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.orcid0000-0003-3368-8123
dc.contributor.researcheridAAR-4341-2020
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.
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.
dc.identifier.endpage228
dc.identifier.issn0014-4886
dc.identifier.issue1
dc.identifier.pubmed10448435
dc.identifier.scopus2-s2.0-0032840954
dc.identifier.startpage221
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.volume158
dc.identifier.wos000081561800023
dc.indexed.scopusScopus
dc.indexed.wosSCIE
dc.language.isoen
dc.publisherAcademic Press Inc
dc.relation.collaborationYurt dışı
dc.relation.journalExperimental Neurology
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectAlzheimer's disease
dc.subjectBrain biopsy
dc.subjectBeta-amyloid
dc.subjectImmunoreactivity
dc.subjectUltrastructure
dc.subjectAstrocytes
dc.subjectGlycogen
dc.subjectSenile plaques
dc.subjectDiffuse plaques
dc.subjectPrecursor protein
dc.subjectPreamyloid deposits
dc.subjectMicroglial cells
dc.subjectLocalization
dc.subjectAccumulation
dc.subjectAntibodies
dc.subjectGlycation
dc.subjectGlycogen
dc.subject.wosNeurosciences
dc.titleBeta-amyloid immunoreactivity in astrocytes in alzheimer's disease brain biopsies: An electron microscope study
dc.typeArticle
dc.wos.quartileQ1
dspace.entity.typePublication
local.contributor.departmentTıp Fakültesi/Anatomi Ana Bilim Dalı
local.indexed.atPubMed
local.indexed.atScopus

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