메뉴 건너뛰기




Volumn 16, Issue 20, 1996, Pages 6331-6341

Immunohistochemical distribution and electron microscopic subcellular localization of the proteasome in the rat CNS

Author keywords

CNS; immunoelectron microscopy; immunohistochemistry; multicatalytic proteinase; prosome; proteasome; rat

Indexed keywords

PROTEASOME; PROTEINASE; REGULATOR PROTEIN; TRANSCRIPTION FACTOR;

EID: 0029815028     PISSN: 02706474     EISSN: None     Source Type: Journal    
DOI: 10.1523/jneurosci.16-20-06331.1996     Document Type: Article
Times cited : (85)

References (40)
  • 1
    • 0028287522 scopus 로고
    • Antibodies against the C2 COOH-terminal region discriminate the active and latent forms of the multicatalytic proteinase complex
    • Arribas J, Arizti P, Castaño JG (1994) Antibodies against the C2 COOH-terminal region discriminate the active and latent forms of the multicatalytic proteinase complex. J Biol Chem 269:12858-12864.
    • (1994) J Biol Chem , vol.269 , pp. 12858-12864
    • Arribas, J.1    Arizti, P.2    Castaño, J.G.3
  • 2
    • 0025128190 scopus 로고
    • Kinetic studies of the differential effect of detergents on the peptidase activities of the multicatalytic proteinase from rat liver
    • Arribas J, Castaño JG (1990) Kinetic studies of the differential effect of detergents on the peptidase activities of the multicatalytic proteinase from rat liver. J Biol Chem 265:13969-13973.
    • (1990) J Biol Chem , vol.265 , pp. 13969-13973
    • Arribas, J.1    Castaño, J.G.2
  • 3
    • 0026011789 scopus 로고
    • Autoantibodies against the multicatalytic proteinase in patients with systemic lupus erythematosus
    • Arribas J, Luz-Rodriguez M, Alvarez-Do-Forno R, Castaño JG (1991) Autoantibodies against the multicatalytic proteinase in patients with systemic lupus erythematosus. J Exp Med 173:423-427.
    • (1991) J Exp Med , vol.173 , pp. 423-427
    • Arribas, J.1    Luz-Rodriguez, M.2    Alvarez-Do-Forno, R.3    Castaño, J.G.4
  • 4
    • 0027707099 scopus 로고
    • Modulation of the multicatalytic proteinase complex by lipids, interconversion and proteolytic processing
    • Arizti P, Arribas J, Castaño J G (1993) Modulation of the multicatalytic proteinase complex by lipids, interconversion and proteolytic processing. Enzyme Protein 47:285-295.
    • (1993) Enzyme Protein , vol.47 , pp. 285-295
    • Arizti, P.1    Arribas, J.2    Castaño, J.G.3
  • 5
    • 0028799949 scopus 로고
    • Persistent activation of cAMP dependent protein kinase by regulated proteolysis suggests a neuron-specific function of the ubiquitin system in Aplysia
    • Chain DG, Hegde AN, Yamamoto N, Liu-Marsh B, Schwartz JH (1995) Persistent activation of cAMP dependent protein kinase by regulated proteolysis suggests a neuron-specific function of the ubiquitin system in Aplysia. J Neurosci 15:7592-7603.
    • (1995) J Neurosci , vol.15 , pp. 7592-7603
    • Chain, D.G.1    Hegde, A.N.2    Yamamoto, N.3    Liu-Marsh, B.4    Schwartz, J.H.5
  • 6
    • 0029146930 scopus 로고
    • Signal-induced site-specific phosphorylation targets I kappa B alpha to the ubiquitin-proteasome pathway
    • Chen Z, Hagler J, Palombella VJ, Melandri F, Scherer D, Ballard D, Maniatis T (1995) Signal-induced site-specific phosphorylation targets I kappa B alpha to the ubiquitin-proteasome pathway. Genes Dev 9:1586-1597.
    • (1995) Genes Dev , vol.9 , pp. 1586-1597
    • Chen, Z.1    Hagler, J.2    Palombella, V.J.3    Melandri, F.4    Scherer, D.5    Ballard, D.6    Maniatis, T.7
  • 7
    • 0028018268 scopus 로고
    • The ubiquitin-proteasome proteolytic pathway
    • Ciechanover A (1994) The ubiquitin-proteasome proteolytic pathway. Cell 79:13-21.
    • (1994) Cell , vol.79 , pp. 13-21
    • Ciechanover, A.1
  • 8
    • 0028276554 scopus 로고
    • Degradation of the tumor suppressor protein p53 by the ubiquitin-mediated proteolytic system requires a novel species of ubiquitin-carrier protein, E2
