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10.1126/scitranslmed.aad3650 http://scihub22266oqcxt.onion/10.1126/scitranslmed.aad3650 C5512541!5512541!27030596     free     free     free Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 251.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 251.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 251.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 251.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Sci+Transl+Med 2016 ; 8 (332): 332ra44 Nephropedia Template TP {{tp|p=27030596|t=2016. 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 (HS), expressed on all cell types including neurons, have been implicated in several features in the pathogenesis of AD including its co-localization with amyloid plaques and modulatory role in A? aggregation. Here, 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 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 (ISF), suggesting that neuronal HS either inhibited or represented an inefficient pathway for A? clearance. Interestingly, 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 PMID27030596show 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 (HS), expressed on all cell types including neurons, have been implicated in several features in the pathogenesis of AD including its co-localization with amyloid plaques and modulatory role in A? aggregation. Here, 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 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 (ISF), suggesting that neuronal HS either inhibited or represented an inefficient pathway for A? clearance. Interestingly, 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. äNeuronal heparan sulfates promote amyloid pathology by modulating brai(epmc).pdf DeepDyve Pubget Overpricing