메뉴 건너뛰기




Volumn 10, Issue 18, 2010, Pages 3272-3291

Proteomic analysis of synaptosomal protein expression reveals that cerebral ischemia alters lysosomal Psap processing

Author keywords

Animal proteomics; Cerebral ischemia; Hippocampus; Isotope coded affinity tags; Prosaposin; Synaptosome

Indexed keywords

PROSAPOSIN; PROTEIN PRECURSOR; PROTEIN SAPOSIN C; UNCLASSIFIED DRUG;

EID: 77956534059     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.200900447     Document Type: Article
Times cited : (17)

References (76)
  • 1
    • 1842612444 scopus 로고    scopus 로고
    • Stability of dendritic spines and synaptic contacts is controlled by alpha N-catenin
    • DOI 10.1038/nn1212
    • Abe, K., Chisaka, O., Van Roy, F., Takeichi, M., Stability of dendritic spines and synaptic contacts is controlled by alpha N-catenin. Nat. Neurosci. 2004, 7, 357-363. (Pubitemid 38429175)
    • (2004) Nature Neuroscience , vol.7 , Issue.4 , pp. 357-363
    • Abe, K.1    Chisaka, O.2    Van Roy, F.3    Takeichi, M.4
  • 2
    • 0345169052 scopus 로고    scopus 로고
    • Syndecans: Proteoglycan regulators of cell-surface microdomains?
    • Couchman, J. R., Syndecans: proteoglycan regulators of cell-surface microdomains? Nat. Rev. Mol. Cell Biol. 2003, 4, 926-937.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 926-937
    • Couchman, J.R.1
  • 3
    • 0036467761 scopus 로고    scopus 로고
    • Molecular morphogens for dendritic spines
    • Ehlers, M. D., Molecular morphogens for dendritic spines. Trends Neurosci. 2002, 25, 64-67.
    • (2002) Trends Neurosci. , vol.25 , pp. 64-67
    • Ehlers, M.D.1
  • 4
    • 0041989616 scopus 로고    scopus 로고
    • Induction of dendritic spines by an extracellular domain of AMPA receptor subunit GluR2
    • Passafaro, M., Nakagawa, T., Sala, C., Sheng, M., Induction of dendritic spines by an extracellular domain of AMPA receptor subunit GluR2. Nature 2003, 424, 677-681.
    • (2003) Nature , vol.424 , pp. 677-681
    • Passafaro, M.1    Nakagawa, T.2    Sala, C.3    Sheng, M.4
  • 5
    • 0037418622 scopus 로고    scopus 로고
    • To die or to sleep, perhaps to dream
    • Gasic, G. P., Nicotera, P., To die or to sleep, perhaps to dream. Toxicol. Lett. 2003, 139, 221-227.
    • (2003) Toxicol. Lett. , vol.139 , pp. 221-227
    • Gasic, G.P.1    Nicotera, P.2
  • 7
    • 0020315562 scopus 로고
    • Neurotransmitter metabolism in rat brain synaptosomes: Effect of anoxia and pH
    • Pastuszko, A., Wilson, D. F., Erecinska, M., Neurotransmitter metabolism in rat brain synaptosomes: effect of anoxia and pH. J. Neurochem. 1982, 38, 1657-1667.
    • (1982) J. Neurochem. , vol.38 , pp. 1657-1667
    • Pastuszko, A.1    Wilson, D.F.2    Erecinska, M.3
  • 8
    • 0018891693 scopus 로고
    • The effect of acute hypoxia on synaptosomes from rat brain
    • Rafalowska, U., Erecinska, M., Wilson, D. F., The effect of acute hypoxia on synaptosomes from rat brain. J. Neurochem. 1980, 34, 1160-1165.
    • (1980) J. Neurochem. , vol.34 , pp. 1160-1165
    • Rafalowska, U.1    Erecinska, M.2    Wilson, D.F.3
  • 9
    • 0036178223 scopus 로고    scopus 로고
    • Synaptosomal susceptibility on global ischaemia caused by cardiac arrest correlated with early and late times after recirculation in rats
    • DOI 10.1016/S0300-9572(01)00451-8, PII S0300957201004518
    • Sulkowski, G., Waskiewicz, J., Walski, M., Januszewski, S., Rafalowska, U., Synaptosomal susceptibility on global ischaemia caused by cardiac arrest correlated with early and late times after recirculation in rats. Resuscitation 2002, 52, 203-213. (Pubitemid 34159032)
    • (2002) Resuscitation , vol.52 , Issue.2 , pp. 203-213
    • Sulkowski, G.1    Waskiewicz, J.2    Walski, M.3    Januszewski, S.4    Rafalowska, U.5
  • 10
    • 34247120020 scopus 로고    scopus 로고
    • Fine mapping of the spatial relationship between acute ischemia and dendritic structure indicates selective vulnerability of layer V neuron dendritic tufts within single neurons in vivo
    • Enright, L. E., Zhang, S., Murphy, T. H., Fine mapping of the spatial relationship between acute ischemia and dendritic structure indicates selective vulnerability of layer V neuron dendritic tufts within single neurons in vivo. J. Cereb. Blood Flow Metab. 2007, 27, 1185-1200.
