{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Yao Q"],"funding":["National Natural Science Foundation of China","Ministry of Science and Technology of the People&amp;apos;s Republic of China"],"pagination":["102765"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9808002"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["299(1)"],"pubmed_abstract":["Hyperlipidemia characterized by high blood levels of free fatty acids (FFAs) is important for the progression of inflammatory cardiovascular diseases. Integrin β<sub>1</sub> is a transmembrane receptor that drives various cellular functions, including differentiation, migration, and phagocytosis. However, the underlying mechanisms modifying integrin β<sub>1</sub> protein and activity in mediating monocyte/macrophage adhesion to endothelium remain poorly understood. In this study, we demonstrated that integrin β<sub>1</sub> protein underwent S-nitrosylation in response to nitrosative stress in macrophages. To examine the effect of elevated levels of FFA on the modulation of integrin β<sub>1</sub> expression, we treated the macrophages with a combination of oleic acid and palmitic acid (2:1)"],"journal":["The Journal of biological chemistry"],"pubmed_title":["Free fatty acids stabilize integrin β<sub>1</sub>via S-nitrosylation to promote monocyte-endothelial adhesion."],"pmcid":["PMC9808002"],"funding_grant_id":["81770497","91939108","81600389","2018YFA0800600","82070829","81830015"],"pubmed_authors":["Wang N","Liu J","Xiao L","Xie X","Zhao W","Du X","Lai B","Yao Q","Jiang T","Wang H","Zhao Z","Cui Q"],"additional_accession":[]},"is_claimable":false,"name":"Free fatty acids stabilize integrin β<sub>1</sub>via S-nitrosylation to promote monocyte-endothelial adhesion.","description":"Hyperlipidemia characterized by high blood levels of free fatty acids (FFAs) is important for the progression of inflammatory cardiovascular diseases. Integrin β<sub>1</sub> is a transmembrane receptor that drives various cellular functions, including differentiation, migration, and phagocytosis. However, the underlying mechanisms modifying integrin β<sub>1</sub> protein and activity in mediating monocyte/macrophage adhesion to endothelium remain poorly understood. In this study, we demonstrated that integrin β<sub>1</sub> protein underwent S-nitrosylation in response to nitrosative stress in macrophages. To examine the effect of elevated levels of FFA on the modulation of integrin β<sub>1</sub> expression, we treated the macrophages with a combination of oleic acid and palmitic acid (2:1)","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Dec","modification":"2025-04-04T21:04:41.119Z","creation":"2025-04-04T21:04:41.119Z"},"accession":"S-EPMC9808002","cross_references":{"pubmed":["36470423"],"doi":["10.1016/j.jbc.2022.102765"]}}