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Volumn 43, Issue 18, 2004, Pages 5119-5125

Association of Human Neuroglobin with Cystatin C, a Cysteine Proteinase Inhibitor

Author keywords

[No Author keywords available]

Indexed keywords

BRAIN; DIMERS; DISEASE CONTROL; MONOMERS; NEUROLOGY; OXYGEN; SURFACE PLASMON RESONANCE;

EID: 2442584665     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0495782     Document Type: Article
Times cited : (47)

References (35)
  • 1
    • 0034726874 scopus 로고    scopus 로고
    • A vertebrate globin expressed in the brain
    • Burmester, T., Weich, B., Reinhardt, S., and Hankeln, T. (2000) A vertebrate globin expressed in the brain. Nature 407, 520-523.
    • (2000) Nature , vol.407 , pp. 520-523
    • Burmester, T.1    Weich, B.2    Reinhardt, S.3    Hankeln, T.4
  • 2
    • 0035929255 scopus 로고    scopus 로고
    • Neuroglobins from the zebrafish Danio rerio and the pufferfish Tetraodon nigroviridis
    • Awenius, C., Hankeln, T., and Burmester, T. (2001) Neuroglobins from the zebrafish Danio rerio and the pufferfish Tetraodon nigroviridis. Biochem. Biophys. Res. Commun. 287, 418-421.
    • (2001) Biochem. Biophys. Res. Commun. , vol.287 , pp. 418-421
    • Awenius, C.1    Hankeln, T.2    Burmester, T.3
  • 5
    • 0035839641 scopus 로고    scopus 로고
    • Human neuroglobin, a hexacorordinate hemoglobin that reversibly binds oxygen
    • Trent, J. T. 3rd, Watts, R. A., and Hargrove, M. S. (2001) Human neuroglobin, a hexacorordinate hemoglobin that reversibly binds oxygen. J. Biol. Chem. 276, 30106-30110.
    • (2001) J. Biol. Chem. , vol.276 , pp. 30106-30110
    • Trent III, J.T.1    Watts, R.A.2    Hargrove, M.S.3
  • 8
    • 0035909992 scopus 로고    scopus 로고
    • Neuroglobin is up-regulated by and protects neurons from hypoxicischemic injury
    • Sun, Y., Jin, K., Mao, X. O., Zhu, Y., and Greenberg, D. A. (2001) Neuroglobin is up-regulated by and protects neurons from hypoxicischemic injury. Proc. Natl. Acad. Sci. U.S.A. 98, 15306-15311.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 15306-15311
    • Sun, Y.1    Jin, K.2    Mao, X.O.3    Zhu, Y.4    Greenberg, D.A.5
  • 10
    • 0141704224 scopus 로고    scopus 로고
    • Oxidized human neuroglobin acts as a heterotrimeric Galpha protein guanine nucleotide dissociation inhibitor
    • Wakasugi, K., Nakano, T., and Morishima, I. (2003) Oxidized human neuroglobin acts as a heterotrimeric Galpha protein guanine nucleotide dissociation inhibitor. J. Biol. Chem. 278, 36505-36512.
    • (2003) J. Biol. Chem. , vol.278 , pp. 36505-36512
    • Wakasugi, K.1    Nakano, T.2    Morishima, I.3
  • 11
    • 0035952766 scopus 로고    scopus 로고
    • Heterotrimeric G-protein betagamma-dimers in growth and differentiation
    • Schwindinger, W. F., and Robishaw, J. D. (2001) Heterotrimeric G-protein betagamma-dimers in growth and differentiation. Oncogene 20, 1653-1660.
    • (2001) Oncogene , vol.20 , pp. 1653-1660
    • Schwindinger, W.F.1    Robishaw, J.D.2
  • 13
    • 0030052426 scopus 로고    scopus 로고
    • Folding-related dimerization of human cystatin C
    • Ekiel, I., and Abrahamson, M. (1996) Folding-related dimerization of human cystatin C. J. Biol. Chem. 271, 1314-1321.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1314-1321
    • Ekiel, I.1    Abrahamson, M.2
  • 14
    • 0023099296 scopus 로고
    • c-Ha-ras gene products are potent inhibitors of cathepsins B and L
    • Hiwasa, T., Yokoyama, S., Ha, J.-M., Noguchi, S., and Sakiyama, S. (1987) c-Ha-ras gene products are potent inhibitors of cathepsins B and L. FEBS Lett. 211, 23-26.
    • (1987) FEBS Lett. , vol.211 , pp. 23-26
    • Hiwasa, T.1    Yokoyama, S.2    Ha, J.-M.3    Noguchi, S.4    Sakiyama, S.5
  • 15
    • 0033551781 scopus 로고    scopus 로고