    • (2007) J. Cereb. Blood Flow Metab. , vol.27 , pp. 1185-1200
    • Enright, L.E.1    Zhang, S.2    Murphy, T.H.3
  • 11
    • 34249007157 scopus 로고    scopus 로고
    • Imaging the impact of cortical microcirculation on synaptic structure and sensory-evoked hemodynamic responses in vivo
    • Zhang, S., Murphy, T. H., Imaging the impact of cortical microcirculation on synaptic structure and sensory-evoked hemodynamic responses in vivo. PLoS Biol. 2007, 5, e119.
    • (2007) PLoS Biol. , vol.5
    • Zhang, S.1    Murphy, T.H.2
  • 12
    • 37549000214 scopus 로고    scopus 로고
    • Cerebral ischemia causes dysregulation of synaptic adhesion in mouse synaptosomes
    • Costain, W. J., Rasquinha, I., Sandhu, J. K., Rippstein, P. et al., Cerebral ischemia causes dysregulation of synaptic adhesion in mouse synaptosomes. J. Cereb. Blood Flow Metab. 2008, 28, 99-110.
    • (2008) J. Cereb. Blood Flow Metab. , vol.28 , pp. 99-110
    • Costain, W.J.1    Rasquinha, I.2    Sandhu, J.K.3    Rippstein, P.4
  • 13
    • 0035313299 scopus 로고    scopus 로고
    • Dendritic spines lost during glutamate receptor activation reemerge at original sites of synaptic contact
    • Hasbani, M. J., Schlief, M. L., Fisher, D. A., Goldberg, M. P., Dendritic spines lost during glutamate receptor activation reemerge at original sites of synaptic contact. J. Neurosci. 2001, 21, 2393-2403.
    • (2001) J. Neurosci. , vol.21 , pp. 2393-2403
    • Hasbani, M.J.1    Schlief, M.L.2    Fisher, D.A.3    Goldberg, M.P.4
  • 15
    • 0030175149 scopus 로고    scopus 로고
    • Rapid alterations in dendrite morphology during sublethal hypoxia or glutamate receptor activation
    • Park, J. S., Bateman, M. C., Goldberg, M. P., Rapid alterations in dendrite morphology during sublethal hypoxia or glutamate receptor activation. Neurobiol. Dis. 1996, 3, 215-227.
    • (1996) Neurobiol. Dis. , vol.3 , pp. 215-227
    • Park, J.S.1    Bateman, M.C.2    Goldberg, M.P.3
  • 16
    • 0033560011 scopus 로고    scopus 로고
    • Modification of postsynaptic densities after transient cerebral ischemia: A quantitative and three-dimensional ultrastructural study
    • Martone, M. E., Jones, Y. Z., Young, S. J., Ellisman, M. H. et al., Modification of postsynaptic densities after transient cerebral ischemia: a quantitative and three-dimensional ultrastructural study. J. Neurosci. 1999, 19, 1988-1997.
    • (1999) J. Neurosci. , vol.19 , pp. 1988-1997
    • Martone, M.E.1    Jones, Y.Z.2    Young, S.J.3    Ellisman, M.H.4
  • 18
    • 33646823604 scopus 로고    scopus 로고
    • Molecular characterization and comparison of the components and multiprotein complexes in the postsynaptic proteome
    • Collins, M. O., Husi, H., Yu, L., Brandon, J. M. et al., Molecular characterization and comparison of the components and multiprotein complexes in the postsynaptic proteome. J. Neurochem. 2006, 97, 16-23.
    • (2006) J. Neurochem. , vol.97 , pp. 16-23
    • Collins, M.O.1    Husi, H.2    Yu, L.3    Brandon, J.M.4
  • 19
    • 2442683994 scopus 로고    scopus 로고
    • Semi-quantitative proteomic analysis of rat forebrain post-synaptic density fractions by mass spectrometry
    • Peng, J., Kim, M. J., Cheng, D., Duong, D. M. et al., Semi-quantitative proteomic analysis of rat forebrain post-synaptic density fractions by mass spectrometry. J. Biol. Chem. 2004, 279, 21003-21011.
    • (2004) J. Biol. Chem. , vol.279 , pp. 21003-21011
    • Peng, J.1    Kim, M.J.2    Cheng, D.3    Duong, D.M.4
  • 20
    • 5644266504 scopus 로고    scopus 로고
    • Identification and verification of novel rodent post-synaptic density proteins
    • Jordan, B. A., Fernholz, B. D., Boussac, M., Xu, C. et al., Identification and verification of novel rodent post-synaptic density proteins. Mol. Cell Proteomics 2004, 3, 857-871.
