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10.1126/scitranslmed.aad3650 http://scihub22266oqcxt.onion/10.1126/scitranslmed.aad3650 C5512541!5512541 !27030596     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=27030596 &cmd=llinks): Failed to open stream: HTTP request failed! 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Neuronal heparan sulfates promote amyloid pathology by modulating brain amyloid-? clearance and aggregation in Alzheimer s disease |pdf=|usr=}}{{27030596 }} gab.com Text Neuronal heparan sulfates promote amyloid pathology by modulating brain amyloid- clearance and aggregation in Alzheimer s disease JO: Sci Transl Med http://www.kidney.de/pget.php?&tw=1&pmid=27030596 #FOAvip Accumulation of amyloid-? (A?) peptide in the brain is the first critical step in the pathogenesis of Alzheimer's disease (AD). Studies in humans suggest that A? clearance from the brain is frequently impaired in late-onset AD. A? accumulation leads to the formation of A? aggregates, which injure synapses and contribute to eventual neurodegeneration. Cell surface heparan sulfates (HSs), expressed on all cell types including neurons, have been implicated in several features in the pathogenesis of AD including its colocalization with amyloid plaques and modulatory role in A? aggregation. We show that removal of neuronal HS by conditional deletion of the Ext1 gene, which encodes an essential glycosyltransferase for HS biosynthesis, in postnatal neurons of amyloid model APP/PS1 mice led to a reduction in both A? oligomerization and the deposition of amyloid plaques. In vivo microdialysis experiments also detected an accelerated rate of A? clearance in the brain interstitial fluid, suggesting that neuronal HS either inhibited or represented an inefficient pathway for A? clearance. We found that the amounts of various HS proteoglycans (HSPGs) were increased in postmortem human brain tissues from AD patients, suggesting that this pathway may contribute directly to amyloid pathogenesis. Our findings have implications for AD pathogenesis and provide insight into therapeutic interventions targeting A?-HSPG interactions. Twit Text FOAVip Neuronal heparan sulfates promote amyloid pathology by modulating brain amyloid- clearance and aggregation in Alzheimer s disease ????Sci Transl Med http://www.kidney.de/pget.php?&tw=1&pmid=27030596 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27030596 #FOAvip English Wikipedia <ref>{{Cite pmid|27030596 }}</ref> Neuronal heparan sulfates promote amyloid pathology by modulating brain amyloid-? clearance and aggregation in Alzheimer s disease #MMPMID27030596 Liu CC ; Zhao N ; Yamaguchi Y ; Cirrito JR ; Kanekiyo T ; Holtzman DM ; Bu G Sci Transl Med 2016[Mar]; 8 (332 ): 332ra44 PMID27030596 show ga Accumulation of amyloid-? (A?) peptide in the brain is the first critical step in the pathogenesis of Alzheimer's disease (AD). Studies in humans suggest that A? clearance from the brain is frequently impaired in late-onset AD. A? accumulation leads to the formation of A? aggregates, which injure synapses and contribute to eventual neurodegeneration. Cell surface heparan sulfates (HSs), expressed on all cell types including neurons, have been implicated in several features in the pathogenesis of AD including its colocalization with amyloid plaques and modulatory role in A? aggregation. We show that removal of neuronal HS by conditional deletion of the Ext1 gene, which encodes an essential glycosyltransferase for HS biosynthesis, in postnatal neurons of amyloid model APP/PS1 mice led to a reduction in both A? oligomerization and the deposition of amyloid plaques. In vivo microdialysis experiments also detected an accelerated rate of A? clearance in the brain interstitial fluid, suggesting that neuronal HS either inhibited or represented an inefficient pathway for A? clearance. We found that the amounts of various HS proteoglycans (HSPGs) were increased in postmortem human brain tissues from AD patients, suggesting that this pathway may contribute directly to amyloid pathogenesis. Our findings have implications for AD pathogenesis and provide insight into therapeutic interventions targeting A?-HSPG interactions. |Aged, 80 and over [MESH] |Alzheimer Disease/*metabolism/*pathology [MESH] |Amyloid beta-Peptides/*metabolism [MESH] |Amyloid/*metabolism [MESH] |Animals [MESH] |Disease Models, Animal [MESH] |Heparitin Sulfate/*metabolism [MESH] |Hippocampus/blood supply/pathology [MESH] |Humans [MESH] |Inflammation/pathology [MESH] |Mice [MESH] |Neurons/*metabolism/pathology [MESH]Neuronal heparan sulfates promote amyloid pathology by modulating brai(epmc).pdf DeepDyve Pubget Overpricing