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Volumn 5, Issue 11, 2004, Pages 884-895

Unexpected intracellular localization of the AMD-associated cystatin C variant

Author keywords

Age related macular degeneration; Precursor cystatin C; Processing; Retinal pigment epithelium; Variant B

Indexed keywords

ALANINE; CYSTATIN C; CYTOPLASM PROTEIN; GREEN FLUORESCENT PROTEIN; HYBRID PROTEIN; PROTEIN PRECURSOR; SIGNAL PEPTIDE; THREONINE;

EID: 7244221537     PISSN: 13989219     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1600-0854.2004.00230.x     Document Type: Article
Times cited : (43)

References (37)
  • 1
    • 0015694444 scopus 로고
    • Post-γ-globulin: Isolation and physicochemical characterization
    • Cejka J, Fleischmann LE. Post-γ-globulin: isolation and physicochemical characterization. Arch Biochem Biophys 1973;157:168-176.
    • (1973) Arch. Biochem. Biophys. , vol.157 , pp. 168-176
    • Cejka, J.1    Fleischmann, L.E.2
  • 3
    • 0018718823 scopus 로고
    • Quantitation of γ-trace in human biological fluids: Indications for production in the central nervous system
    • Lofberg H, Grubb AO. Quantitation of γ-trace in human biological fluids: indications for production in the central nervous system. Scand J Clin Lab Invest 1979;39:619-626.
    • (1979) Scand. J. Clin. Lab. Invest. , vol.39 , pp. 619-626
    • Lofberg, H.1    Grubb, A.O.2
  • 4
    • 0020609588 scopus 로고
    • The γ-trace concentration of normal human seminal plasma is thirty-six times that of normal human blood plasma
    • Grubb AO, Weiber H, Lofberg H. The γ-trace concentration of normal human seminal plasma is thirty-six times that of normal human blood plasma. Scand J Clin Lab Invest 1983;43:421-425.
    • (1983) Scand. J. Clin. Lab. Invest. , vol.43 , pp. 421-425
    • Grubb, A.O.1    Weiber, H.2    Lofberg, H.3
  • 5
    • 0023024774 scopus 로고
    • Isolation of six cysteine proteinase inhibitors from human urine. Their physicochemical and enzyme kinetic properties and concentrations in biological fluids
    • Abrahamson M, Barrett AJ, Salvesen G, Grubb A. Isolation of six cysteine proteinase inhibitors from human urine. Their physicochemical and enzyme kinetic properties and concentrations in biological fluids. J Biol Chem 1986;261:11282-11289.
    • (1986) J. Biol. Chem. , vol.261 , pp. 11282-11289
    • Abrahamson, M.1    Barrett, A.J.2    Salvesen, G.3    Grubb, A.4
  • 6
    • 0023471335 scopus 로고
    • Constitutive secretion of cystatin C (γ-trace) by monocytes and macrophages and its downregulation after stimulation
    • Warfel AH, Zucker-Franklin D, Frangione B, Ghiso J. Constitutive secretion of cystatin C (γ-trace) by monocytes and macrophages and its downregulation after stimulation. J Exp Med 1987;166: 1912-1917.
    • (1987) J. Exp. Med. , vol.166 , pp. 1912-1917
    • Warfel, A.H.1    Zucker-Franklin, D.2    Frangione, B.3    Ghiso, J.4
  • 7
    • 0025105872 scopus 로고
    • Levels of neutrophil elastase and cathepsin B activities, and cystatins in human sputum: Relationship to inflammation
    • Buttle DJ, Burnett D, Abrahamson M. Levels of neutrophil elastase and cathepsin B activities, and cystatins in human sputum: relationship to inflammation. Scand J Clin Lab Invest 1990;50:509-516.
    • (1990) Scand. J. Clin. Lab. Invest. , vol.50 , pp. 509-516
    • Buttle, D.J.1    Burnett, D.2    Abrahamson, M.3
  • 8