    • (2004) Mol. Cell Proteomics , vol.3 , pp. 857-871
    • Jordan, B.A.1    Fernholz, B.D.2    Boussac, M.3    Xu, C.4
  • 21
    • 0942287657 scopus 로고    scopus 로고
    • Molecular constituents of the postsynaptic density fraction revealed by proteomic analysis using multidimensional liquid chromatography-tandem mass spectrometry
    • Yoshimura, Y., Yamauchi, Y., Shinkawa, T., Taoka, M. et al., Molecular constituents of the postsynaptic density fraction revealed by proteomic analysis using multidimensional liquid chromatography-tandem mass spectrometry. J. Neurochem. 2004, 88, 759-768.
    • (2004) J. Neurochem. , vol.88 , pp. 759-768
    • Yoshimura, Y.1    Yamauchi, Y.2    Shinkawa, T.3    Taoka, M.4
  • 22
    • 33847661220 scopus 로고    scopus 로고
    • Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations
    • Munton, R. P., Tweedie-Cullen, R., Livingstone-Zatchej, M., Weinandy, F. et al., Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations. Mol. Cell Proteomics 2007, 6, 283-293.
    • (2007) Mol. Cell Proteomics , vol.6 , pp. 283-293
    • Munton, R.P.1    Tweedie-Cullen, R.2    Livingstone-Zatchej, M.3    Weinandy, F.4
  • 24
    • 1642398957 scopus 로고    scopus 로고
    • Proteomic analysis of the synaptic plasma membrane fraction isolated from rat forebrain
    • Stevens, S. M., Jr, Zharikova, A. D., Prokai, L., Proteomic analysis of the synaptic plasma membrane fraction isolated from rat forebrain. Brain Res. Mol. Brain Res. 2003, 117, 116-128.
    • (2003) Brain Res. Mol. Brain Res. , vol.117 , pp. 116-128
    • Stevens Jr., S.M.1    Zharikova, A.D.2    Prokai, L.3
  • 25
    • 17444413094 scopus 로고    scopus 로고
    • Phosphoproteomic analysis of synaptosomes from human cerebral cortex
    • DeGiorgis, J. A., Jaffe, H., Moreira, J. E., Carlotti, C. G., Jr et al., Phosphoproteomic analysis of synaptosomes from human cerebral cortex. J. Proteome Res. 2005, 4, 306-315.
    • (2005) J. Proteome Res. , vol.4 , pp. 306-315
    • DeGiorgis, J.A.1    Jaffe, H.2    Moreira, J.E.3    Carlotti Jr., C.G.4
  • 26
    • 34250875149 scopus 로고    scopus 로고
    • Proteomic analysis of rat prefrontal cortex in three phases of morphine-induced conditioned place preference
    • Yang, L., Sun, Z. S., Zhu, Y. P., Proteomic analysis of rat prefrontal cortex in three phases of morphine-induced conditioned place preference. J. Proteome Res. 2007, 6, 2239-2247.
    • (2007) J. Proteome Res. , vol.6 , pp. 2239-2247
    • Yang, L.1    Sun, Z.S.2    Zhu, Y.P.3
  • 27
    • 29144493185 scopus 로고    scopus 로고
    • Immunoisolation of two synaptic vesicle pools from synaptosomes: A proteomics analysis
    • DOI 10.1111/j.1471-4159.2005.03506.x
    • Morciano, M., Burre, J., Corvey, C., Karas, M. et al., Immunoisolation of two synaptic vesicle pools from synaptosomes: a proteomics analysis. J. Neurochem. 2005, 95, 1732-1745. (Pubitemid 41804069)
    • (2005) Journal of Neurochemistry , vol.95 , Issue.6 , pp. 1732-1745
    • Morciano, M.1    Burre, J.2    Corvey, C.3    Karas, M.4    Zimmermann, H.5    Volknandt, W.6
  • 29
    • 33646900710 scopus 로고    scopus 로고
    • O-linked N-acetylglucosamine proteomics of post-synaptic density preparations using lectin weak affinity chromatography and mass spectrometry
    • Vosseller, K., Trinidad, J. C., Chalkley, R. J., Specht, C. G. et al., O-linked N-acetylglucosamine proteomics of post-synaptic density preparations using lectin weak affinity chromatography and mass spectrometry. Mol. Cell Proteomics 2006, 5, 923-934.
    • (2006) Mol. Cell Proteomics , vol.5 , pp. 923-934
    • Vosseller, K.1    Trinidad, J.C.2    Chalkley, R.J.3    Specht, C.G.4
  • 30
    • 33745617102 scopus 로고    scopus 로고
    • Relative and absolute quantification of postsynaptic density proteome isolated from rat forebrain and cerebellum
    • Cheng, D., Hoogenraad, C. C., Rush, J., Ramm, E. et al., Relative and absolute quantification of postsynaptic density proteome isolated from rat forebrain and cerebellum. Mol. Cell Proteomics 2006, 5, 1158-1170.