    • Ciechanover A, Shkedy D, Oren M, Bercovich (1994) Degradation of the tumor suppressor protein p53 by the ubiquitin-mediated proteolytic system requires a novel species of ubiquitin-carrier protein, E2. J Biol Chem 269:9582-9589.
    • (1994) J Biol Chem , vol.269 , pp. 9582-9589
    • Ciechanover, A.1    Shkedy, D.2    Oren, M.3    Bercovich4
  • 9
    • 0029033981 scopus 로고
    • Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin
    • Fenteany G, Standaert RF, Lane WS, Choi S, Corey EJ, Schreiber SL (1995) Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin. Science 268:726-731.
    • (1995) Science , vol.268 , pp. 726-731
    • Fenteany, G.1    Standaert, R.F.2    Lane, W.S.3    Choi, S.4    Corey, E.J.5    Schreiber, S.L.6
  • 10
    • 0028180516 scopus 로고
    • A beta-lactone related to lactacystin induces neurite outgrowth in a neuroblastoma cell line and inhibits cell cycle progression in an osteosarcoma cell line
    • Fenteany G, Standaert RF, Reichard GA, Corey FJ, Schreiber SL (1994) A beta-lactone related to lactacystin induces neurite outgrowth in a neuroblastoma cell line and inhibits cell cycle progression in an osteosarcoma cell line. Proc Natl Acad Sci USA 91:3358-3362.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 3358-3362
    • Fenteany, G.1    Standaert, R.F.2    Reichard, G.A.3    Corey, F.J.4    Schreiber, S.L.5
  • 11
    • 0028293250 scopus 로고
    • Comparison of the effect of calpain inhibitors on two extralysosomal proteinases: The multicatalytic proteinase complex and m-calpain
    • Figueiredo-Pereira ME, Banik N, Wilk S (1994) Comparison of the effect of calpain inhibitors on two extralysosomal proteinases: the multicatalytic proteinase complex and m-calpain. J Neurochem 62:1989-1994.
    • (1994) J Neurochem , vol.62 , pp. 1989-1994
    • Figueiredo-Pereira, M.E.1    Banik, N.2    Wilk, S.3
  • 12
    • 0025601637 scopus 로고
    • Immunohistochemical distribution of calcium-activated neutral proteinases and endogeneous CANP inhibitor in the rabbit hippocampus
    • Fukuda T, Adachi E, Kawashima S, Yoshiya I, Hashimoto PH (1990) Immunohistochemical distribution of calcium-activated neutral proteinases and endogeneous CANP inhibitor in the rabbit hippocampus. J Comp Neurol 302:100-109.
    • (1990) J Comp Neurol , vol.302 , pp. 100-109
    • Fukuda, T.1    Adachi, E.2    Kawashima, S.3    Yoshiya, I.4    Hashimoto, P.H.5
  • 13
    • 0028108923 scopus 로고
    • CREB: A mediator of long-term memory from mollusks to mammals
    • Frank DA, Greenberg ME (1994) CREB: a mediator of long-term memory from mollusks to mammals. Cell 79:5-8.
    • (1994) Cell , vol.79 , pp. 5-8
    • Frank, D.A.1    Greenberg, M.E.2
  • 15
    • 0014979739 scopus 로고
    • Distribution of acetyl cholinesterase in the hippocampal region of the guinea pig. I. Entorhinal area, parasubiculum and presubiculum
    • Geneser-Jensen FA, Blackstad TW (1971) Distribution of acetyl cholinesterase in the hippocampal region of the guinea pig. I. Entorhinal area, parasubiculum and presubiculum. Z Zellforsch Mikrosk Anat 114:460-481.
    • (1971) Z Zellforsch Mikrosk Anat , vol.114 , pp. 460-481
    • Geneser-Jensen, F.A.1    Blackstad, T.W.2
  • 16
  • 17
    • 0027304239 scopus 로고
    • Regulatory subunits of cAMP-dependent protein kinase are degraded after conjugation to ubiquitin: A molecular mechanism underlying long-term synaptic plasticity
    • Hegde AN, Goldberg A, Schwartz JH (1993) Regulatory subunits of cAMP-dependent protein kinase are degraded after conjugation to ubiquitin: a molecular mechanism underlying long-term synaptic plasticity. Proc Natl Acad Sci USA 90:7436-7440.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 7436-7440
    • Hegde, A.N.1    Goldberg, A.2    Schwartz, J.H.3