    • Highly differentiated motifs responsible for two cytokine activities of a split human tRNA synthetase
    • Wakasugi, K., and Schimmel, P. (1999) Highly differentiated motifs responsible for two cytokine activities of a split human tRNA synthetase. J. Biol. Chem. 274, 23155-23159.
    • (1999) J. Biol. Chem. , vol.274 , pp. 23155-23159
    • Wakasugi, K.1    Schimmel, P.2
  • 16
    • 0033515887 scopus 로고    scopus 로고
    • Two distinct cytokines released from a human aminoacyl-tRNA synthetase
    • Wakasugi, K., and Schimmel, P. (1999) Two distinct cytokines released from a human aminoacyl-tRNA synthetase. Science 284, 147-151.
    • (1999) Science , vol.284 , pp. 147-151
    • Wakasugi, K.1    Schimmel, P.2
  • 17
  • 20
    • 0034849483 scopus 로고    scopus 로고
    • Elevation of cystatin C in susceptible neurons in Alzheimer's disease
    • Deng, A., Irizarry, M. C., Nitsch, R. M., Growdon, J. H., and Rebeck, G. W. (2001) Elevation of cystatin C in susceptible neurons in Alzheimer's disease. Am. J. Pathol. 159, 1061-1068.
    • (2001) Am. J. Pathol. , vol.159 , pp. 1061-1068
    • Deng, A.1    Irizarry, M.C.2    Nitsch, R.M.3    Growdon, J.H.4    Rebeck, G.W.5
  • 21
    • 0029097834 scopus 로고
    • Cystatin C, a protease inhibitor, in degenerating rat hippocampal neurons following transient forebrain ischemia
    • Palm, D. E., Knuckey, N. W., Primiano, M. J., Spangenberger, A. G., and Johanson, C. E. (1995) Cystatin C, a protease inhibitor, in degenerating rat hippocampal neurons following transient forebrain ischemia. Brain Res. 691, 1-8.
    • (1995) Brain Res. , vol.691 , pp. 1-8
    • Palm, D.E.1    Knuckey, N.W.2    Primiano, M.J.3    Spangenberger, A.G.4    Johanson, C.E.5
  • 22
    • 0034637296 scopus 로고    scopus 로고
    • Involvement of cystatin C in oxidative stress-induced apoptosis of cultured rat CNS neurons
    • Nishio, C., Yoshida, K., Nishiyama, K., Hatanaka, H., and Yamada, M. (2000) Involvement of cystatin C in oxidative stress-induced apoptosis of cultured rat CNS neurons. Brain Res. 873, 252-262.
    • (2000) Brain Res. , vol.873 , pp. 252-262
    • Nishio, C.1    Yoshida, K.2    Nishiyama, K.3    Hatanaka, H.4    Yamada, M.5
  • 23
    • 0031764610 scopus 로고    scopus 로고
    • Progressive ataxia, myoclonic epilepsy and cerebellar apoptosis in cystatin B-deficient mice
    • Pennacchio, L. A., Bouley, D. M., Higgins, K. M., Scott, M. P., Noebels, J. L., and Myers, R. M. (1998) Progressive ataxia, myoclonic epilepsy and cerebellar apoptosis in cystatin B-deficient mice. Nat. Genet. 20, 251-258.
    • (1998) Nat. Genet. , vol.20 , pp. 251-258
    • Pennacchio, L.A.1    Bouley, D.M.2    Higgins, K.M.3    Scott, M.P.4    Noebels, J.L.5    Myers, R.M.6
  • 25
    • 0035980006 scopus 로고    scopus 로고
    • Evidence that inhibition of cathepsin-B contributes to the neuroprotective properties of caspase inhibitor Tyr-Val-Ala-Asp-chloromethyl ketone
    • Gray, J., Haran, M. M., Schneider, K., Vesce, S., Ray, A. M., Owen, D., White, I. R., Cutler, P., and Davis, J. B. (2001) Evidence that inhibition of cathepsin-B contributes to the neuroprotective properties of caspase inhibitor Tyr-Val-Ala-Asp-chloromethyl ketone. J. Biol. Chem. 276, 32750-32755.
    • (2001) J. Biol. Chem. , vol.276 , pp. 32750-32755
    • Gray, J.1    Haran, M.M.2    Schneider, K.3    Vesce, S.4    Ray, A.M.5    Owen, D.6    White, I.R.7    Cutler, P.8    Davis, J.B.9
  • 27
    • 0035408169 scopus 로고    scopus 로고
    • The lysosomal protease cathepsin D mediates apoptosis induced by oxidative stress
    • Kagedal, K., Johansson, U., and Öllinger, K. (2001) The lysosomal protease cathepsin D mediates apoptosis induced by oxidative stress. FASEB J. 15, 1592-1594.
    • (2001) FASEB J. , vol.15 , pp. 1592-1594
    • Kagedal, K.1    Johansson, U.2    Öllinger, K.3
  • 28
    • 0035801540 scopus 로고    scopus 로고