    • (2006) Mol. Cell Proteomics , vol.5 , pp. 1158-1170
    • Cheng, D.1    Hoogenraad, C.C.2    Rush, J.3    Ramm, E.4
  • 32
    • 20844455428 scopus 로고    scopus 로고
    • Organelle proteomics of rat synaptic proteins: Correlation-profiling by isotope-coded affinity tagging in conjunction with liquid chromatography-tandem mass spectrometry to reveal post-synaptic density specific proteins
    • Li, K., Hornshaw, M. P., van Minnen, J., Smalla, K. H. et al., Organelle proteomics of rat synaptic proteins: correlation-profiling by isotope-coded affinity tagging in conjunction with liquid chromatography-tandem mass spectrometry to reveal post-synaptic density specific proteins. J. Proteome Res. 2005, 4, 725-733.
    • (2005) J. Proteome Res. , vol.4 , pp. 725-733
    • Li, K.1    Hornshaw, M.P.2    Van Minnen, J.3    Smalla, K.H.4
  • 33
    • 27444442454 scopus 로고    scopus 로고
    • Proteomic comparison of two fractions derived from the transsynaptic scaffold
    • Phillips, G. R., Florens, L., Tanaka, H., Khaing, Z. Z. et al., Proteomic comparison of two fractions derived from the transsynaptic scaffold. J. Neurosci. Res. 2005, 81, 762-775.
    • (2005) J. Neurosci. Res. , vol.81 , pp. 762-775
    • Phillips, G.R.1    Florens, L.2    Tanaka, H.3    Khaing, Z.Z.4
  • 34
    • 22044446815 scopus 로고    scopus 로고
    • Proteomic analysis of synaptosomes using isotope-coded affinity tags and mass spectrometry
    • Schrimpf, S. P., Meskenaite, V., Brunner, E., Rutishauser, D. et al., Proteomic analysis of synaptosomes using isotope-coded affinity tags and mass spectrometry. Proteomics 2005, 5, 2531-2541.
    • (2005) Proteomics , vol.5 , pp. 2531-2541
    • Schrimpf, S.P.1    Meskenaite, V.2    Brunner, E.3    Rutishauser, D.4
  • 35
    • 20044371655 scopus 로고    scopus 로고
    • A proteomic survey of rat cerebral cortical synaptosomes
    • Witzmann, F. A., Arnold, R. J., Bai, F., Hrncirova, P. et al., A proteomic survey of rat cerebral cortical synaptosomes. Proteomics 2005, 5, 2177-2201.
    • (2005) Proteomics , vol.5 , pp. 2177-2201
    • Witzmann, F.A.1    Arnold, R.J.2    Bai, F.3    Hrncirova, P.4
  • 36
    • 28044435060 scopus 로고    scopus 로고
    • The stress-regulated protein M6a is a key modulator for neurite outgrowth and filopodium/spine formation
    • Alfonso, J., Fernandez, M. E., Cooper, B., Flugge, G., Frasch, A. C., The stress-regulated protein M6a is a key modulator for neurite outgrowth and filopodium/spine formation. Proc. Natl. Acad. Sci. USA 2005, 102, 17196-17201.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 17196-17201
    • Alfonso, J.1    Fernandez, M.E.2    Cooper, B.3    Flugge, G.4    Frasch, A.C.5
  • 37
    • 0033798454 scopus 로고    scopus 로고
    • Prosaposin-derived peptides enhanced sprouting of sensory neurons in vitro and induced sprouting at motor endplates in vivo
    • Campana, W. M., Mohiuddin, L., Misasi, R., O'Brien, J. S., Calcutt, N. A., Prosaposin-derived peptides enhanced sprouting of sensory neurons in vitro and induced sprouting at motor endplates in vivo. J. Peripher. Nerv. Syst. 2000, 5, 126-130.
    • (2000) J. Peripher. Nerv. Syst. , vol.5 , pp. 126-130
    • Campana, W.M.1    Mohiuddin, L.2    Misasi, R.3    O'Brien, J.S.4    Calcutt, N.A.5
  • 38
    • 22144458983 scopus 로고    scopus 로고
    • Neurotractin/kilon promotes neurite outgrowth and is expressed on reactive astrocytes after entorhinal cortex lesion
    • Schafer, M., Brauer, A. U., Savaskan, N. E., Rathjen, F. G., Brummendorf, T., Neurotractin/kilon promotes neurite outgrowth and is expressed on reactive astrocytes after entorhinal cortex lesion. Mol. Cell Neurosci. 2005, 29, 580-590.
    • (2005) Mol. Cell Neurosci. , vol.29 , pp. 580-590
    • Schafer, M.1    Brauer, A.U.2    Savaskan, N.E.3    Rathjen, F.G.4    Brummendorf, T.5
  • 39
    • 84934438018 scopus 로고    scopus 로고
    • Quantitative protein profiling by mass spectrometry using isotope-coded affinity tags
    • Haqqani, A. S., Kelly, J. F., Stanimirovic, D. B., Quantitative protein profiling by mass spectrometry using isotope-coded affinity tags. Methods Mol. Biol. 2008, 439, 225-240.
