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Title: | Hyaluronic acid graft polymers displaying peptide antigen modulate dendritic cell response in vitro |
Authors: | Chittasupho C. Sestak J. Shannon L. Siahaan T.J. Vines C.M. Berkland C. |
Keywords: | gamma interferon hyaluronic acid intercellular adhesion molecule 1 interleukin 10 interleukin 17 interleukin 4 ovalbumin polymer tumor necrosis factor alpha animal cell animal experiment antigen presentation article cell adhesion cell culture cell surface conjugation controlled study cytokine production dendritic cell fluorescence microscopy immune response in vitro study lymphocyte proliferation macrophage mouse neutrophil nonhuman peptide synthesis priority journal protein binding T lymphocyte Animals Antigen-Presenting Cells CD8-Positive T-Lymphocytes Cells, Cultured Cytokines Dendritic Cells Enzyme-Linked Immunosorbent Assay Hyaluronic Acid Intercellular Adhesion Molecule-1 Lymphocyte Activation Mice Mice, Inbred C57BL Ovalbumin Peptide Fragments Polymers T-Lymphocytes, Regulatory |
Issue Date: | 2014 |
Abstract: | A novel oxime grafting scheme was utilized to conjugate an ICAM-1 ligand (LABL), a cellular antigen ovalbumin (OVA), or both peptides simultaneously to hyaluronic acid (HA). Samples of HA only and the various peptide grafted HA were found to bind to dendritic cells (DCs). HA with grafted LABL and OVA showed the greatest binding to DCs. Dendritic cells treated with HA, HA with grafted LABL, or HA with grafted LABL and OVA significantly suppressed T cell and DC conjugate formation and T cell proliferation and reduced proinflammatory cytokine production compared to untreated cells. These results suggest that HA serves as an effective backbone for multivalent ligand presentation for inhibiting T cell response to antigen presentation. In addition, multivalent display of both antigen and an ICAM-1 inhibitor (LABL) may enhance binding to DCs and could potentially disrupt cellular signaling leading to autoimmunity. © 2013 American Chemical Society. |
URI: | https://ir.swu.ac.th/jspui/handle/123456789/14499 https://www.scopus.com/inward/record.uri?eid=2-s2.0-84891756544&doi=10.1021%2fmp4003909&partnerID=40&md5=75df0a33de86306173559d9484569faf |
ISSN: | 15438384 |
Appears in Collections: | Scopus 1983-2021 |
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