메뉴 건너뛰기




Volumn 37, Issue 5, 2011, Pages 484-499

Neuropathological changes correlate temporally but not spatially with selected neuromodulatory responses in natural scrapie

Author keywords

Neuromodulation; Neuropathology; Preclinical; Prion; Sheep; Transmissible spongiform encephalopathy

Indexed keywords

ADENOSINE A1 RECEPTOR; ADENYLATE CYCLASE; ADENYLATE CYCLASE 1; METABOTROPIC RECEPTOR 1; PARVALBUMIN; PHOSPHOLIPASE C BETA1; SYNAPTOPHYSIN; UNCLASSIFIED DRUG;

EID: 79960259700     PISSN: 03051846     EISSN: 13652990     Source Type: Journal    
DOI: 10.1111/j.1365-2990.2010.01152.x     Document Type: Article
Times cited : (3)

References (57)
  • 1
    • 0002975117 scopus 로고    scopus 로고
    • The prion diseases of humans and animals
    • Eds RN Rosenber, SB Prusiner, S DiMauro, RL Barchi. Boston, MA: Butterworth-Heinemann
    • Prusiner SB. The prion diseases of humans and animals. In The Molecular and Genetic Basis of Neurological Diseases. Eds RN Rosenber, SB Prusiner, S DiMauro, RL Barchi. Boston, MA: Butterworth-Heinemann, 1997; 165-86.
    • (1997) The Molecular and Genetic Basis of Neurological Diseases , pp. 165-186
    • Prusiner, S.B.1
  • 7
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • Prusiner SB. Novel proteinaceous infectious particles cause scrapie. Science 1982; 216: 136-44.
    • (1982) Science , vol.216 , pp. 136-144
    • Prusiner, S.B.1
  • 8
    • 0003035152 scopus 로고    scopus 로고
    • Neuropathology of prion diseases
    • Ed. SB Prusiner. New York: Cold Spring Harbor Laboratory Press
    • DeArmond SJ, Ironside JW. Neuropathology of prion diseases. In Prion Biology and Diseases. Ed. SB Prusiner. New York: Cold Spring Harbor Laboratory Press, 1999; 585-652.
    • (1999) Prion Biology and Diseases , pp. 585-652
    • DeArmond, S.J.1    Ironside, J.W.2
  • 9
    • 34447132913 scopus 로고    scopus 로고
    • Classical sheep transmissible spongiform encephalopathies: pathogenesis, pathological phenotypes and clinical disease
    • Jeffrey M, González L. Classical sheep transmissible spongiform encephalopathies: pathogenesis, pathological phenotypes and clinical disease. Neuropathol Appl Neurobiol 2007; 33: 373-94.
    • (2007) Neuropathol Appl Neurobiol , vol.33 , pp. 373-394
    • Jeffrey, M.1    González, L.2
  • 10
    • 65349151298 scopus 로고    scopus 로고
    • Neuroinvasion in sheep transmissible spongiform encephalopathies: the role of the haematogenous route
    • Sisó S, Jeffrey M, González L. Neuroinvasion in sheep transmissible spongiform encephalopathies: the role of the haematogenous route. Neuropathol Appl Neurobiol 2009; 35: 232-46.
    • (2009) Neuropathol Appl Neurobiol , vol.35 , pp. 232-246
    • Sisó, S.1    Jeffrey, M.2    González, L.3
  • 11
    • 77953816392 scopus 로고    scopus 로고
    • Pathogenesis of natural goat scrapie: modulation by host PRNP genotype and effect of co-existent conditions
    • González L, Martin S, Hawkins SA, Goldmann W, Jeffrey M, Sisó S. Pathogenesis of natural goat scrapie: modulation by host PRNP genotype and effect of co-existent conditions. Vet Res 2010; 41: 48.
    • (2010) Vet Res , vol.41 , pp. 48
    • González, L.1    Martin, S.2    Hawkins, S.A.3    Goldmann, W.4    Jeffrey, M.5    Sisó, S.6
  • 12
    • 0036620682 scopus 로고    scopus 로고
    • Vacuolar lesion profile in sheep scrapie: factors influencing its variation and relationship to disease-specific PrP accumulation
    • Begara-McGorum I, González L, Simmons M, Hunter N, Houston F, Jeffrey M. Vacuolar lesion profile in sheep scrapie: factors influencing its variation and relationship to disease-specific PrP accumulation. J Comp Pathol 2002; 127: 59-68.