  • 18
    • 0028109918 scopus 로고
    • PRE5 and PRE6, the last missing genes encoding 20S proteasome subunits from yeast? Indication for a set of 14 different subunits in the eukaryotic proteasome core
    • Heinemeyer W, Trondle N, Albrecht G, Wolf DH (1994) PRE5 and PRE6, the last missing genes encoding 20S proteasome subunits from yeast? Indication for a set of 14 different subunits in the eukaryotic proteasome core. Biochemistry 33:12229-12237.
    • (1994) Biochemistry , vol.33 , pp. 12229-12237
    • Heinemeyer, W.1    Trondle, N.2    Albrecht, G.3    Wolf, D.H.4
  • 19
    • 0028935165 scopus 로고
    • Ubiquitin, proteasomes, and the regulation of intracellular protein degradation
    • Hochstrasser M (1995) Ubiquitin, proteasomes, and the regulation of intracellular protein degradation. Curr Opin Cell Biol 7:215-223.
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 215-223
    • Hochstrasser, M.1
  • 20
    • 0029068172 scopus 로고
    • Ubiquitinylation is not an absolute requirement for degradation of c-Jun protein by the 26 S proteasome
    • Jariel-Encontre I, Pariat M, Martin F, Carillo S, Salvat C, Piechaczyk M (1995) Ubiquitinylation is not an absolute requirement for degradation of c-Jun protein by the 26 S proteasome. J Biol Chem 270:11623-11627.
    • (1995) J Biol Chem , vol.270 , pp. 11623-11627
    • Jariel-Encontre, I.1    Pariat, M.2    Martin, F.3    Carillo, S.4    Salvat, C.5    Piechaczyk, M.6
  • 21
    • 0023692734 scopus 로고
    • Localization of ingensin in rat central nervous system and skeletal muscle
    • Kamakura K, Ishiura S, Nonaka I, Sugita H (1988) Localization of ingensin in rat central nervous system and skeletal muscle. J Neurosci Res 20:473-478.
    • (1988) J Neurosci Res , vol.20 , pp. 473-478
    • Kamakura, K.1    Ishiura, S.2    Nonaka, I.3    Sugita, H.4
  • 22
    • 0029046441 scopus 로고
    • The neuritogenesis inducer lactacystin arrests cell cycle at both G0/G1 and G2 phases in neuro 2a cells
    • Tokyo
    • Katagiri M, Hayashi M, Matsuzaki K, Tanaka H, Omura S (1995) The neuritogenesis inducer lactacystin arrests cell cycle at both G0/G1 and G2 phases in neuro 2a cells. J Antibiol (Tokyo) 48:344-346.
    • (1995) J Antibiol , vol.48 , pp. 344-346
    • Katagiri, M.1    Hayashi, M.2    Matsuzaki, K.3    Tanaka, H.4    Omura, S.5
  • 23
    • 0025760931 scopus 로고
    • Multicatalytic proteinase is present in Lewy bodies and neurofibrillary tangles in diffuse Lewy body disease brains
    • Kwak S, Masaki T, Ishiura S, Sugita H (1991) Multicatalytic proteinase is present in Lewy bodies and neurofibrillary tangles in diffuse Lewy body disease brains. Neurosci Lett 128:21-24.
    • (1991) Neurosci Lett , vol.128 , pp. 21-24
    • Kwak, S.1    Masaki, T.2    Ishiura, S.3    Sugita, H.4
  • 25
    • 0029042511 scopus 로고
    • Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 a resolution
    • Lowe J, Stock D, Jap B, Zwickl P, Baumeister W, Huber R (1995) Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution [see comments]. Science 268:533-539.
    • (1995) Science , vol.268 , pp. 533-539
    • Lowe, J.1    Stock, D.2    Jap, B.3    Zwickl, P.4    Baumeister, W.5    Huber, R.6
  • 26
    • 0028944691 scopus 로고
    • Changes in immunocytochemical detectability of proteasome epitopes depending on cell growth and fixation conditions of lung cancer cell lines
    • Machiels BM, Henfling ME, Broers JL, Hendil KB, Ramekers FC (1995) Changes in immunocytochemical detectability of proteasome epitopes depending on cell growth and fixation conditions of lung cancer cell lines. Eur J Cell Biol 66:282-292.
    • (1995) Eur J Cell Biol , vol.66 , pp. 282-292
    • Machiels, B.M.1    Henfling, M.E.2    Broers, J.L.3    Hendil, K.B.4    Ramekers, F.C.5
  • 27
    • 0028297514 scopus 로고