    • 0033838159 scopus 로고    scopus 로고
    • Identification of proteins from human cerebrospinal fluid, separated by two-dimensional polyacrylamide gel electrophoresis
    • Sickmann A, Dormeyer W, Wortelkamp S, Woitalla D, Kuhn W, Meyer HE. Identification of proteins from human cerebrospinal fluid, separated by two-dimensional polyacrylamide gel electrophoresis. Electrophoresis 2000;21:2721-2728.
    • (2000) Electrophoresis , vol.21 , pp. 2721-2728
    • Sickmann, A.1    Dormeyer, W.2    Wortelkamp, S.3    Woitalla, D.4    Kuhn, W.5    Meyer, H.E.6
  • 9
    • 0021236724 scopus 로고
    • The place of human γ-trace (cystatin C) amongst the cysteine proteinase inhibitors
    • Barrett AJ, Davies ME, Grubb A. The place of human γ-trace (cystatin C) amongst the cysteine proteinase inhibitors. Biochem Biophys Res Commun 1984;120:631-636.
    • (1984) Biochem. Biophys. Res. Commun. , vol.120 , pp. 631-636
    • Barrett, A.J.1    Davies, M.E.2    Grubb, A.3
  • 10
    • 0023229953 scopus 로고
    • Molecular cloning and sequence analysis of cDNA coding for the precursor of the human cysteine proteinase inhibitor cystatin C
    • Abrahamson M, Grubb A, Olafsson I, Lundwall A. Molecular cloning and sequence analysis of cDNA coding for the precursor of the human cysteine proteinase inhibitor cystatin C. FEBS Lett 1987;216: 229-233.
    • (1987) FEBS Lett. , vol.216 , pp. 229-233
    • Abrahamson, M.1    Grubb, A.2    Olafsson, I.3    Lundwall, A.4
  • 12
    • 0034174478 scopus 로고    scopus 로고
    • Analysis of expressed sequence tags of retinal pigment epithelium: Cystatin C is an abundant transcript
    • Paraoan L, Grierson I, Maden BEH. Analysis of expressed sequence tags of retinal pigment epithelium: cystatin C is an abundant transcript. Int J Biochem Cell Biol 2000;32:417-426.
    • (2000) Int. J. Biochem. Cell Biol. , vol.32 , pp. 417-426
    • Paraoan, L.1    Grierson, I.2    Maden, B.E.H.3
  • 13
    • 0002441838 scopus 로고
    • Anatomy of the human retinal pigment epithelium
    • Marmor MF, ad. Cambridge, MA: Harvard University Press
    • Zinn KM, Benjamin-Henkind JV. Anatomy of the human retinal pigment epithelium. In: Marmor MF, ad. The Retinal Pigment Epithelium. Cambridge, MA: Harvard University Press, 1979: 3-31.
    • (1979) The Retinal Pigment Epithelium , pp. 3-31
    • Zinn, K.M.1    Benjamin-Henkind, J.V.2
  • 14
    • 0022344155 scopus 로고
    • Retinal photoreceptor-pigment epithelium interactions. Friedenwald lecture
    • Bok D. Retinal photoreceptor-pigment epithelium interactions. Friedenwald lecture. Invest Ophthalmol Vis Sci 1985;26: 1659-1694.
    • (1985) Invest. Ophthalmol. Vis. Sci. , vol.26 , pp. 1659-1694
    • Bok, D.1
  • 15
    • 0013501421 scopus 로고    scopus 로고
    • Comparative and evolutionary aspects of the retinal pigment epithelium
    • Marmor MF, Wolfensberger TJ, ads. Cambridge, MA: Harvard University Press
    • Marmor MF. Comparative and evolutionary aspects of the retinal pigment epithelium. In: Marmor MF, Wolfensberger TJ, ads. The Retinal Pigment Epithelium. Cambridge, MA: Harvard University Press, 1998: 23-37.
    • (1998) The Retinal Pigment Epithelium , pp. 23-37
    • Marmor, M.F.1
  • 16
    • 0034792875 scopus 로고    scopus 로고
    • Precursor cystatin C in cultured retinal pigment epithelium cells: Evidence for processing through the secretory pathway
