{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Perera B"],"funding":["Therapeutic Innovation Australia (TIA)","Heart Foundation Future Leader Fellowship","Promoting Women Fellowship from the University of Queensland","Australian Government","Australian Research Council"],"pagination":["13650"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11678699"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["25(24)"],"pubmed_abstract":["The vascular cell adhesion molecule-1 (VCAM-1) plays an important role in inflammation, where it facilitates the recruitment of leukocytes to the inflamed area via leukocytes' VLA-4 and endothelial cells' VCAM-1 interaction. VCAM-1 expression is also upregulated in certain cancers. VCAM-1 has seven Ig-like domains, with domains 1 and 4 shown to be critical for VLA-4 binding. However, the specific functions of individual VCAM-1 Ig-like domains remain poorly understood. In this study, we identified single-chain variable fragment (scFv) antibodies targeting domains 2, 3, and 5 of VCAM-1, and investigated the ability of these antibodies to block VCAM-1-mediated cell adhesion to macrophages. We show that scFv antibodies against Ig-like domains 2 and 3 interfere with the ability of macrophages t"],"journal":["International journal of molecular sciences"],"pubmed_title":["Isolation and Characterization of Antibodies Against Vascular Cell Adhesion Molecule-1 Reveals Putative Role for Ig-like Domains 2 and 3 in Cell-to-Cell Interaction."],"pmcid":["PMC11678699"],"funding_grant_id":["IC160100027"],"pubmed_authors":["Pickett JR","Zacchi LF","Ta HT","Fercher C","Sester DP","Barretto FM","Perera B","Jones ML","Wu Y","Panagides N"],"additional_accession":[]},"is_claimable":false,"name":"Isolation and Characterization of Antibodies Against Vascular Cell Adhesion Molecule-1 Reveals Putative Role for Ig-like Domains 2 and 3 in Cell-to-Cell Interaction.","description":"The vascular cell adhesion molecule-1 (VCAM-1) plays an important role in inflammation, where it facilitates the recruitment of leukocytes to the inflamed area via leukocytes' VLA-4 and endothelial cells' VCAM-1 interaction. VCAM-1 expression is also upregulated in certain cancers. VCAM-1 has seven Ig-like domains, with domains 1 and 4 shown to be critical for VLA-4 binding. However, the specific functions of individual VCAM-1 Ig-like domains remain poorly understood. In this study, we identified single-chain variable fragment (scFv) antibodies targeting domains 2, 3, and 5 of VCAM-1, and investigated the ability of these antibodies to block VCAM-1-mediated cell adhesion to macrophages. We show that scFv antibodies against Ig-like domains 2 and 3 interfere with the ability of macrophages t","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Dec","modification":"2026-04-13T03:22:00.055Z","creation":"2026-04-13T03:12:22.614Z"},"accession":"S-EPMC11678699","cross_references":{"pubmed":["39769411"],"doi":["10.3390/ijms252413650"]}}