    • (2002) J Comp Pathol , vol.127 , pp. 59-68
    • Begara-McGorum, I.1    González, L.2    Simmons, M.3    Hunter, N.4    Houston, F.5    Jeffrey, M.6
  • 13
    • 0036376780 scopus 로고    scopus 로고
    • Effects of agent strain and host genotype on PrP accumulation in the brain of sheep naturally and experimentally affected with scrapie
    • González L, Martin S, Begara-McGorum I, Hunter N, Houston F, Simmons M, Jeffrey M. Effects of agent strain and host genotype on PrP accumulation in the brain of sheep naturally and experimentally affected with scrapie. J Comp Pathol 2002; 126: 17-29.
    • (2002) J Comp Pathol , vol.126 , pp. 17-29
    • González, L.1    Martin, S.2    Begara-McGorum, I.3    Hunter, N.4    Houston, F.5    Simmons, M.6    Jeffrey, M.7
  • 15
    • 0031729399 scopus 로고    scopus 로고
    • Prion diseases in man
    • Ironside JW. Prion diseases in man. J Pathol 1998; 86: 227-34.
    • (1998) J Pathol , vol.86 , pp. 227-234
    • Ironside, J.W.1
  • 17
    • 0027497306 scopus 로고
    • Parvalbumin-immunoreactive cortical neurons in Creutzfeldt-Jakob disease
    • Ferrer I, Casas R, Rivera R. Parvalbumin-immunoreactive cortical neurons in Creutzfeldt-Jakob disease. Ann Neurol 1993; 34: 864-66.
    • (1993) Ann Neurol , vol.34 , pp. 864-866
    • Ferrer, I.1    Casas, R.2    Rivera, R.3
  • 18
    • 0030929562 scopus 로고    scopus 로고
    • Distribution of parvalbumin-immunoreactive neurons in brain correlates with hippocampal and temporal cortical pathology in Creutzfeldt-Jakob disease
    • Guentchev M, Hainfellner JA, Trabattoni GR, Budka H. Distribution of parvalbumin-immunoreactive neurons in brain correlates with hippocampal and temporal cortical pathology in Creutzfeldt-Jakob disease. J Neuropathol Exp Neurol 1997; 56: 1119-24.
    • (1997) J Neuropathol Exp Neurol , vol.56 , pp. 1119-1124
    • Guentchev, M.1    Hainfellner, J.A.2    Trabattoni, G.R.3    Budka, H.4
  • 19
    • 0032885694 scopus 로고    scopus 로고
    • Early destruction of the extracellular matrix around parvalbumin-immunoreactive interneurons in Creutzfeldt-Jakob disease
    • Belichenko PV, Miklossy J, Belser B, Budka H, Celio MR. Early destruction of the extracellular matrix around parvalbumin-immunoreactive interneurons in Creutzfeldt-Jakob disease. Neurobiol Dis 1999; 6: 269-79.
    • (1999) Neurobiol Dis , vol.6 , pp. 269-279
    • Belichenko, P.V.1    Miklossy, J.2    Belser, B.3    Budka, H.4    Celio, M.R.5
  • 20
    • 0031661397 scopus 로고    scopus 로고
    • Severe, early and selective loss of a subpopulation of GABAergic inhibitory neurons in experimental transmissible spongiform encephalopathies
    • Guentchev M, Groschup MH, Kordek R, Liberski PP, Budka H. Severe, early and selective loss of a subpopulation of GABAergic inhibitory neurons in experimental transmissible spongiform encephalopathies. Brain Pathol 1998; 8: 615-23.
    • (1998) Brain Pathol , vol.8 , pp. 615-623
    • Guentchev, M.1    Groschup, M.H.2    Kordek, R.3    Liberski, P.P.4    Budka, H.5
  • 21
    • 33745883252 scopus 로고    scopus 로고
    • Assessment of calcium-binding proteins (Parvalbumin and Calbindin D-28K) and perineuronal nets in normal and scrapie-affected adult sheep brains
    • Vidal E, Bolea R, Tortosa R, Costa C, Domènech A, Monleón E, Vargas A, Badiola JJ, Pumarola M. Assessment of calcium-binding proteins (Parvalbumin and Calbindin D-28K) and perineuronal nets in normal and scrapie-affected adult sheep brains. J Virol Methods 2006; 136: 137-46.
    • (2006) J Virol Methods , vol.136 , pp. 137-146
    • Vidal, E.1    Bolea, R.2    Tortosa, R.3    Costa, C.4    Domènech, A.5    Monleón, E.6    Vargas, A.7    Badiola, J.J.8    Pumarola, M.9
  • 22
    • 0035013510 scopus 로고    scopus 로고
    • Prion-induced neuronal damage: the mechanisms of neuronal destruction in the subacute spongiform encephalopathies
    • Giese A, Kretzschmar HA. Prion-induced neuronal damage: the mechanisms of neuronal destruction in the subacute spongiform encephalopathies. Curr Top Microbiol Immunol 2001; 253: 203-17.