    • Paraoan L, White MR, Spiller DG, Grierson I, Maden BE. Precursor cystatin C in cultured retinal pigment epithelium cells: evidence for processing through the secretory pathway. Mol Membr Biol 2001;18:229-236.
    • (2001) Mol. Membr. Biol. , vol.18 , pp. 229-236
    • Paraoan, L.1    White, M.R.2    Spiller, D.G.3    Grierson, I.4    Maden, B.E.5
  • 17
    • 0037653685 scopus 로고    scopus 로고
    • Fate of cystatin C lacking the leader sequence in RPE cells
    • Paraoan L, Grierson I, Maden BE. Fate of cystatin C lacking the leader sequence in RPE cells. Exp Eye Res 2003;76:753-756.
    • (2003) Exp. Eye Res. , vol.76 , pp. 753-756
    • Paraoan, L.1    Grierson, I.2    Maden, B.E.3
  • 19
    • 0020770479 scopus 로고
    • Patterns of amino acids near signal-sequence cleavage sites
    • von Heijne G. Patterns of amino acids near signal-sequence cleavage sites. Eur J Biochem 1983;133:17-21.
    • (1983) Eur. J. Biochem. , vol.133 , pp. 17-21
    • von Heijne, G.1
  • 20
    • 0021856417 scopus 로고
    • Signal sequences. The limits of variation
    • von Heijne G. Signal sequences. The limits of variation. J Mol Biol 1985;184:99-105.
    • (1985) J. Mol. Biol. , vol.184 , pp. 99-105
    • von Heijne, G.1
  • 21
    • 0032563163 scopus 로고    scopus 로고
    • Crystal structure of the signal sequence binding subunit of the signal recognition particle
    • Keenan RJ, Freymann DM, Walter P, Stroud RM. Crystal structure of the signal sequence binding subunit of the signal recognition particle. Cell 1998;94:181-191.
    • (1998) Cell , vol.94 , pp. 181-191
    • Keenan, R.J.1    Freymann, D.M.2    Walter, P.3    Stroud, R.M.4
  • 22
    • 0024966540 scopus 로고
    • Model for signal sequence recognition from amino-acid sequence of 54K subunit of signal recognition particle
    • Bernstein HD, Poritz MA, Strub K, Hoben PJ, Brenner S, Walter P. Model for signal sequence recognition from amino-acid sequence of 54K subunit of signal recognition particle. Nature 1989;340: 482-486.
    • (1989) Nature , vol.340 , pp. 482-486
    • Bernstein, H.D.1    Poritz, M.A.2    Strub, K.3    Hoben, P.J.4    Brenner, S.5    Walter, P.6
  • 23
    • 0032511889 scopus 로고    scopus 로고
    • Crystal structure of a bacterial signal peptidase in complex with a β-lactam inhibitor
    • Paetzel M, Dalbey RE, Strynacka NC. Crystal structure of a bacterial signal peptidase in complex with a β-lactam inhibitor. Nature 1998;396:186-190.
    • (1998) Nature , vol.396 , pp. 186-190
    • Paetzel, M.1    Dalbey, R.E.2    Strynacka, N.C.3
  • 24
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen H, Engelbrecht J, Brunak S, von Heijne G. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng 1997; 10: 1-6.
    • (1997) Protein Eng. , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    von Heijne, G.4
  • 25
    • 0034697980 scopus 로고    scopus 로고
    • Predicting subcellular localization of proteins based on their N-terminal amino acid sequence
    • Emanuelsson O, Nielsen H, Brunak S, von Heijne G. Predicting subcellular localization of proteins based on their N-terminal amino acid sequence. J Mol Biol 2000;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
  • 26
    • 0022731676 scopus 로고
    • Mitochondrial targeting sequences may form amphiphilic helices
    • von Heijne G. Mitochondrial targeting sequences may form amphiphilic helices. EMBO J 1986;5:1335-1342.
    • (1986) EMBO J. , vol.5 , pp. 1335-1342
