| First Author | Gao B | Year | 2002 |
| Journal | Immunity | Volume | 16 |
| Issue | 1 | Pages | 99-109 |
| PubMed ID | 11825569 | Mgi Jnum | J:140383 |
| Mgi Id | MGI:3813437 | Doi | 10.1016/s1074-7613(01)00260-6 |
| Citation | Gao B, et al. (2002) Assembly and antigen-presenting function of MHC class I molecules in cells lacking the ER chaperone calreticulin. Immunity 16(1):99-109 |
| abstractText | MHC class I molecules expressed in a calreticulin-deficient cell line (K42) assembled with beta 2-microglobulin (beta2-m) normally, but their subsequent loading with optimal peptides was defective. Suboptimally loaded class I molecules were released into the secretory pathway. This occurred despite the ability of newly synthesized class I to interact with the transporter associated with antigen processing (TAP) loading complex. The efficiency of peptide loading was reduced by 50%-80%, and impaired T cell recognition was observed for three out of four antigens tested. The peptide-loading function was specific to calreticulin, since the defect in K42 could be rectified by transfection with calreticulin but not a soluble form of calnexin, which shares its lectin-like activity. |