    • Multicatalytic proteinase is associated with characteristic oval structures in cortical Lewy bodies: An immunocytochemical study with light and electron microscopy
    • Masaki T, Ishiura S, Sugita H, Kwak S (1994) Multicatalytic proteinase is associated with characteristic oval structures in cortical Lewy bodies: an immunocytochemical study with light and electron microscopy. J Neurol Sci 122:127-134.
    • (1994) J Neurol Sci , vol.122 , pp. 127-134
    • Masaki, T.1    Ishiura, S.2    Sugita, H.3    Kwak, S.4
  • 28
    • 0028267689 scopus 로고
    • Cytolocation of prosome antigens on intermediate filament subnetworks of cytokeratin, vimentin and desmin type
    • Olink-Coux M, Arcangeletti C, Pinardi F, Minisini R, Huesca M, Chezzi C, Scherrer K (1994) Cytolocation of prosome antigens on intermediate filament subnetworks of cytokeratin, vimentin and desmin type. J Cell Sci 107:353-366.
    • (1994) J Cell Sci , vol.107 , pp. 353-366
    • Olink-Coux, M.1    Arcangeletti, C.2    Pinardi, F.3    Minisini, R.4    Huesca, M.5    Chezzi, C.6    Scherrer, K.7
  • 29
    • 0025123346 scopus 로고
    • The multicatalytic proteinase complex, a major extralysosomal proteolytic system
    • Orlowski M (1990) The multicatalytic proteinase complex, a major extralysosomal proteolytic system. Biochemistry 29:10289-10297.
    • (1990) Biochemistry , vol.29 , pp. 10289-10297
    • Orlowski, M.1
  • 30
    • 0027980321 scopus 로고
    • The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B
    • Palombella VJ, Rando OJ, Goldberg AL, Maniatis T (1994) The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B. Cell 78:773-785.
    • (1994) Cell , vol.78 , pp. 773-785
    • Palombella, V.J.1    Rando, O.J.2    Goldberg, A.L.3    Maniatis, T.4
  • 32
    • 0025285178 scopus 로고
    • Distribution of calcium-activated protease calpain in the rat brain
    • Perlmutter LS, Gall C, Baudry M, Lynch G (1990) Distribution of calcium-activated protease calpain in the rat brain. J Comp Neurol 296:269-276.
    • (1990) J Comp Neurol , vol.296 , pp. 269-276
    • Perlmutter, L.S.1    Gall, C.2    Baudry, M.3    Lynch, G.4
  • 33
    • 0027516156 scopus 로고
    • Proteasomes: Multicatalytic proteinase complexes
    • Rivett JA (1993) Proteasomes: multicatalytic proteinase complexes. Biochem J 291:1-10.
    • (1993) Biochem J , vol.291 , pp. 1-10
    • Rivett, J.A.1
  • 34
    • 0001408578 scopus 로고
    • Proteasome location
    • Rivett JA, Knecht E (1993) Proteasome location. Curr Biol 3:127-129.
    • (1993) Curr Biol , vol.3 , pp. 127-129
    • Rivett, J.A.1    Knecht, E.2
  • 35
    • 0027980319 scopus 로고
    • Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules
    • Rock KL, Gramm C, Rothstein L, Clark K, Stein R, Dick L, Hwang D, Goldberg AL (1994) Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell 78:761-771.
    • (1994) Cell , vol.78 , pp. 761-771
    • Rock, K.L.1    Gramm, C.2    Rothstein, L.3    Clark, K.4    Stein, R.5    Dick, L.6    Hwang, D.7    Goldberg, A.L.8
  • 36
    • 0025639158 scopus 로고
    • The E6 oncoprotein encoded by human papillomavirus types 16 and 18 promotes the degradation of p53
    • Scheffner M, Werness BA, Huibregtse JM, Levine AJ, Howley PM (1990) The E6 oncoprotein encoded by human papillomavirus types 16 and 18 promotes the degradation of p53. Cell 63:1129-1136.
    • (1990) Cell , vol.63 , pp. 1129-1136
    • Scheffner, M.1    Werness, B.A.2    Huibregtse, J.M.3    Levine, A.J.4    Howley, P.M.5
  • 39
    • 0028027308 scopus 로고
    • Ubiquitin-dependent c-Jun degradation in vivo is mediated by the delta domain
    • Treier M, Staszewski LM, Bohmann D (1994) Ubiquitin-dependent c-Jun degradation in vivo is mediated by the delta domain. Cell 78:787-798.
    • (1994) Cell , vol.78 , pp. 787-798
    • Treier, M.1    Staszewski, L.M.2    Bohmann, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.