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Titolo:
Neuritogenic-neurotoxic effects of membrane-associated forms of amyloid precursor protein
Autore:
Neill, D; Hughes, D; Leake, A; Morris, C; Jones, D; Oakley, A; Edwardson, J; Estibeiro, P;
Indirizzi:
S Tyneside Dist Hosp, S Shields NE34 0PL, Tyne & Wear, England S Tyneside Dist Hosp S Shields Tyne & Wear England NE34 0PL Wear, England Newcastle Gen Hosp, Inst Hlth Elderly, Newcastle Upon Tyne NE4 6BE, Tyne &Wear, England Newcastle Gen Hosp Newcastle Upon Tyne Tyne & Wear England NE4 6BE ngland Univ Edinburgh, Ctr Genome Res, Edinburgh, Midlothian, Scotland Univ Edinburgh Edinburgh Midlothian Scotland burgh, Midlothian, Scotland
Titolo Testata:
DEMENTIA AND GERIATRIC COGNITIVE DISORDERS
fascicolo: 1, volume: 12, anno: 2001,
pagine: 40 - 51
SICI:
1420-8008(200101/02)12:1<40:NEOMFO>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
ALZHEIMERS-DISEASE; BETA-PROTEIN; NEURITE OUTGROWTH; CELL-SURFACE; HIPPOCAMPAL-NEURONS; TERMINAL FRAGMENT; HUMAN-BRAIN; LOCALIZATION; DERIVATIVES; CULTURE;
Keywords:
Alzheimer's disease; synaptoplasticity; neuroblastoma cells; neurotrophism; neurotoxicity;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Clinical Medicine
Life Sciences
Citazioni:
38
Recensione:
Indirizzi per estratti:
Indirizzo: Neill, D S Tyneside Dist Hosp, Harton Lane, S Shields NE34 0PL, Tyne & Wear, England S Tyneside Dist Hosp Harton Lane S Shields Tyne & Wear England NE34 0PL
Citazione:
D. Neill et al., "Neuritogenic-neurotoxic effects of membrane-associated forms of amyloid precursor protein", DEMENT G C, 12(1), 2001, pp. 40-51

Abstract

The membrane-bound glycoprotein, amyloid precursor protein (APP), plays a central role in Alzheimer's disease (AD). The present paper investigates the neuritogenic-neurotoxic properties of this protein and relates them to possible aetiopathological mechanisms in AD. Marked differences in neuritic differentiation were detected when comparing untransfected tetraploid mouse neuroblastoma cells (or vector only cells) with transfected cells overexpressing APP(751) Transfected cells developed neurites quicker, and whereas all transfected cells differentiated, the degree of differentiation of untransfected cells was more variable. Fully differentiated transfected and untransfected cells had marked differences in neuritic morphology. Transfected cells had more neurites per cell, these being shorter and more branched thanneurites on untransfected cells. The precocious differentiation of transfected cells was not maintained with neuritic process disintegration and celldeath occurring from the seventh day onwards. Untransfected cells continued to extend their neuritic processes for up to five weeks. Membrane-associated forms of APP were responsible for these effects, rather than secreted APP or the beta /A4-peptide. Combined data from Western blot and immunocytochemical procedures showed a prominent accumulation of APP-C-terminal fragments in the perinuclear region, neuritic varicosities and growth cones of transfected cells, suggesting their involvement in the neuritogenic-neurotoxic process. Similar neuritogenic-neurotoxic mechanisms occurring in vivo, inassociation with compensatory synaptoplastic responses in the aged brain, may be part of the pathological process in AD. Copyright (C) 2001 S. KargerAG, Basel.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/01/20 alle ore 00:15:07