We are analyzing https://link.springer.com/article/10.1007/bf03036452.

Title:
Association of apolipoprotein J-positive β-amyloid plaques with dystrophic neurites in alzheimer’s disease brain | Neurotoxicity Research
Description:
Apolipoprotein J (apoJ), also known as clusterin and SP-40,40, binds soluble beta-amyloid (Aβ and is up-regulated in the Alzheimer’s disease (AD) brain. In the present study we classified apoJ-immunopositive Aβ deposits in AD temporal cortex, and found apoJ-immunoreactive plaques were often associated with dystrophic neurites. Quantitative immunohistochemical analysis of five AD brains showed that 29% of Aβ deposited in the parenchyma was associated with apoJ. Of Aβ deposits with apoJ immunopositivity, 71% were associated with phospho-tau-positive dystrophic neurites in the surrounding tissue. Conversely, 64% of phospho-tau-labeled neuritic deposits were labeled with apoJ. ApoJ was found at the core of these deposits, and co-localized with the amyloid staining agent thioflavine-S. To test the direct effects of apoJ on tau metabolism, we treated cells in culture with apoJ-containing conditioned media, and we injected apoJ-containing media into the rat hippocampus. Using both systems, we observed increases in levels of tau and phosphorylated tau. Our findings demonstrate that apoJ immunopositivity strongly correlates with the presence of amyloid and associated neuritic dystrophy in the neuropil of AD temporal cortex, and supports a model where extracellular apoJ facilitates the conversion of diffuse Aβ deposits into amyloid and enhances tau phosphorylation in neurites surrounding these plaques.
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Keywords {🔍}

article, google, scholar, pubmed, cas, alzheimers, amyloid, apolipoprotein, disease, brain, hyman, plaques, rebeck, apoj, neuropathol, usa, research, clusterin, tau, access, deposits, deposition, alzheimer, privacy, cookies, content, neurites, neuritic, neurol, bales, paul, natl, acad, sci, res, wisniewski, publish, search, dystrophic, temporal, model, open, diseaseproc, choimiura, holtzman, pathological, frangione, biol, media, data,

Topics {✒️}

month download article/chapter phospho-tau-positive dystrophic neurites phospho-tau-labeled neuritic deposits ß-amyloid precursor protein binds soluble beta-amyloid caspase-3-independent brain injury amyloid ß-peptide deposition apolipoprotein-e-deficient mice isoform-dependant amyloid deposition related subjects full article pdf found apoj-immunoreactive plaques nh choi-miura amyloid beta-peptide article martin-rehrmann privacy choices/manage cookies js kim-han amyloid beta solubility beta-amyloid deposition enhances tau phosphorylation pathological chaperone protein intracellular aβ levels kuru plaque amyloid aß-protein deposition ad temporal cortex ad brains showed hyang-sook hoe cerebrovascular plaque formation amyloid-beta interaction apolipoprotein j-alzheimer european economic area secondary proteome insolubility gómez-isla dm holtzman sd harr rb demattos neonatal hypoxia-ischemia mc irizarry cultured hippocampal neurons cortical lewy bodies app mutations linked massachusetts general hospital diffuse aβ deposits metabolize apolipoprotein e cerebral amyloid deposits aβ deposit morphology conditions privacy policy fluorescently labeled tissue 40 tau access cerebral amyloid angiopathy

Questions {❓}

Hardy J (1997) The Alzheimer family of diseases: many etiologies, one pathogenesis?
Qiu Z, Strickland DK, Hyman BT, and GW Rebeck (2002) ?
Sasaki K, K Doh-ura, Y Wakisaka and T Iwaki (2002) Clusterin/apolipoprotein J is associated with cortical Lewy bodies: immunohistochemical study in cases with ?

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         headline:Association of apolipoprotein J-positive β-amyloid plaques with dystrophic neurites in alzheimer’s disease brain
         description:Apolipoprotein J (apoJ), also known as clusterin and SP-40,40, binds soluble beta-amyloid (Aβ and is up-regulated in the Alzheimer’s disease (AD) brain. In the present study we classified apoJ-immunopositive Aβ deposits in AD temporal cortex, and found apoJ-immunoreactive plaques were often associated with dystrophic neurites. Quantitative immunohistochemical analysis of five AD brains showed that 29% of Aβ deposited in the parenchyma was associated with apoJ. Of Aβ deposits with apoJ immunopositivity, 71% were associated with phospho-tau-positive dystrophic neurites in the surrounding tissue. Conversely, 64% of phospho-tau-labeled neuritic deposits were labeled with apoJ. ApoJ was found at the core of these deposits, and co-localized with the amyloid staining agent thioflavine-S. To test the direct effects of apoJ on tau metabolism, we treated cells in culture with apoJ-containing conditioned media, and we injected apoJ-containing media into the rat hippocampus. Using both systems, we observed increases in levels of tau and phosphorylated tau. Our findings demonstrate that apoJ immunopositivity strongly correlates with the presence of amyloid and associated neuritic dystrophy in the neuropil of AD temporal cortex, and supports a model where extracellular apoJ facilitates the conversion of diffuse Aβ deposits into amyloid and enhances tau phosphorylation in neurites surrounding these plaques.
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      headline:Association of apolipoprotein J-positive β-amyloid plaques with dystrophic neurites in alzheimer’s disease brain
      description:Apolipoprotein J (apoJ), also known as clusterin and SP-40,40, binds soluble beta-amyloid (Aβ and is up-regulated in the Alzheimer’s disease (AD) brain. In the present study we classified apoJ-immunopositive Aβ deposits in AD temporal cortex, and found apoJ-immunoreactive plaques were often associated with dystrophic neurites. Quantitative immunohistochemical analysis of five AD brains showed that 29% of Aβ deposited in the parenchyma was associated with apoJ. Of Aβ deposits with apoJ immunopositivity, 71% were associated with phospho-tau-positive dystrophic neurites in the surrounding tissue. Conversely, 64% of phospho-tau-labeled neuritic deposits were labeled with apoJ. ApoJ was found at the core of these deposits, and co-localized with the amyloid staining agent thioflavine-S. To test the direct effects of apoJ on tau metabolism, we treated cells in culture with apoJ-containing conditioned media, and we injected apoJ-containing media into the rat hippocampus. Using both systems, we observed increases in levels of tau and phosphorylated tau. Our findings demonstrate that apoJ immunopositivity strongly correlates with the presence of amyloid and associated neuritic dystrophy in the neuropil of AD temporal cortex, and supports a model where extracellular apoJ facilitates the conversion of diffuse Aβ deposits into amyloid and enhances tau phosphorylation in neurites surrounding these plaques.
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      pageEnd:241
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         Immunofluorescence
         SP-40,40
         Tau
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         Neurochemistry
         Pharmacology/Toxicology
         Neurobiology
         Cell Biology
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