    • (2008) Methods Mol. Biol. , vol.439 , pp. 225-240
    • Haqqani, A.S.1    Kelly, J.F.2    Stanimirovic, D.B.3
  • 40
    • 0027286502 scopus 로고
    • MASCOT: Multiple alignment system for protein sequences based on three-way dynamic programming
    • Hirosawa, M., Hoshida, M., Ishikawa, M., Toya, T., MASCOT: multiple alignment system for protein sequences based on three-way dynamic programming. Comput. Appl. Biosci. 1993, 9, 161-167. (Pubitemid 23127138)
    • (1993) Computer Applications in the Biosciences , vol.9 , Issue.2 , pp. 161-167
    • Hirosawa, M.1    Hoshida, M.2    Ishikawa, M.3    Toya, T.4
  • 41
    • 0037277179 scopus 로고    scopus 로고
    • Evaluation of multidimensional chromatography coupled with tandem mass spectrometry (LC/LC-MS/MS) for large-scale protein analysis: The yeast proteome
    • Peng, J., Elias, J. E., Thoreen, C. C., Licklider, L. J., Gygi, S. P., Evaluation of multidimensional chromatography coupled with tandem mass spectrometry (LC/LC-MS/MS) for large-scale protein analysis: the yeast proteome. J. Proteome Res. 2003, 2, 43-50.
    • (2003) J. Proteome Res. , vol.2 , pp. 43-50
    • Peng, J.1    Elias, J.E.2    Thoreen, C.C.3    Licklider, L.J.4    Gygi, S.P.5
  • 42
    • 0033215252 scopus 로고    scopus 로고
    • "Apoptotic" biochemical cascades in synaptic compartments: Roles in adaptive plasticity and neurodegenerative disorders
    • Mattson, M. P., Duan, W., "Apoptotic" biochemical cascades in synaptic compartments: roles in adaptive plasticity and neurodegenerative disorders. J. Neurosci. Res. 1999, 58, 152-166.
    • (1999) J. Neurosci. Res. , vol.58 , pp. 152-166
    • Mattson, M.P.1    Duan, W.2
  • 43
    • 27744495926 scopus 로고    scopus 로고
    • The neuronal death protein par-4 mediates dopaminergic synaptic plasticity
    • Mattson, M. P., Gleichmann, M., The neuronal death protein par-4 mediates dopaminergic synaptic plasticity. Mol. Interv. 2005, 5, 278-281.
    • (2005) Mol. Interv. , vol.5 , pp. 278-281
    • Mattson, M.P.1    Gleichmann, M.2
  • 44
    • 3342980580 scopus 로고    scopus 로고
    • The kinder side of killer proteases: Caspase activation contributes to neuroprotection and CNS remodeling
    • DOI 10.1023/B:APPT.0000018793.10779.dc
    • McLaughlin, B., The kinder side of killer proteases: caspase activation contributes to neuroprotection and CNS remodeling. Apoptosis 2004, 9, 111-121. (Pubitemid 38987588)
    • (2004) Apoptosis , vol.9 , Issue.2 , pp. 111-121
    • McLaughlin, B.1
  • 46
    • 0141994809 scopus 로고    scopus 로고
    • DNA microarray analysis of hippocampal gene expression measured twelve hours after hypoxia-ischemia in the mouse
    • Gilbert, R. W., Costain, W. J., Blanchard, M. E., Mullen, K. L. et al., DNA microarray analysis of hippocampal gene expression measured twelve hours after hypoxia-ischemia in the mouse. J. Cereb. Blood Flow Metab. 2003, 23, 1195-1211.
    • (2003) J. Cereb. Blood Flow Metab. , vol.23 , pp. 1195-1211
    • Gilbert, R.W.1    Costain, W.J.2    Blanchard, M.E.3    Mullen, K.L.4
  • 47
    • 2642587489 scopus 로고    scopus 로고
    • Translation-state analysis of gene expression in mouse brain after focal ischemia
    • MacManus, J. P., Graber, T., Luebbert, C., Preston, E. et al., Translation-state analysis of gene expression in mouse brain after focal ischemia. J. Cereb. Blood Flow Metab. 2004, 24, 657-667.
    • (2004) J. Cereb. Blood Flow Metab. , vol.24 , pp. 657-667
    • MacManus, J.P.1    Graber, T.2    Luebbert, C.3    Preston, E.4
  • 48
    • 0034524665 scopus 로고    scopus 로고
    • The pathogenic activation of calpain: A marker and mediator of cellular toxicity and disease states
    • Vanderklish, P. W., Bahr, B. A., The pathogenic activation of calpain: a marker and mediator of cellular toxicity and disease states. Int. J. Exp. Pathol. 2000, 81, 323-339.
