Publication:
Beta-amyloid immunoreactivity in astrocytes in alzheimer's disease brain biopsies: An electron microscope study

dc.contributor.authorDavies, D. Ceirj
dc.contributor.authorKidd, M.
dc.contributor.buuauthorKurt, Mustafa Ayberk
dc.contributor.departmentTıp Fakültesi
dc.contributor.departmentAnatomi Ana Bilim Dalı
dc.contributor.orcid0000-0003-3368-8123tr_TR
dc.contributor.researcheridAAR-4341-2020tr_TR
dc.date.accessioned2021-06-24T08:42:36Z
dc.date.available2021-06-24T08:42:36Z
dc.date.issued1999
dc.description.abstractThe deposition of amyloid beta (A beta) protein plays a central role in the neuropathology of Alzheimer's disease (AD) and it constitutes the core of classical senile plaques. However, little is known about its intracellular distribution. An immunogold electron microscope study was therefore carried out on biopsies of brain tissue from patients with AD using a monoclonal antibody raised against residues 8 to 17 of the A beta protein. Specific A beta immunogold labeling was observed over extracellular amyloid fibrils associated with senile plaques. In addition, widespread intracellular A beta immunolabeling was observed adjacent to granular structures (30-40 nm in diameter) within membrane-bound processes, Pretreatment of some sections with amylase or omission of lead citrate staining from others strongly suggests that the electron-dense granular structures associated with A beta immunoreactivity are glycogen. Some of the A beta-immunolabeled processes contained gliofilaments and immunolabeling of alternate sections for glial fibrillary acidic protein confirmed that the A beta-immunolabeled processes were astrocytic. A beta immunolabeling was not observed over neuronal or microglial processes, Whether the presence of A beta protein in astrocytes is the result of synthetic or degradation processes requires further investigation. (C) 1999 Academic Press.en_US
dc.identifier.citationKurt, M. A. vd. (1999). "Beta-amyloid immunoreactivity in astrocytes in alzheimer's disease brain biopsies: An electron microscope study". Experimental Neurology, 158(1), 221-228.en_US
dc.identifier.endpage228tr_TR
dc.identifier.issn0014-4886
dc.identifier.issue1tr_TR
dc.identifier.pubmed10448435tr_TR
dc.identifier.scopus2-s2.0-0032840954tr_TR
dc.identifier.startpage221tr_TR
dc.identifier.urihttps://doi.org/10.1006/exnr.1999.7096
dc.identifier.urihttps://www.sciencedirect.com/science/article/pii/S0014488699970966#!
dc.identifier.urihttp://hdl.handle.net/11452/20820
dc.identifier.volume158tr_TR
dc.identifier.wos000081561800023
dc.indexed.pubmedPubmeden_US
dc.indexed.scopusScopusen_US
dc.indexed.wosSCIEen_US
dc.language.isoenen_US
dc.publisherAcademic Press Incen_US
dc.relation.collaborationYurt dışıtr_TR
dc.relation.journalExperimental Neurologyen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergitr_TR
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectAlzheimer's diseaseen_US
dc.subjectBrain biopsyen_US
dc.subjectBeta-amyloiden_US
dc.subjectImmunoreactivityen_US
dc.subjectUltrastructureen_US
dc.subjectAstrocytesen_US
dc.subjectGlycogenen_US
dc.subjectSenile plaquesen_US
dc.subjectDiffuse plaquesen_US
dc.subjectPrecursor proteinen_US
dc.subjectPreamyloid depositsen_US
dc.subjectMicroglial cellsen_US
dc.subjectLocalizationen_US
dc.subjectAccumulationen_US
dc.subjectAntibodiesen_US
dc.subjectGlycationen_US
dc.subjectGlycogenen_US
dc.subject.wosNeurosciencesen_US
dc.titleBeta-amyloid immunoreactivity in astrocytes in alzheimer's disease brain biopsies: An electron microscope studyen_US
dc.typeArticle
dc.wos.quartileQ1en_US
dspace.entity.typePublication
local.contributor.departmentTıp Fakültesi/Anatomi Ana Bilim Dalıen_US

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