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10.2119/molmed.2015.00148 http://scihub22266oqcxt.onion/10.2119/molmed.2015.00148 C4607614!4607614 !26101955     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=26101955 &cmd=llinks): Failed to open stream: HTTP request failed! 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Aspirin s Active Metabolite Salicylic Acid Targets High Mobility Group Box 1 to Modulate Inflammatory Responses |pdf=|usr=}}{{26101955 }} gab.com Text Aspirin s Active Metabolite Salicylic Acid Targets High Mobility Group Box 1 to Modulate Inflammatory Responses JO: Mol Med http://www.kidney.de/pget.php?&tw=1&pmid=26101955 #FOAvip Salicylic acid (SA) and its derivatives have been used for millennia to reduce pain, fever and inflammation. In addition, prophylactic use of acetylsalicylic acid, commonly known as aspirin, reduces the risk of heart attack, stroke and certain cancers. Because aspirin is rapidly de-acetylated by esterases in human plasma, much of aspirin's bioactivity can be attributed to its primary metabolite, SA. Here we demonstrate that human high mobility group box 1 (HMGB1) is a novel SA-binding protein. SA-binding sites on HMGB1 were identified in the HMG-box domains by nuclear magnetic resonance (NMR) spectroscopic studies and confirmed by mutational analysis. Extracellular HMGB1 is a damage-associated molecular pattern molecule (DAMP), with multiple redox states. SA suppresses both the chemoattractant activity of fully reduced HMGB1 and the increased expression of proinflammatory cytokine genes and cyclooxygenase 2 (COX-2) induced by disulfide HMGB1. Natural and synthetic SA derivatives with greater potency for inhibition of HMGB1 were identified, providing proof-of-concept that new molecules with high efficacy against sterile inflammation are attainable. An HMGB1 protein mutated in one of the SA-binding sites identified by NMR chemical shift perturbation studies retained chemoattractant activity, but lost binding of and inhibition by SA and its derivatives, thereby firmly establishing that SA binding to HMGB1 directly suppresses its proinflammatory activities. Identification of HMGB1 as a pharmacological target of SA/aspirin provides new insights into the mechanisms of action of one of the world's longest and most used natural and synthetic drugs. It may also provide an explanation for the protective effects of low-dose aspirin usage. Twit Text FOAVip Aspirin s Active Metabolite Salicylic Acid Targets High Mobility Group Box 1 to Modulate Inflammatory Responses ????Mol Med http://www.kidney.de/pget.php?&tw=1&pmid=26101955 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26101955 #FOAvip English Wikipedia <ref>{{Cite pmid|26101955 }}</ref> Aspirin s Active Metabolite Salicylic Acid Targets High Mobility Group Box 1 to Modulate Inflammatory Responses #MMPMID26101955 Choi HW ; Tian M ; Song F ; Venereau E ; Preti A ; Park SW ; Hamilton K ; Swapna GV ; Manohar M ; Moreau M ; Agresti A ; Gorzanelli A ; De Marchis F ; Wang H ; Antonyak M ; Micikas RJ ; Gentile DR ; Cerione RA ; Schroeder FC ; Montelione GT ; Bianchi ME ; Klessig DF Mol Med 2015[Jun]; 21 (1 ): 526-35 PMID26101955 show ga Salicylic acid (SA) and its derivatives have been used for millennia to reduce pain, fever and inflammation. In addition, prophylactic use of acetylsalicylic acid, commonly known as aspirin, reduces the risk of heart attack, stroke and certain cancers. Because aspirin is rapidly de-acetylated by esterases in human plasma, much of aspirin's bioactivity can be attributed to its primary metabolite, SA. Here we demonstrate that human high mobility group box 1 (HMGB1) is a novel SA-binding protein. SA-binding sites on HMGB1 were identified in the HMG-box domains by nuclear magnetic resonance (NMR) spectroscopic studies and confirmed by mutational analysis. Extracellular HMGB1 is a damage-associated molecular pattern molecule (DAMP), with multiple redox states. SA suppresses both the chemoattractant activity of fully reduced HMGB1 and the increased expression of proinflammatory cytokine genes and cyclooxygenase 2 (COX-2) induced by disulfide HMGB1. Natural and synthetic SA derivatives with greater potency for inhibition of HMGB1 were identified, providing proof-of-concept that new molecules with high efficacy against sterile inflammation are attainable. An HMGB1 protein mutated in one of the SA-binding sites identified by NMR chemical shift perturbation studies retained chemoattractant activity, but lost binding of and inhibition by SA and its derivatives, thereby firmly establishing that SA binding to HMGB1 directly suppresses its proinflammatory activities. Identification of HMGB1 as a pharmacological target of SA/aspirin provides new insights into the mechanisms of action of one of the world's longest and most used natural and synthetic drugs. It may also provide an explanation for the protective effects of low-dose aspirin usage. |Aspirin/chemistry/*pharmacology [MESH] |Cyclooxygenase 2/biosynthesis/genetics [MESH] |HMGB1 Protein/biosynthesis/chemistry/*genetics [MESH] |Humans [MESH] |Inflammation/drug therapy/*genetics/pathology [MESH] |Mutation [MESH] |Nuclear Magnetic Resonance, Biomolecular [MESH]Aspirin s Active Metabolite Salicylic Acid Targets High Mobility Group(epmc).pdf DeepDyve Pubget Overpricing