    • (2000) Int. J. Exp. Pathol. , vol.81 , pp. 323-339
    • Vanderklish, P.W.1    Bahr, B.A.2
  • 49
    • 0035408169 scopus 로고    scopus 로고
    • The lysosomal protease cathepsin D mediates apoptosis induced by oxidative stress
    • Kagedal, K., Johansson, U., Ollinger, K., The lysosomal protease cathepsin D mediates apoptosis induced by oxidative stress. FASEB J. 2001, 15, 1592-1594.
    • (2001) FASEB J. , vol.15 , pp. 1592-1594
    • Kagedal, K.1    Johansson, U.2    Ollinger, K.3
  • 50
    • 0036167612 scopus 로고    scopus 로고
    • Molecular pathways of protein synthesis inhibition during brain reperfusion: Implications for neuronal survival or death
    • DeGracia, D. J., Kumar, R., Owen, C. R., Krause, G. S., White, B. C., Molecular pathways of protein synthesis inhibition during brain reperfusion: implications for neuronal survival or death. J. Cereb. Blood Flow Metab. 2002, 22, 127-141. (Pubitemid 34135644)
    • (2002) Journal of Cerebral Blood Flow and Metabolism , vol.22 , Issue.2 , pp. 127-141
    • DeGracia, D.J.1    Kumar, R.2    Owen, C.R.3    Krause, G.S.4    White, B.C.5
  • 51
    • 36448993027 scopus 로고    scopus 로고
    • Protein aggregation and proteasome dysfunction after brain ischemia
    • Ge, P., Luo, Y., Liu, C. L., Hu, B., Protein aggregation and proteasome dysfunction after brain ischemia. Stroke 2007, 38, 3230-3236.
    • (2007) Stroke , vol.38 , pp. 3230-3236
    • Ge, P.1    Luo, Y.2    Liu, C.L.3    Hu, B.4
  • 52
    • 27144446140 scopus 로고    scopus 로고
    • Akt contributes to neuroprotection by hypothermia against cerebral ischemia in rats
    • Zhao, H., Shimohata, T., Wang, J. Q., Sun, G. et al., Akt contributes to neuroprotection by hypothermia against cerebral ischemia in rats. J. Neurosci. 2005, 25, 9794-9806.
    • (2005) J. Neurosci. , vol.25 , pp. 9794-9806
    • Zhao, H.1    Shimohata, T.2    Wang, J.Q.3    Sun, G.4
  • 53
    • 84934444912 scopus 로고    scopus 로고
    • Quantitative protein profiling by mass spectrometry using label-free proteomics
    • Haqqani, A. S., Kelly, J. F., Stanimirovic, D. B., Quantitative protein profiling by mass spectrometry using label-free proteomics. Methods Mol. Biol. 2008, 439, 241-256.
    • (2008) Methods Mol. Biol. , vol.439 , pp. 241-256
    • Haqqani, A.S.1    Kelly, J.F.2    Stanimirovic, D.B.3
  • 54
    • 33646811861 scopus 로고    scopus 로고
    • Mitochondrial membrane potential and ischemic neuronal death
    • DOI 10.1016/j.neures.2006.04.005, PII S0168010206000873
    • Iijima, T., Mitochondrial membrane potential and ischemic neuronal death. Neurosci. Res. 2006, 55, 234-243. (Pubitemid 43766411)
    • (2006) Neuroscience Research , vol.55 , Issue.3 , pp. 234-243
    • Iijima, T.1
  • 55
    • 34247485841 scopus 로고    scopus 로고
    • Role of the mitochondrial membrane permeability transition in cell death
    • Tsujimoto, Y., Shimizu, S., Role of the mitochondrial membrane permeability transition in cell death. Apoptosis 2007, 12, 835-840.
    • (2007) Apoptosis , vol.12 , pp. 835-840
    • Tsujimoto, Y.1    Shimizu, S.2
  • 56
    • 34247279899 scopus 로고    scopus 로고
    • Hypoxia affects the physiological behavior of rat cortical synaptosomes
    • Aldinucci, C., Carretta, A., Ciccoli, L., Leoncini, S. et al., Hypoxia affects the physiological behavior of rat cortical synaptosomes. Free Radic. Biol. Med. 2007, 42, 1749-1756.
    • (2007) Free Radic. Biol. Med. , vol.42 , pp. 1749-1756
    • Aldinucci, C.1    Carretta, A.2    Ciccoli, L.3    Leoncini, S.4
  • 57
    • 33744964144 scopus 로고    scopus 로고
    • Synaptic mitochondria are more susceptible to Ca2+overload than nonsynaptic mitochondria
    • Brown, M. R., Sullivan, P. G., Geddes, J. W., Synaptic mitochondria are more susceptible to Ca2+overload than nonsynaptic mitochondria. J. Biol. Chem. 2006, 281, 11658-11668.