    • Three-dimensional domain swapping in the folded and molten-globule states of cystatins, an amyloid-forming structural superfamily
    • Staniforth, R. A., Giannini, S., Higgins, L. D., Conroy, M. J., Hounslow, A. M., Jerala, R., Craven, C. J., and Waltho, J. P. (2001) Three-dimensional domain swapping in the folded and molten-globule states of cystatins, an amyloid-forming structural superfamily. EMBO J. 20, 4774-4781.
    • (2001) EMBO J. , vol.20 , pp. 4774-4781
    • Staniforth, R.A.1    Giannini, S.2    Higgins, L.D.3    Conroy, M.J.4    Hounslow, A.M.5    Jerala, R.6    Craven, C.J.7    Waltho, J.P.8
  • 29
    • 0033635021 scopus 로고    scopus 로고
    • FGF-2-responsive neural stem cell proliferation requires CCg, a novel autocrine/paracrine cofactor
    • Taupin, P., Ray, J., Fischer, W. H., Suhr, S. T., Hakansson, K., Grubb, A., and Gage, F. H. (2000) FGF-2-responsive neural stem cell proliferation requires CCg, a novel autocrine/paracrine cofactor. Neuron 28, 385-397.
    • (2000) Neuron , vol.28 , pp. 385-397
    • Taupin, P.1    Ray, J.2    Fischer, W.H.3    Suhr, S.T.4    Hakansson, K.5    Grubb, A.6    Gage, F.H.7
  • 30
    • 0011766298 scopus 로고
    • Amyloid fibrils in hereditary cerebral hemorrhage with amyloidosis of Icelandic type is a variant of gamma-trace basic protein (cystatin C)
    • Ghiso, J., Jensson, O., and Frangione, B. (1986) Amyloid fibrils in hereditary cerebral hemorrhage with amyloidosis of Icelandic type is a variant of gamma-trace basic protein (cystatin C). Proc. Natl. Acad. Sci. U.S.A. 83, 2974-2978.
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 2974-2978
    • Ghiso, J.1    Jensson, O.2    Frangione, B.3
  • 31
    • 0038472441 scopus 로고    scopus 로고
    • Cystatin C colocalizes with amyloid-beta and coimmunoprecipitates with amyloid-beta precursor protein in sporadic inclusion-body myositis muscles
    • Vattemi, G., Engel, W. K., McFerrin, J., and Askanas, V. (2003) Cystatin C colocalizes with amyloid-beta and coimmunoprecipitates with amyloid-beta precursor protein in sporadic inclusion-body myositis muscles. J. Neurochem. 85, 1539-1546.
    • (2003) J. Neurochem. , vol.85 , pp. 1539-1546
    • Vattemi, G.1    Engel, W.K.2    McFerrin, J.3    Askanas, V.4
  • 32
    • 0027976996 scopus 로고
    • Increased body temperature accelerates aggregation of the Leu68→Gln mutant cystatin C, the amyloid-forming protein in hereditary cystatin C amyloid angiopathy
    • Abrahamson, M., and Grubb, A. (1994) Increased body temperature accelerates aggregation of the Leu68→Gln mutant cystatin C, the amyloid-forming protein in hereditary cystatin C amyloid angiopathy. Proc. Natl. Acad. Sci. U.S.A. 91, 1416-1420.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 1416-1420
    • Abrahamson, M.1    Grubb, A.2
  • 33
    • 0026730350 scopus 로고
    • Amyloidogenicity of βA4 and βA4-bearing amyloid protein precursor fragments by metal-catalyzed oxidation
    • Dyrks, T., Dyrks, E., Hartmann, T., Masters, C., and Beyreuther, K. (1992) Amyloidogenicity of βA4 and βA4-bearing amyloid protein precursor fragments by metal-catalyzed oxidation. J. Biol. Chem. 267, 18210-18217.
    • (1992) J. Biol. Chem. , vol.267 , pp. 18210-18217
    • Dyrks, T.1    Dyrks, E.2    Hartmann, T.3    Masters, C.4    Beyreuther, K.5
  • 34
    • 0032879452 scopus 로고    scopus 로고
    • Role of cytochrome c as a stimulator of α-synuclein aggregation in Lewy body disease
    • Hashimoto, M., Takeda, A., Hsu, L. J., Takenouchi, T., and Masliah, E. (1999) Role of cytochrome c as a stimulator of α-synuclein aggregation in Lewy body disease. J. Biol. Chem. 274, 28849-28852.
    • (1999) J. Biol. Chem. , vol.274 , pp. 28849-28852
    • Hashimoto, M.1    Takeda, A.2    Hsu, L.J.3    Takenouchi, T.4    Masliah, E.5


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