    • (2001) Curr Top Microbiol Immunol , vol.253 , pp. 203-217
    • Giese, A.1    Kretzschmar, H.A.2
  • 24
    • 0028949460 scopus 로고
    • Early unsuspected neuron and axon terminal loss in scrapie-infected mice revealed by morphometry and immunohistochemistry
    • Jeffrey M, Fraser JR, Halliday BWG, Fowler N, Goodsir CM, Brown DA. Early unsuspected neuron and axon terminal loss in scrapie-infected mice revealed by morphometry and immunohistochemistry. Neuropathol Appl Neurobiol 1995; 21: 41-9.
    • (1995) Neuropathol Appl Neurobiol , vol.21 , pp. 41-49
    • Jeffrey, M.1    Fraser, J.R.2    Halliday, B.W.G.3    Fowler, N.4    Goodsir, C.M.5    Brown, D.A.6
  • 26
    • 73549119497 scopus 로고    scopus 로고
    • Degenerating synaptic boutons in prion disease
    • Siskova Z, Page A, O'Connor V, Perry VH. Degenerating synaptic boutons in prion disease. Am J Pathol 2009; 175: 1610-21.
    • (2009) Am J Pathol , vol.175 , pp. 1610-1621
    • Siskova, Z.1    Page, A.2    O'Connor, V.3    Perry, V.H.4
  • 27
    • 67349280983 scopus 로고    scopus 로고
    • Selective presynaptic degeneration in the synaptopathy associated with ME7-induced hippocampal pathology
    • Gray BC, Siskova Z, Perry VH, O'Connor V. Selective presynaptic degeneration in the synaptopathy associated with ME7-induced hippocampal pathology. Neurobiol Dis 2009; 35: 63-74.
    • (2009) Neurobiol Dis , vol.35 , pp. 63-74
    • Gray, B.C.1    Siskova, Z.2    Perry, V.H.3    O'Connor, V.4
  • 28
    • 0019394488 scopus 로고
    • Golgi and electronmicroscopic studies of spongiform encephalopathies
    • Landis DM, Williams RS, Masters CL. Golgi and electronmicroscopic studies of spongiform encephalopathies. Neurology 1981; 31: 538-49.
    • (1981) Neurology , vol.31 , pp. 538-549
    • Landis, D.M.1    Williams, R.S.2    Masters, C.L.3
  • 30
    • 0025330884 scopus 로고
    • Neuronal alterations in patients with dementia: a Golgi study on biopsy samples
    • Ferrer I, Guionnet N, Cruz-Sánchez F, Tuñón T. Neuronal alterations in patients with dementia: a Golgi study on biopsy samples. Neurosci Lett 1990; 114: 11-16.
    • (1990) Neurosci Lett , vol.114 , pp. 11-16
    • Ferrer, I.1    Guionnet, N.2    Cruz-Sánchez, F.3    Tuñón, T.4
  • 31
    • 0027394220 scopus 로고
    • Synaptic degeneration is the primary neuropathological feature in prion diseases: a preliminary study
    • Clinton J, Forsyth C, Royston MC, Roberts GW. Synaptic degeneration is the primary neuropathological feature in prion diseases: a preliminary study. Neuroreport 1993; 4: 65-8.
    • (1993) Neuroreport , vol.4 , pp. 65-68
    • Clinton, J.1    Forsyth, C.2    Royston, M.C.3    Roberts, G.W.4
  • 32
    • 0032949115 scopus 로고    scopus 로고
    • Expression of proteins linked to exocytosis and neurotransmission in patients with Creutzfeldt-Jakob disease
    • Ferrer I, Rivera R, Blanco R, Martí E. Expression of proteins linked to exocytosis and neurotransmission in patients with Creutzfeldt-Jakob disease. Neurobiol Dis 1999; 6: 92-100.
    • (1999) Neurobiol Dis , vol.6 , pp. 92-100
    • Ferrer, I.1    Rivera, R.2    Blanco, R.3    Martí, E.4
  • 33
    • 0034109081 scopus 로고    scopus 로고
    • Prion protein deposition and abnormal synaptic protein expression in the cerebellum in Creutzfeldt-Jakob disease
    • Ferrer I, Puig B, Blanco R, Martí E. Prion protein deposition and abnormal synaptic protein expression in the cerebellum in Creutzfeldt-Jakob disease. Neuroscience 2000; 97: 715-26.