    • von Heijne, G.1
  • 27
    • 0023920458 scopus 로고
    • Mitochondrial presequences
    • Roise D, Schatz G. Mitochondrial presequences. J Biol Chem 1988;263:4509-4511.
    • (1988) J. Biol. Chem. , vol.263 , pp. 4509-4511
    • Roise, D.1    Schatz, G.2
  • 28
    • 0024298711 scopus 로고
    • A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptices
    • Deshaies RJ, Koch BD, Werner-Washburne M, Craig EA, Schekman R. A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptices. Nature 1988;332:800-805.
    • (1988) Nature , vol.332 , pp. 800-805
    • Deshaies, R.J.1    Koch, B.D.2    Werner-Washburne, M.3    Craig, E.A.4    Schekman, R.5
  • 29
    • 0030969942 scopus 로고    scopus 로고
    • Protein import into mitochondria
    • Neupert W. Protein import into mitochondria. Annu Rev Biochem 1997;66:863-917.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 863-917
    • Neupert, W.1
  • 30
    • 0034734011 scopus 로고    scopus 로고
    • Targeting of proteins to mitochondria
    • Lithgow T. Targeting of proteins to mitochondria. FEBS Lett 2000;476:22-26.
    • (2000) FEBS Lett. , vol.476 , pp. 22-26
    • Lithgow, T.1
  • 33
    • 0033118573 scopus 로고    scopus 로고
    • Detection of changes in mitochondrial function during apoptosis by simultaneous staining with multiple fluorescent dyes and correlated multiparameter flow cytometry
    • Foot M, Pierce RH. Detection of changes in mitochondrial function during apoptosis by simultaneous staining with multiple fluorescent dyes and correlated multiparameter flow cytometry. Cytometry 1999;35:311-317.
    • (1999) Cytometry , vol.35 , pp. 311-317
    • Foot, M.1    Pierce, R.H.2
  • 34
    • 0037442128 scopus 로고    scopus 로고
    • The mitochondrial network of human neutrophils: Role in chemotaxis, phagocytosis, respiratory burst activation, and commitment to apoptosis
    • Fossati G, Moulding DA, Spiller DG, Moots RJ, White MR, Edwards SW. The mitochondrial network of human neutrophils: role in chemotaxis, phagocytosis, respiratory burst activation, and commitment to apoptosis. J Immunol 2003;170:1964-1972.
    • (2003) J. Immunol. , vol.170 , pp. 1964-1972
    • Fossati, G.1    Moulding, D.A.2    Spiller, D.G.3    Moots, R.J.4    White, M.R.5    Edwards, S.W.6
  • 35
    • 0033776271 scopus 로고    scopus 로고
    • Changes in intramitochondrial and cytosolic pH: Early events that modulate caspase activation during apoptosis
    • Matsuyama S, Llopis J, Deveraux QL, Tsien RY, Reed JC. Changes in intramitochondrial and cytosolic pH: early events that modulate caspase activation during apoptosis. Nat Cell Biol 2000;2: 318-325.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 318-325
    • Matsuyama, S.1    Llopis, J.2    Deveraux, Q.L.3    Tsien, R.Y.4    Reed, J.C.5
  • 36
    • 0034644670 scopus 로고    scopus 로고
    • Identification of two transmembrane regions and a cytosolic domain of rat mitochondrial glycerophosphate acyltransferase
    • Balija VS, Chakraborty TR, Nikonov AV, Morimoto T, Halclar D. Identification of two transmembrane regions and a cytosolic domain of rat mitochondrial glycerophosphate acyltransferase. J Biol Chem 2000;275:31668-31673.
    • (2000) J. Biol. Chem. , vol.275 , pp. 31668-31673
    • Balija, V.S.1    Chakraborty, T.R.2    Nikonov, A.V.3    Morimoto, T.4    Halclar, D.5


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