{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,18]],"date-time":"2026-08-18T00:46:04Z","timestamp":1787013964846,"version":"build-2736575974"},"reference-count":71,"publisher":"Wiley","issue":"11","license":[{"start":{"date-parts":[[2026,2,9]],"date-time":"2026-02-09T00:00:00Z","timestamp":1770595200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"},{"start":{"date-parts":[[2026,2,9]],"date-time":"2026-02-09T00:00:00Z","timestamp":1770595200000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"content-domain":{"domain":["bpspubs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["British J Pharmacology"],"published-print":{"date-parts":[[2026,6]]},"abstract":"<jats:sec>\n                    <jats:title>Background and Purpose<\/jats:title>\n                    <jats:p>Lysine demethylase 1A (KDM1A; LSD1) plays anti\u2010ferroptosis role and has been confirmed to be lowly expressed in Alzheimer disease (AD). This study explores whether LSD1 affects the progression of AD by regulating ferroptosis and related mechanisms involved.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Experimental Approach<\/jats:title>\n                    <jats:p>AD mice (APP\/PS1 double transgenic) were injected with adeno\u2010associated virus expressing LSD1 overexpression vector, or siRNA against leucine carboxyl methyltransferase 1 (LCMT1)\/transcription factor EB (TFEB). SH\u2010SY5Y cells were treated with A\u03b21\u201042 to establish an AD cell injury model. The levels of lipid peroxidation and ferroptosis\u2010related markers were tested to evaluate ferroptosis. The protein levels of LSD1, O\u2010GlcNAcase (OGA), forkhead box transcription factor A2 (FOXA2), LCMT1, protein phosphatase 2A catalytic subunit alpha (PP2A) and TFEB were detected by western blot. The mRNA levels of LSD1 and OGA were assessed using quantitative real\u2010time PCR. Interactions between targets were measured by ChIP\u2010qPCR, DNA pull down, co\u2010immunoprecipitation and dual\u2010luciferase reporter assay.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Key Results<\/jats:title>\n                    <jats:p>LSD1 upregulation suppressed neuronal ferroptosis to attenuate AD progression in mice. Further, LSD1 overexpression alleviated A\u03b21\u201042\u2010induced cell injury by reducing OGA transcription and expression. OGA inhibited FOXA2 O\u2010GlcNAcylation modification to promote its expression and transcriptional activity. Also, FOXA2 repressed LCMT1\u2010mediated the activation of PP2A and TFEB. Furthermore, LSD1 alleviated AD process by inhibiting neuronal ferroptosis through the regulation of OGA\/FOXA2\/LCMT1\/PP2A\/TFEB axis.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Conclusions and Implications<\/jats:title>\n                    <jats:p>Overall, LSD1 restrained neuronal ferroptosis to alleviate the progression of AD by regulating LCMT1\/PP2A\/TFEB pathway via OGA\u2010mediated FOXA2 O\u2010GlcNAcylation modification, providing novel mechanistic insights into the deeper understanding of AD pathogenesis and the development of potential drug targets.<\/jats:p>\n                  <\/jats:sec>","DOI":"10.1111\/bph.70289","type":"journal-article","created":{"date-parts":[[2026,2,10]],"date-time":"2026-02-10T05:38:44Z","timestamp":1770701924000},"page":"2720-2738","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["Lysine demethylase 1A alleviates Alzheimer disease progression by regulating the leucine carboxyl methyltransferase 1\/protein phosphatase 2 catalytic subunit alpha\/transcription factor EB pathway via O\u2010GlcNAcase\u2010mediated forkhead box transcription factor A2 O\u2010GlcNAcylation modification"],"prefix":"10.1111","volume":"183","author":[{"given":"Jingwei","family":"Cao","sequence":"first","affiliation":[{"name":"Department of Neurology The First Affiliated Hospital of Harbin Medical University  Harbin City China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jihe","family":"Song","sequence":"additional","affiliation":[{"name":"Department of Neurology The First Affiliated Hospital of Harbin Medical University  Harbin City China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zeyu","family":"Yin","sequence":"additional","affiliation":[{"name":"Department of Neurology The First Affiliated Hospital of Harbin Medical University  Harbin City China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zhanbin","family":"Tang","sequence":"additional","affiliation":[{"name":"Department of Neurology The First Affiliated Hospital of Harbin Medical University  Harbin City China"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2026,2,9]]},"reference":[{"key":"e_1_2_13_2_1","doi-asserted-by":"publisher","DOI":"10.1111\/bph.16181"},{"issue":"2","key":"e_1_2_13_3_1","first-page":"S1","article-title":"The concise guide to PHARMACOLOGY 2023\/24: Introduction and other protein targets","volume":"180","author":"Alexander S. 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