Science , vol.270 , pp. 464-467
    • Adames, N.1    Blundell, K.2    Ashby, M.N.3    Boone, C.4
  • 49
    • 0022260057 scopus 로고
    • Arginine in the leader peptide is required for both import and proteolytic cleavage of a mitochondrial precursor
    • Horwich, A. L., Kalousek, F. and Rosenberg, L. E. (1985) Arginine in the leader peptide is required for both import and proteolytic cleavage of a mitochondrial precursor. Proc. Natl. Acad. Sci. U.S.A. 82, 4930-4933
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 4930-4933
    • Horwich, A.L.1    Kalousek, F.2    Rosenberg, L.E.3
  • 50
    • 0038321341 scopus 로고    scopus 로고
    • Increased vulnerability of brain mitochondria in diabetic (Goto-Kakizaki) rats with aging and amyloid-β exposure
    • Moreira, P. I., Santos, M. S., Moreno, A. M., Seica, R. and Oliveira, C. R. (2003) Increased vulnerability of brain mitochondria in diabetic (Goto-Kakizaki) rats with aging and amyloid-β exposure. Diabetes 52, 1449-1456
    • (2003) Diabetes , vol.52 , pp. 1449-1456
    • Moreira, P.I.1    Santos, M.S.2    Moreno, A.M.3    Seica, R.4    Oliveira, C.R.5
  • 51
    • 0036865991 scopus 로고    scopus 로고
    • Mitochondria as the conductor of metabolic signals tor insulin exocytosis in pancreatic β-cells
    • Maechler, P. (2002) Mitochondria as the conductor of metabolic signals tor insulin exocytosis in pancreatic β-cells. Cell Mol. Lite Sci. 59, 1803-1818
    • (2002) Cell Mol. Lite Sci. , vol.59 , pp. 1803-1818
    • Maechler, P.1
  • 52
    • 1642377274 scopus 로고    scopus 로고
    • Impaired mitochondrial activity in the insulin-resistant offspring of patients with type 2 diabetes
    • Petersen, K. F., Dufour, S., Befroy, D., Garcia, R. and Shulman, G. I. (2004) Impaired mitochondrial activity in the insulin-resistant offspring of patients with type 2 diabetes. N. Engl. J. Med. 350, 664-671
    • (2004) N. Engl. J. Med. , vol.350 , pp. 664-671
    • Petersen, K.F.1    Dufour, S.2    Befroy, D.3    Garcia, R.4    Shulman, G.I.5
  • 53
    • 18744431459 scopus 로고    scopus 로고
    • Mitochondrial control of neuron death and its role in neurodegenerative disorders
    • Jordan, J., Cena, V. and Prehn, J. H. (2003) Mitochondrial control of neuron death and its role in neurodegenerative disorders. J. Physiol. Biochem. 59, 129-141
    • (2003) J. Physiol. Biochem. , vol.59 , pp. 129-141
    • Jordan, J.1    Cena, V.2    Prehn, J.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.