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10.1371/journal.pone.0233180 http://scihub22266oqcxt.onion/10.1371/journal.pone.0233180 32437392!7241781!32437392     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=32437392&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       PLoS+One 2020 ; 15 (5): e0233180 Nephropedia Template TP {{tp|p=32437392|t=2020. THP-1 macrophage cholesterol efflux is impaired by palmitoleate through Akt activation |pdf=|usr=}}{{32437392}} gab.com Text THP-1 macrophage cholesterol efflux is impaired by palmitoleate through Akt activation JO: PLoS One http://www.kidney.de/pget.php?&tw=1&pmid=32437392 #FOAvip Lipoprotein lipase (LPL) is upregulated in atherosclerotic lesions and it may promote the progression of atherosclerosis, but the mechanisms behind this process are not completely understood. We previously showed that the phosphorylation of Akt within THP-1 macrophages is increased in response to the lipid hydrolysis products generated by LPL from total lipoproteins. Notably, the free fatty acid (FFA) component was responsible for this effect. In the present study, we aimed to reveal more detail as to how the FFA component may affect Akt signalling. We show that the phosphorylation of Akt within THP-1 macrophages increases with total FFA concentration and that phosphorylation is elevated up to 18 hours. We further show that specifically the palmitoleate component of the total FFA affects Akt phosphorylation. This is tied with changes to the levels of select molecular species of phosphoinositides. We further show that the total FFA component, and specifically palmitoleate, reduces apolipoprotein A-I-mediated cholesterol efflux, and that the reduction can be reversed in the presence of the Akt inhibitor MK-2206. Overall, our data support a negative role for the FFA component of lipoprotein hydrolysis products generated by LPL, by impairing macrophage cholesterol efflux via Akt activation. Twit Text FOAVip THP-1 macrophage cholesterol efflux is impaired by palmitoleate through Akt activation ????PLoS One http://www.kidney.de/pget.php?&tw=1&pmid=32437392 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32437392 #FOAvip English Wikipedia <ref>{{Cite pmid|32437392}}</ref> THP-1 macrophage cholesterol efflux is impaired by palmitoleate through Akt activation #MMPMID32437392 Marshall JD; Courage ER; Elliott RF; Fitzpatrick MN; Kim AD; Lopez-Clavijo AF; Woolfrey BA; Ouimet M; Wakelam MJO; Brown RJ PLoS One 2020[]; 15 (5): e0233180 PMID32437392show ga Lipoprotein lipase (LPL) is upregulated in atherosclerotic lesions and it may promote the progression of atherosclerosis, but the mechanisms behind this process are not completely understood. We previously showed that the phosphorylation of Akt within THP-1 macrophages is increased in response to the lipid hydrolysis products generated by LPL from total lipoproteins. Notably, the free fatty acid (FFA) component was responsible for this effect. In the present study, we aimed to reveal more detail as to how the FFA component may affect Akt signalling. We show that the phosphorylation of Akt within THP-1 macrophages increases with total FFA concentration and that phosphorylation is elevated up to 18 hours. We further show that specifically the palmitoleate component of the total FFA affects Akt phosphorylation. This is tied with changes to the levels of select molecular species of phosphoinositides. We further show that the total FFA component, and specifically palmitoleate, reduces apolipoprotein A-I-mediated cholesterol efflux, and that the reduction can be reversed in the presence of the Akt inhibitor MK-2206. Overall, our data support a negative role for the FFA component of lipoprotein hydrolysis products generated by LPL, by impairing macrophage cholesterol efflux via Akt activation. |Apolipoprotein A-I/metabolism[MESH] |Cholesterol/*metabolism[MESH] |Enzyme Activation/drug effects[MESH] |Heterocyclic Compounds, 3-Ring/pharmacology[MESH] |Humans[MESH] |Lipoprotein Lipase/metabolism[MESH] |Macrophages/cytology/*metabolism[MESH] |Palmitic Acid/*metabolism[MESH] |Phosphorylation/drug effects[MESH] |Proto-Oncogene Proteins c-akt/antagonists & inhibitors/*metabolism[MESH]THP-1 macrophage cholesterol efflux is impaired by palmitoleate throug(epmc).pdf DeepDyve Pubget Overpricing