    • (2006) J. Biol. Chem. , vol.281 , pp. 11658-11668
    • Brown, M.R.1    Sullivan, P.G.2    Geddes, J.W.3
  • 58
    • 0033780693 scopus 로고    scopus 로고
    • Delayed neuronal death
    • Kirino, T., Delayed neuronal death. Neuropathology 2000, 20, S95-97.
    • (2000) Neuropathology , vol.20
    • Kirino, T.1
  • 59
    • 33646572879 scopus 로고    scopus 로고
    • DNA microarray analysis of striatal gene expression in symptomatic transgenic Huntington's mice (R6/2) reveals neuroinflammation and insulin associations
    • Crocker, S. F., Costain, W. J., Robertson, H. A., DNA microarray analysis of striatal gene expression in symptomatic transgenic Huntington's mice (R6/2) reveals neuroinflammation and insulin associations. Brain Res. 2006, 1088, 176-186.
    • (2006) Brain Res. , vol.1088 , pp. 176-186
    • Crocker, S.F.1    Costain, W.J.2    Robertson, H.A.3
  • 60
    • 9144228118 scopus 로고    scopus 로고
    • Purified recombinant human prosaposin forms oligomers that bind procathepsin D and affect its autoactivation
    • Gopalakrishnan, M. M., Grosch, H. W., Locatelli-Hoops, S., Werth, N. et al., Purified recombinant human prosaposin forms oligomers that bind procathepsin D and affect its autoactivation. Biochem. J. 2004, 383, 507-515.
    • (2004) Biochem. J. , vol.383 , pp. 507-515
    • Gopalakrishnan, M.M.1    Grosch, H.W.2    Locatelli-Hoops, S.3    Werth, N.4
  • 61
    • 19244385377 scopus 로고    scopus 로고
    • Lysosomal proteolysis of prosaposin, the precursor of saposins (sphingolipid activator proteins): Its mechanism and inhibition by ganglioside
    • Hiraiwa, M., Martin, B. M., Kishimoto, Y., Conner, G. E. et al., Lysosomal proteolysis of prosaposin, the precursor of saposins (sphingolipid activator proteins): its mechanism and inhibition by ganglioside. Arch. Biochem. Biophys. 1997, 341, 17-24.
    • (1997) Arch. Biochem. Biophys. , vol.341 , pp. 17-24
    • Hiraiwa, M.1    Martin, B.M.2    Kishimoto, Y.3    Conner, G.E.4
  • 62
    • 34447294548 scopus 로고    scopus 로고
    • Combined saposin C and D deficiencies in mice lead to a neuronopathic phenotype, glucosylceramide and alpha-hydroxy ceramide accumulation, and altered prosaposin trafficking
    • Sun, Y., Witte, D. P., Zamzow, M., Ran, H. et al., Combined saposin C and D deficiencies in mice lead to a neuronopathic phenotype, glucosylceramide and alpha-hydroxy ceramide accumulation, and altered prosaposin trafficking. Hum. Mol. Genet. 2007, 16, 957-971.
    • (2007) Hum. Mol. Genet. , vol.16 , pp. 957-971
    • Sun, Y.1    Witte, D.P.2    Zamzow, M.3    Ran, H.4
  • 63
    • 0031769454 scopus 로고    scopus 로고
    • Colocalization and complex formation between prosaposin and monosialoganglioside GM3 in neural cells
    • Misasi, R., Sorice, M., Garofalo, T., Griggi, T. et al., Colocalization and complex formation between prosaposin and monosialoganglioside GM3 in neural cells. J. Neurochem. 1998, 71, 2313-2321.
    • (1998) J. Neurochem. , vol.71 , pp. 2313-2321
    • Misasi, R.1    Sorice, M.2    Garofalo, T.3    Griggi, T.4
  • 64
    • 0028402219 scopus 로고
    • Occurrence of prosaposin as a neuronal surface membrane component
    • Fu, Q., Carson, G. S., Hiraiwa, M., Grafe, M. et al., Occurrence of prosaposin as a neuronal surface membrane component. J. Mol. Neurosci. 1994, 5, 59-67.
    • (1994) J. Mol. Neurosci. , vol.5 , pp. 59-67
    • Fu, Q.1    Carson, G.S.2    Hiraiwa, M.3    Grafe, M.4
  • 66
    • 0029013931 scopus 로고
    • Identification of the neurotrophic factor sequence of prosaposin
    • O'Brien, J. S., Carson, G. S., Seo, H. C., Hiraiwa, M. et al., Identification of the neurotrophic factor sequence of prosaposin. FASEB J. 1995, 9, 681-685.
