Karakikes, Ioannis and Morrison, Ian EG and O'Toole, Peter and Metodieva, Gergana and Navarrete, Cristina V and Gomez, Jesus and Miranda‐Sayago, Jose M and Cherry, Richard J and Metodiev, Metodi and Fernandez, Nelson (2012) Interaction of HLA‐DR and CD74 at the cell surface of antigen‐presenting cells by single particle image analysis. The FASEB Journal, 26 (12). pp. 4886-4896. DOI https://doi.org/10.1096/fj.12-211466
Karakikes, Ioannis and Morrison, Ian EG and O'Toole, Peter and Metodieva, Gergana and Navarrete, Cristina V and Gomez, Jesus and Miranda‐Sayago, Jose M and Cherry, Richard J and Metodiev, Metodi and Fernandez, Nelson (2012) Interaction of HLA‐DR and CD74 at the cell surface of antigen‐presenting cells by single particle image analysis. The FASEB Journal, 26 (12). pp. 4886-4896. DOI https://doi.org/10.1096/fj.12-211466
Karakikes, Ioannis and Morrison, Ian EG and O'Toole, Peter and Metodieva, Gergana and Navarrete, Cristina V and Gomez, Jesus and Miranda‐Sayago, Jose M and Cherry, Richard J and Metodiev, Metodi and Fernandez, Nelson (2012) Interaction of HLA‐DR and CD74 at the cell surface of antigen‐presenting cells by single particle image analysis. The FASEB Journal, 26 (12). pp. 4886-4896. DOI https://doi.org/10.1096/fj.12-211466
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 HA 307-319. 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 |
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Uncontrolled Keywords: | dendritic cells; monocytes; phycobiliprotein |
Subjects: | Q Science > QH Natural history > QH301 Biology |
Divisions: | Faculty of Science and Health Faculty of Science and Health > Life Sciences, School of |
SWORD Depositor: | Unnamed user with email elements@essex.ac.uk |
Depositing User: | Unnamed user with email elements@essex.ac.uk |
Date Deposited: | 22 Jan 2013 11:08 |
Last Modified: | 30 Oct 2024 19:50 |
URI: | http://repository.essex.ac.uk/id/eprint/5188 |