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Interaction of HLA-DR and CD74 at the cell surface of antigen-presenting cells by single particle image analysis

Karakikes, I and Morrison, IEG and O'Toole, P and Metodieva, G and Navarrete, CV and Gomez, J and Miranda-Sayago, JM and Cherry, RJ and Metodiev, M and Fernandez, N (2012) 'Interaction of HLA-DR and CD74 at the cell surface of antigen-presenting cells by single particle image analysis.' FASEB Journal, 26 (12). 4886 - 4896. ISSN 1530-6860

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Abstract

Major histocompatibility complex (MHC) class II-associated antigen presentation involves an array of interacting molecules. CD74, the cell surface isoform of the MHC class II-associated invariant chain, is one such molecule; its role remains poorly defined. To address this, we have employed a high-resolution single-particle imaging method for quantifying the colocalization of CD74 with human leukocyte antigen (HLA)-DR molecules on human fibroblast cells known for their capacity to function as antigen-presenting cells. We have also examined whether the colocalization induces internalization of HLA-DR using HA307-319, a "universal" peptide that binds specifically to the peptide-binding groove of all HLA-DR molecules, irrespective of their alleles. We have determined that 25 ± 1.3% of CD74 and 17 ± 0.3% of HLA-DR are colocalized, and the association of CD74 with HLA-DR and the internalization of HLA-DR are both inhibited by HA307-319. A similar inhibition of HLA-DR internalization was observed in freshly isolated monocyte-derived dendritic cells. A key role of CD74 is to translocate HLA-DR molecules to early endosomes for reloading with peptides prior to recycling to the cell surface. We conclude that CD74 regulates the balance of peptide-occupied and peptide-free forms of MHC class II at the cell surface. © FASEB.

Item Type: Article
Subjects: Q Science > QH Natural history > QH301 Biology
Divisions: Faculty of Science and Health > Life Sciences, School of
Depositing User: Jim Jamieson
Date Deposited: 22 Jan 2013 11:08
Last Modified: 20 Aug 2019 17:15
URI: http://repository.essex.ac.uk/id/eprint/5188

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