    • (2000) Neuroscience , vol.97 , pp. 715-726
    • Ferrer, I.1    Puig, B.2    Blanco, R.3    Martí, E.4
  • 34
    • 0142125765 scopus 로고    scopus 로고
    • A receptors in Creutzfeldt-Jakob disease
    • A receptors in Creutzfeldt-Jakob disease. Acta Neuropathol 2003; 106: 311-18.
    • (2003) Acta Neuropathol , vol.106 , pp. 311-318
    • Ferrer, I.1    Puig, B.2
  • 35
    • 0042734442 scopus 로고    scopus 로고
    • Synaptic pathology and cell death in the cerebellum in Creutzfeldt-Jakob disease
    • Ferrer I. Synaptic pathology and cell death in the cerebellum in Creutzfeldt-Jakob disease. Cerebellum 2002; 1: 213-22.
    • (2002) Cerebellum , vol.1 , pp. 213-222
    • Ferrer, I.1
  • 36
    • 14644427216 scopus 로고    scopus 로고
    • Metabotropic glutamate receptor/phospholipase C pathway: a vulnerable target to Creutzfeldt-Jakob disease in the cerebral cortex
    • Rodríguez A, Freixes M, Dalfó E, Martín M, Puig B, Ferrer I. Metabotropic glutamate receptor/phospholipase C pathway: a vulnerable target to Creutzfeldt-Jakob disease in the cerebral cortex. Neuroscience 2005; 131: 825-32.
    • (2005) Neuroscience , vol.131 , pp. 825-832
    • Rodríguez, A.1    Freixes, M.2    Dalfó, E.3    Martín, M.4    Puig, B.5    Ferrer, I.6
  • 38
    • 0034934355 scopus 로고    scopus 로고
    • Onset and distribution of tissue PrP accumulation in scrapie-affected Suffolk sheep as demonstrated by sequential necropsies and tonsillar biopsies
    • Jeffrey M, Martin S, Thomson JR, Dingwall WS, Begara-McGorum I, González L. Onset and distribution of tissue PrP accumulation in scrapie-affected Suffolk sheep as demonstrated by sequential necropsies and tonsillar biopsies. J Comp Pathol 2001; 125: 48-57.
    • (2001) J Comp Pathol , vol.125 , pp. 48-57
    • Jeffrey, M.1    Martin, S.2    Thomson, J.R.3    Dingwall, W.S.4    Begara-McGorum, I.5    González, L.6
  • 39
    • 42449113378 scopus 로고    scopus 로고
    • Diagnosis of preclinical scrapie in live sheep by the immunohistochemical examination of rectal biopsies
    • González L, Dagleish MP, Martin S, Dexter G, Steele P, Finlayson J, Jeffrey M. Diagnosis of preclinical scrapie in live sheep by the immunohistochemical examination of rectal biopsies. Vet Rec 2008; 162: 397-403.
    • (2008) Vet Rec , vol.162 , pp. 397-403
    • González, L.1    Dagleish, M.P.2    Martin, S.3    Dexter, G.4    Steele, P.5    Finlayson, J.6    Jeffrey, M.7
  • 40
    • 14744289958 scopus 로고    scopus 로고
    • Phenotype of disease-associated PrP accumulation in the brain of bovine spongiform encephalopathy experimentally infected sheep
    • González L, Martin S, Houston FE, Hunter N, Reid HW, Bellworthy SJ, Jeffrey M. Phenotype of disease-associated PrP accumulation in the brain of bovine spongiform encephalopathy experimentally infected sheep. J Gen Virol 2005; 86: 827-38.
    • (2005) J Gen Virol , vol.86 , pp. 827-838
    • González, L.1    Martin, S.2    Houston, F.E.3    Hunter, N.4    Reid, H.W.5    Bellworthy, S.J.6    Jeffrey, M.7
  • 41
    • 34250796207 scopus 로고    scopus 로고
    • Actin-binding proteins coronin-1a and IBA-1 are effective microglial markers for immunohistochemistry
    • Ahmed Z, Shaw G, Sharma VP, Yang C, McGowan E, Dickson DW. Actin-binding proteins coronin-1a and IBA-1 are effective microglial markers for immunohistochemistry. J Histochem Cytochem 2007; 55: 687-700.
