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000259245 1001_ $$0P:(DE-2719)9001998$$aYazar, Volkan$$b0$$eFirst author$$udzne
000259245 245__ $$aImpaired ATF3 signaling involves SNAP25 in SOD1 mutant ALS patients.
000259245 260__ $$a[London]$$bMacmillan Publishers Limited, part of Springer Nature$$c2023
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000259245 520__ $$aEpigenetic remodeling is emerging as a critical process for several neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS). Genetics alone fails to explain the etiology of ALS, the investigation of the epigenome might therefore provide novel insights into the molecular mechanisms of the disease. In this study, we interrogated the epigenetic landscape in peripheral blood mononuclear cells (PBMCs) of familial ALS (fALS) patients with either chromosome 9 open reading frame 72 (C9orf72) or superoxide dismutase 1 (SOD1) mutation and aimed to identify key epigenetic footprints of the disease. To this end, we used an integrative approach that combines chromatin immunoprecipitation targeting H3K27me3 (ChIP-Seq) with the matching gene expression data to gain new insights into the likely impact of blood-specific chromatin remodeling on ALS-related molecular mechanisms. We demonstrated that one of the hub molecules that modulates changes in PBMC transcriptome in SOD1-mutant ALS patients is ATF3, which has been previously reported in an SOD1G93A mouse model. We also identified potential suppression of SNAP25, with impaired ATF3 signaling in SOD1-mutant ALS blood. Together, our study shed light on the mechanistic underpinnings of SOD1 mutations in ALS.
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000259245 650_2 $$2MeSH$$aAnimals
000259245 650_2 $$2MeSH$$aMice
000259245 650_2 $$2MeSH$$aAmyotrophic Lateral Sclerosis: genetics
000259245 650_2 $$2MeSH$$aAmyotrophic Lateral Sclerosis: metabolism
000259245 650_2 $$2MeSH$$aLeukocytes, Mononuclear: metabolism
000259245 650_2 $$2MeSH$$aMice, Transgenic
000259245 650_2 $$2MeSH$$aMutation
000259245 650_2 $$2MeSH$$aSuperoxide Dismutase: genetics
000259245 650_2 $$2MeSH$$aSuperoxide Dismutase: metabolism
000259245 650_2 $$2MeSH$$aSuperoxide Dismutase-1: genetics
000259245 650_7 $$0EC 1.15.1.1$$2NLM Chemicals$$aSuperoxide Dismutase
000259245 650_7 $$0EC 1.15.1.1$$2NLM Chemicals$$aSuperoxide Dismutase-1
000259245 650_7 $$2NLM Chemicals$$aSNAP25 protein, human
000259245 650_7 $$2NLM Chemicals$$aSOD1 protein, human
000259245 7001_ $$0P:(DE-2719)9001523$$aKühlwein, Julia$$b1$$udzne
000259245 7001_ $$aKnehr, Antje$$b2
000259245 7001_ $$0P:(DE-2719)9001519$$aGrozdanov, Veselin$$b3$$udzne
000259245 7001_ $$aEkici, Arif B$$b4
000259245 7001_ $$0P:(DE-2719)2812633$$aLudolph, Albert C$$b5$$udzne
000259245 7001_ $$0P:(DE-2719)9001513$$aDanzer, Karin M$$b6$$eLast author$$udzne
000259245 773__ $$0PERI:(DE-600)2615211-3$$a10.1038/s41598-023-38684-8$$gVol. 13, no. 1, p. 12019$$n1$$p12019$$tScientific reports$$v13$$x2045-2322$$y2023
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