    • (1995) FASEB J. , vol.9 , pp. 681-685
    • O'Brien, J.S.1    Carson, G.S.2    Seo, H.C.3    Hiraiwa, M.4
  • 67
  • 68
    • 0030971534 scopus 로고    scopus 로고
    • Cell death prevention, mitogen-activated protein kinase stimulation, and increased sulfatide concentrations in Schwann cells and oligodendrocytes by prosaposin and prosaptides
    • Hiraiwa, M., Taylor, E. M., Campana, W. M., Darin, S. J., O'Brien, J. S., Cell death prevention, mitogen-activated protein kinase stimulation, and increased sulfatide concentrations in Schwann cells and oligodendrocytes by prosaposin and prosaptides. Proc. Natl. Acad. Sci. USA 1997, 94, 4778-4781.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 4778-4781
    • Hiraiwa, M.1    Taylor, E.M.2    Campana, W.M.3    Darin, S.J.4    O'Brien, J.S.5
  • 69
    • 0032190625 scopus 로고    scopus 로고
    • Prosaposin prevents programmed cell death of rat cerebellar granule neurons in culture
    • Tsuboi, K., Hiraiwa, M., O'Brien, J. S., Prosaposin prevents programmed cell death of rat cerebellar granule neurons in culture. Brain Res. Dev. Brain Res. 1998, 110, 249-255.
    • (1998) Brain Res. Dev. Brain Res. , vol.110 , pp. 249-255
    • Tsuboi, K.1    Hiraiwa, M.2    O'Brien, J.S.3
  • 70
    • 0043023931 scopus 로고    scopus 로고
    • Regulation of gene expression in response to brain injury: Enhanced expression and alternative splicing of rat prosaposin (SGP-1) mRNA in injured brain
    • Hiraiwa, M., Liu, J., Lu, A. G., Wang, C. Y. et al., Regulation of gene expression in response to brain injury: enhanced expression and alternative splicing of rat prosaposin (SGP-1) mRNA in injured brain. J. Neurotrauma 2003, 20, 755-765.
    • (2003) J. Neurotrauma , vol.20 , pp. 755-765
    • Hiraiwa, M.1    Liu, J.2    Lu, A.G.3    Wang, C.Y.4
  • 71
    • 0027272548 scopus 로고
    • Transient forebrain ischemia induces increased expression and specific localization of cathepsins e and D in rat hippocampus and neonstriatum
    • DOI 10.1006/exnr.1993.1088
    • Nakanishi, H., Tsukuba, T., Kondou, T., Tanaka, T., Yamamoto, K., Transient forebrain ischemia induces increased expression and specific localization of cathepsins E and D in rat hippocampus and neostriatum. Exp. Neurol. 1993, 121, 215-223. (Pubitemid 23234740)
    • (1993) Experimental Neurology , vol.121 , Issue.2 , pp. 215-223
    • Nakanishi, H.1    Tsukuba, T.2    Kondou, T.3    Tanaka, T.4    Yamamoto, K.5
  • 72
    • 33644658460 scopus 로고    scopus 로고
    • Oxidative stress and lysosomes: CNS-related consequences and implications for lysosomal enhancement strategies and induction of autophagy
    • Butler, D., Bahr, B. A., Oxidative stress and lysosomes: CNS-related consequences and implications for lysosomal enhancement strategies and induction of autophagy. Antioxid. Redox Signal. 2006, 8, 185-196.
    • (2006) Antioxid. Redox Signal. , vol.8 , pp. 185-196
    • Butler, D.1    Bahr, B.A.2
  • 74
    • 0028924890 scopus 로고
    • Delayed neuronal death in the CA1 pyramidal cell layer of the gerbil hippocampus following transient ischemia is apoptosis
    • Nitatori, T., Sato, N., Waguri, S., Karasawa, Y. et al., Delayed neuronal death in the CA1 pyramidal cell layer of the gerbil hippocampus following transient ischemia is apoptosis. J. Neurosci. 1995, 15, 1001-1011.
    • (1995) J. Neurosci. , vol.15 , pp. 1001-1011
    • Nitatori, T.1    Sato, N.2    Waguri, S.3    Karasawa, Y.4
  • 75
    • 33746637534 scopus 로고    scopus 로고
    • Cerebral ischemia-hypoxia induces intravascular coagulation and autophagy
    • Adhami, F., Liao, G., Morozov, Y. M., Schloemer, A. et al., Cerebral ischemia-hypoxia induces intravascular coagulation and autophagy. Am. J. Pathol. 2006, 169, 566-583.
    • (2006) Am. J. Pathol. , vol.169 , pp. 566-583
    • Adhami, F.1    Liao, G.2    Morozov, Y.M.3    Schloemer, A.4
  • 76
    • 0034608343 scopus 로고    scopus 로고
    • Neuroprotective effect of retro-inverso Prosaptide D5 on focal cerebral ischemia in rat
    • Lu, A. G., Otero, D. A., Hiraiwa, M., O'Brien, J. S., Neuroprotective effect of retro-inverso Prosaptide D5 on focal cerebral ischemia in rat. Neuroreport 2000, 11, 1791-1794.
    • (2000) Neuroreport , vol.11 , pp. 1791-1794
    • Lu, A.G.1    Otero, D.A.2    Hiraiwa, M.3    O'Brien, J.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.