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10.1126/scisignal.aad5614 http://scihub22266oqcxt.onion/10.1126/scisignal.aad5614 C5023144!5023144 !26732762     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=26732762 &cmd=llinks): Failed to open stream: HTTP request failed! 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Inclusion bodies enriched for p62 and polyubiquitinated proteins in macrophages protect against atherosclerosis |pdf=|usr=}}{{26732762 }} gab.com Text Inclusion bodies enriched for p62 and polyubiquitinated proteins in macrophages protect against atherosclerosis JO: Sci Signal http://www.kidney.de/pget.php?&tw=1&pmid=26732762 #FOAvip Autophagy is a catabolic cellular mechanism that degrades dysfunctional proteins and organelles. Atherosclerotic plaque formation is enhanced in mice with macrophages deficient for the critical autophagy protein ATG5. We showed that exposure of macrophages to lipids that promote atherosclerosis increased the abundance of the autophagy chaperone p62 and that p62 colocalized with polyubiquitinated proteins in cytoplasmic inclusions, which are characterized by insoluble protein aggregates. ATG5-null macrophages developed further p62 accumulation at the sites of large cytoplasmic ubiquitin-positive inclusion bodies. Aortas from atherosclerotic mice and plaques from human endarterectomy samples showed increased abundance of p62 and polyubiquitinated proteins that colocalized with plaque macrophages, suggesting that p62-enriched protein aggregates were characteristic of atherosclerosis. The formation of the cytoplasmic inclusions depended on p62 because lipid-loaded p62-null macrophages accumulated polyubiquitinated proteins in a diffuse cytoplasmic pattern. Lipid-loaded p62-null macrophages also exhibited increased secretion of interleukin-1? (IL-1?) and had an increased tendency to undergo apoptosis, which depended on the p62 ubiquitin-binding domain and at least partly involved p62-mediated clearance of NLRP3 inflammasomes. Consistent with our in vitro observations, p62-deficient mice formed greater numbers of more complex atherosclerotic plaques, and p62 deficiency further increased atherosclerotic plaque burden in mice with a macrophage-specific ablation of ATG5. Together, these data suggested that sequestration of cytotoxic ubiquitinated proteins by p62 protects against atherogenesis, a condition in which the clearance of protein aggregates is disrupted. Twit Text FOAVip Inclusion bodies enriched for p62 and polyubiquitinated proteins in macrophages protect against atherosclerosis ????Sci Signal http://www.kidney.de/pget.php?&tw=1&pmid=26732762 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26732762 #FOAvip English Wikipedia <ref>{{Cite pmid|26732762 }}</ref> Inclusion bodies enriched for p62 and polyubiquitinated proteins in macrophages protect against atherosclerosis #MMPMID26732762 Sergin I ; Bhattacharya S ; Emanuel R ; Esen E ; Stokes CJ ; Evans TD ; Arif B ; Curci JA ; Razani B Sci Signal 2016[Jan]; 9 (409 ): ra2 PMID26732762 show ga Autophagy is a catabolic cellular mechanism that degrades dysfunctional proteins and organelles. Atherosclerotic plaque formation is enhanced in mice with macrophages deficient for the critical autophagy protein ATG5. We showed that exposure of macrophages to lipids that promote atherosclerosis increased the abundance of the autophagy chaperone p62 and that p62 colocalized with polyubiquitinated proteins in cytoplasmic inclusions, which are characterized by insoluble protein aggregates. ATG5-null macrophages developed further p62 accumulation at the sites of large cytoplasmic ubiquitin-positive inclusion bodies. Aortas from atherosclerotic mice and plaques from human endarterectomy samples showed increased abundance of p62 and polyubiquitinated proteins that colocalized with plaque macrophages, suggesting that p62-enriched protein aggregates were characteristic of atherosclerosis. The formation of the cytoplasmic inclusions depended on p62 because lipid-loaded p62-null macrophages accumulated polyubiquitinated proteins in a diffuse cytoplasmic pattern. Lipid-loaded p62-null macrophages also exhibited increased secretion of interleukin-1? (IL-1?) and had an increased tendency to undergo apoptosis, which depended on the p62 ubiquitin-binding domain and at least partly involved p62-mediated clearance of NLRP3 inflammasomes. Consistent with our in vitro observations, p62-deficient mice formed greater numbers of more complex atherosclerotic plaques, and p62 deficiency further increased atherosclerotic plaque burden in mice with a macrophage-specific ablation of ATG5. Together, these data suggested that sequestration of cytotoxic ubiquitinated proteins by p62 protects against atherogenesis, a condition in which the clearance of protein aggregates is disrupted. |Adaptor Proteins, Signal Transducing/genetics/*metabolism [MESH] |Animals [MESH] |Apolipoproteins E/genetics/metabolism [MESH] |Apoptosis/genetics [MESH] |Atherosclerosis/genetics/*metabolism [MESH] |Autophagy-Related Protein 5 [MESH] |Autophagy/genetics [MESH] |Carrier Proteins/genetics/metabolism [MESH] |Cells, Cultured [MESH] |Cytoplasm/genetics/metabolism [MESH] |Heat-Shock Proteins/genetics/*metabolism [MESH] |Humans [MESH] |Immunoblotting [MESH] |Inclusion Bodies/*metabolism [MESH] |Inflammasomes/genetics/metabolism [MESH] |Interleukin-1beta/metabolism [MESH] |Macrophages/*metabolism [MESH] |Mice, Inbred C57BL [MESH] |Mice, Knockout [MESH] |Microscopy, Fluorescence [MESH] |Microtubule-Associated Proteins/genetics/*metabolism [MESH] |NLR Family, Pyrin Domain-Containing 3 Protein [MESH] |Polyubiquitin [MESH] |RNA Interference [MESH] |Sequestosome-1 Protein [MESH]Inclusion bodies enriched for p62 and polyubiquitinated proteins in ma(epmc).pdf DeepDyve Pubget Overpricing