{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Poejo J"],"funding":["Spanish Ministerio de Ciencia e Innovación","Junta de Extremadura","Spanish Ministerio de Economía y Competitividad"],"pagination":["12678"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9604325"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["23(20)"],"pubmed_abstract":["Dysregulation in calcium signaling pathways plays a major role in the initiation of Alzheimer's disease (AD) pathogenesis. Accumulative experimental evidence obtained with cellular and animal models, as well as with AD brain samples, points out the high cytotoxicity of soluble small oligomeric forms of amyloid-β peptides (Aβ) in AD. In recent works, we have proposed that Aβ-calmodulin (CaM) complexation may play a major role in neuronal Ca<sup>2+</sup> signaling, mediated by CaM-binding proteins (CaMBPs). STIM1, a recognized CaMBP, plays a key role in store-operated calcium entry (SOCE), and it has been shown that the SOCE function is diminished in AD, resulting in the instability of dendric spines and enhanced amyloidogenesis. In this work, we show that 2 and 5 h of incubation with 2 μM A"],"journal":["International journal of molecular sciences"],"pubmed_title":["Internalized Amyloid-β (1-42) Peptide Inhibits the Store-Operated Calcium Entry in HT-22 Cells."],"pmcid":["PMC9604325"],"funding_grant_id":["GR18118","PID2020-112997GB-100","BFU2017-85723-P","PID2020-115512GB-100","GR21051"],"pubmed_authors":["Gutierrez-Merino C","Poejo J","Martin-Romero FJ","Orantos-Aguilera Y","Mata AM"],"additional_accession":[]},"is_claimable":false,"name":"Internalized Amyloid-β (1-42) Peptide Inhibits the Store-Operated Calcium Entry in HT-22 Cells.","description":"Dysregulation in calcium signaling pathways plays a major role in the initiation of Alzheimer's disease (AD) pathogenesis. Accumulative experimental evidence obtained with cellular and animal models, as well as with AD brain samples, points out the high cytotoxicity of soluble small oligomeric forms of amyloid-β peptides (Aβ) in AD. In recent works, we have proposed that Aβ-calmodulin (CaM) complexation may play a major role in neuronal Ca<sup>2+</sup> signaling, mediated by CaM-binding proteins (CaMBPs). STIM1, a recognized CaMBP, plays a key role in store-operated calcium entry (SOCE), and it has been shown that the SOCE function is diminished in AD, resulting in the instability of dendric spines and enhanced amyloidogenesis. In this work, we show that 2 and 5 h of incubation with 2 μM A","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Oct","modification":"2025-04-19T12:04:16.792Z","creation":"2025-04-19T12:04:16.792Z"},"accession":"S-EPMC9604325","cross_references":{"pubmed":["36293540"],"doi":["10.3390/ijms232012678"]}}