Cutting edge: CD91-independent cross-presentation of GRP94(gp96)-associated peptides.
GRP94(gp96) elicits CD8(+) T cell responses against its bound peptides, a process requiring access of its associated peptides into the MHC class I cross-presentation pathway of APCs. Entry into this pathway requires receptor-mediated endocytosis, and CD91 (low-density lipoprotein receptor-related protein) has been reported to be the receptor mediating GRP94 uptake into APC. However, a direct role for CD91 in chaperone-based peptide Ag re-presentation has not been demonstrated. We investigated the contribution of CD91 to GRP94 cell surface binding, internalization, and trafficking in APCs. Whereas a clear role for CD91 in alpha(2)-macroglobulin binding and uptake was readily obtained, the addition of excess CD91 ligand, activated alpha(2)-macroglobulin, or receptor-associated protein, an antagonist of all known CD91 ligands, did not affect GRP94 cell surface binding, receptor-mediated endocytosis, or peptide re-presentation. These data identify a CD91-independent, GRP94 internalization pathway that functions in peptide Ag re-presentation.
Duke Scholars
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- alpha-Macroglobulins
- Protein Transport
- Peptides
- Mice, Inbred C57BL
- Mice
- Macrophages
- Low Density Lipoprotein Receptor-Related Protein-1
- LDL-Receptor Related Protein-Associated Protein
- Immunology
- Endocytosis
Citation
Published In
DOI
ISSN
Publication Date
Volume
Issue
Start / End Page
Location
Related Subject Headings
- alpha-Macroglobulins
- Protein Transport
- Peptides
- Mice, Inbred C57BL
- Mice
- Macrophages
- Low Density Lipoprotein Receptor-Related Protein-1
- LDL-Receptor Related Protein-Associated Protein
- Immunology
- Endocytosis