<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Perera B</submitter><funding>Therapeutic Innovation Australia (TIA)</funding><funding>Heart Foundation Future Leader Fellowship</funding><funding>Promoting Women Fellowship from the University of Queensland</funding><funding>Australian Government</funding><funding>Australian Research Council</funding><pagination>13650</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC11678699</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>25(24)</volume><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</pubmed_abstract><journal>International journal of molecular sciences</journal><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.</pubmed_title><pmcid>PMC11678699</pmcid><funding_grant_id>IC160100027</funding_grant_id><pubmed_authors>Pickett JR</pubmed_authors><pubmed_authors>Zacchi LF</pubmed_authors><pubmed_authors>Ta HT</pubmed_authors><pubmed_authors>Fercher C</pubmed_authors><pubmed_authors>Sester DP</pubmed_authors><pubmed_authors>Barretto FM</pubmed_authors><pubmed_authors>Perera B</pubmed_authors><pubmed_authors>Jones ML</pubmed_authors><pubmed_authors>Wu Y</pubmed_authors><pubmed_authors>Panagides N</pubmed_authors></additional><is_claimable>false</is_claimable><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.</name><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</description><dates><release>2024-01-01T00:00:00Z</release><publication>2024 Dec</publication><modification>2026-04-13T03:22:00.055Z</modification><creation>2026-04-13T03:12:22.614Z</creation></dates><accession>S-EPMC11678699</accession><cross_references><pubmed>39769411</pubmed><doi>10.3390/ijms252413650</doi></cross_references></HashMap>