Please use this identifier to cite or link to this item: http://ir.swu.ac.th/jspui/handle/123456789/14499
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://www.scopus.com/inward/record.uri?eid=2-s2.0-84891756544&doi=10.1021%2fmp4003909&partnerID=40&md5=75df0a33de86306173559d9484569faf
http://ir.swu.ac.th/jspui/handle/123456789/14499
ISSN: 15438384
Appears in Collections:Scopus 1983-2021

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