    • (2007) J Histochem Cytochem , vol.55 , pp. 687-700
    • Ahmed, Z.1    Shaw, G.2    Sharma, V.P.3    Yang, C.4    McGowan, E.5    Dickson, D.W.6
  • 42
    • 12244258260 scopus 로고    scopus 로고
    • Abnormal neuronal expression of the calcium-binding proteins, parvalbumin and calbindin D-28k, in aged dogs
    • Sisó S, Tort S, Aparici C, Pérez L, Vidal E, Pumarola M. Abnormal neuronal expression of the calcium-binding proteins, parvalbumin and calbindin D-28k, in aged dogs. J Comp Pathol 2003; 128: 9-14.
    • (2003) J Comp Pathol , vol.128 , pp. 9-14
    • Sisó, S.1    Tort, S.2    Aparici, C.3    Pérez, L.4    Vidal, E.5    Pumarola, M.6
  • 45
    • 0016905630 scopus 로고
    • The pathology of natural and experimental scrapie
    • Fraser H. The pathology of natural and experimental scrapie. Front Biol 1976; 44: 267-305.
    • (1976) Front Biol , vol.44 , pp. 267-305
    • Fraser, H.1
  • 47
    • 0034746485 scopus 로고    scopus 로고
    • Onset of accumulation of PrPres in murine ME7 scrapie in relation to pathological and PrP immunohistochemical changes
    • Jeffrey M, Martin S, Barr J, Chong A, Fraser JR. Onset of accumulation of PrPres in murine ME7 scrapie in relation to pathological and PrP immunohistochemical changes. J Comp Pathol 2001; 124: 20-8.
    • (2001) J Comp Pathol , vol.124 , pp. 20-28
    • Jeffrey, M.1    Martin, S.2    Barr, J.3    Chong, A.4    Fraser, J.R.5
  • 49
    • 0037847400 scopus 로고    scopus 로고
    • d immunoreactivity in the brain of scrapie- and BSE-infected sheep: implications for differential cell targeting and PrP processing
    • d immunoreactivity in the brain of scrapie- and BSE-infected sheep: implications for differential cell targeting and PrP processing. J Gen Virol 2003; 84: 1339-50.
    • (2003) J Gen Virol , vol.84 , pp. 1339-1350
    • González, L.1    Martin, S.2    Jeffrey, M.3
  • 50
  • 51
    • 0037744773 scopus 로고    scopus 로고
    • Sub-cellular pathology of scrapie: coated pits are increased in PrP codon 136 alanine homozygous scrapie-affected sheep
    • Ersdal C, Simmons MM, Goodsir C, Martin S, Jeffrey M. Sub-cellular pathology of scrapie: coated pits are increased in PrP codon 136 alanine homozygous scrapie-affected sheep. Acta Neuropathol 2003; 103: 17-28.
    • (2003) Acta Neuropathol , vol.103 , pp. 17-28
    • Ersdal, C.1    Simmons, M.M.2    Goodsir, C.3    Martin, S.4    Jeffrey, M.5
  • 52
    • 0027447304 scopus 로고
    • Calcium-binding proteins: selective markers of nerve cells
    • Andressen C, Blümcke I, Celio MR. Calcium-binding proteins: selective markers of nerve cells. Cell Tissue Res 1993; 271: 181-208.
    • (1993) Cell Tissue Res , vol.271 , pp. 181-208
    • Andressen, C.1    Blümcke, I.2    Celio, M.R.3
  • 56
    • 33749493534 scopus 로고    scopus 로고
    • Adenosine A1 receptor protein levels and activity is increased in the cerebral cortex in Creutzfeldt-Jakob disease and in bovine spongiform encephalopathy-infected bovine-PrP mice
    • Rodríguez A, Martín M, Albasanz JL, Barrachina M, Espinosa JC, Torres JM, Ferrer I. Adenosine A1 receptor protein levels and activity is increased in the cerebral cortex in Creutzfeldt-Jakob disease and in bovine spongiform encephalopathy-infected bovine-PrP mice. J Neuropathol Exp Neurol 2006; 65: 964-75.
    • (2006) J Neuropathol Exp Neurol , vol.65 , pp. 964-975
    • Rodríguez, A.1    Martín, M.2    Albasanz, J.L.3    Barrachina, M.4    Espinosa, J.C.5    Torres, J.M.6    Ferrer, I.7
  • 57
    • 0023882404 scopus 로고
    • How does adenosine inhibit transmitter release?
    • Fredholm BB, Dunwiddie TV. How does adenosine inhibit transmitter release? Trends Pharmacol Sci 1988; 9: 130-4.
    • (1988) Trends Pharmacol Sci , vol.9 , pp. 130-134
    • Fredholm, B.B.1    Dunwiddie, T.V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.