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Titolo:
Immunohistochemical and biochemical studies demonstrate a distinct profileof alpha-synuclein permutations in multiple system atrophy
Autore:
Duda, JE; Giasson, BI; Gur, TL; Montine, TJ; Robertson, D; Biaggioni, I; Hurtig, HI; Stern, MB; Gollomp, SM; Grossman, M; Lee, VMY; Trojanowski, JQ;
Indirizzi:
Univ Penn, Sch Med, Dept Pathol & Lab Med, Ctr Neurodegenerat Dis Res, Philadelphia, PA 19104 USA Univ Penn Philadelphia PA USA 19104 t Dis Res, Philadelphia, PA 19104 USA Univ Penn, Sch Med, Dept Neurol, Philadelphia, PA 19104 USA Univ Penn Philadelphia PA USA 19104 pt Neurol, Philadelphia, PA 19104 USA Vanderbilt Univ, Dept Pathol, Nashville, TN USA Vanderbilt Univ NashvilleTN USA lt Univ, Dept Pathol, Nashville, TN USA Vanderbilt Univ, Auton Dysfunct Ctr, Nashville, TN USA Vanderbilt Univ Nashville TN USA , Auton Dysfunct Ctr, Nashville, TN USA
Titolo Testata:
JOURNAL OF NEUROPATHOLOGY AND EXPERIMENTAL NEUROLOGY
fascicolo: 9, volume: 59, anno: 2000,
pagine: 830 - 841
SICI:
0022-3069(200009)59:9<830:IABSDA>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
SPORADIC PARKINSONS-DISEASE; GLIAL CYTOPLASMIC INCLUSIONS; PERIPHERAL NERVOUS-SYSTEM; LEWY BODIES; NACP/ALPHA-SYNUCLEIN; ALZHEIMERS-DISEASE; NEURODEGENERATIVE DISORDERS; NO MUTATION; GENE; DEMENTIA;
Keywords:
alpha-synuclein; dementia with Lewy bodies; glial cytoplasmic inclusions; Lewy bodies; multiple system atrophy; Parkinson disease; synucleinopathies;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
52
Recensione:
Indirizzi per estratti:
Indirizzo: Trojanowski, JQ Univ Penn, Sch Med, Dept Pathol & Lab Med, Ctr Neurodegenerat Dis Res, 3rdFloor Maloney Bldg, Philadelphia, PA 19104 USA Univ Penn 3rd Floor Maloney Bldg Philadelphia PA USA 19104
Citazione:
J.E. Duda et al., "Immunohistochemical and biochemical studies demonstrate a distinct profileof alpha-synuclein permutations in multiple system atrophy", J NE EXP NE, 59(9), 2000, pp. 830-841

Abstract

Although alpha-synuclein (alpha-syn) has been implicated as a major component of the abnormal filaments that form glial cytoplasmic inclusions (GCIs)in multiple system atrophy (MSA), it is uncertain if GCIs are homogenous and contain full-length alpha-syn. Since this has implications for hypotheses about the pathogenesis of GCIs, we used a novel panel of antibodies to defined regions throughout alpha-syn in immunohistochemical epitope mapping studies of GCIs in MSA brains. Although the immunostaining profile of GCIs with these antibodies was similar for all MSA brains, there were significantdifferences in the immunoreactivity of the alpha-syn epitopes detected in GCIs. Notably, carboxy-terminal alpha-syn epitopes were immunodominant in GCIs, but the entire panel of antibodies immunostained cortical Lewy bodies (LBs) in dementia with LBs brain with similar intensity. While the distribution of alpha-syn labeled GCIs paralleled that previously reported using silver stains, antibodies to carboxy-terminal alpha-syn epitopes revealed a previously undescribed burden of GCIs in the MSA hippocampal formation. Finally, Western blots demonstrated detergent insoluble monomeric and high-molecular weight alpha-syn species in GCI rich MSA cerebellar white matter. Collectively, these data indicate that alpha-syn is a prominent component of GCIs in MSA, and that GCIs and LBs may result from cell type specific conformational or post-translational permutations in alpha-syn.

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Documento generato il 07/07/20 alle ore 12:36:06