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Science 6 March 1992: Vol. 255. no. 5049, pp. 1264 - 1266 DOI: 10.1126/science.1546329
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Articles
Science, Vol 255, Issue 5049, 1264-1266
Copyright © 1992 by American Association for the Advancement of Science
HLA-A2.1-associated peptides from a mutant cell line: a second pathway of antigen presentation
RA Henderson,
H Michel,
K Sakaguchi,
J Shabanowitz,
E Appella,
DF Hunt,
and
VH Engelhard
Department of Microbiology, University of Virginia School of Medicine, Charlottesville 22908.
Peptides extracted from HLA-A2.1 class I major histocompatibility complex (MHC) molecules expressed on the antigen processing mutant CEMx721.174.T2 were characterized by electrospray ionization-tandem mass spectrometry. Only seven dominant peptides were found, in contrast to over 200 associated with HLA-A2.1 on normal cells. These peptides were derived from the signal peptide domains of normal cellular proteins, were usually larger than nine residues, and were also associated with HLA-A2.1 in normal cells. These results suggest that proteolysis of signal peptide domains in the endoplasmic reticulum is a second mechanism for processing and presentation of peptides for association with class I molecules.
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- Dependence of Elevated Human Leukocyte Antigen Class I Molecule Expression on Increased Heavy Chain, Light Chain (beta 2-Microglobulin), Transporter Associated with Antigen Processing, Tapasin, and Peptide.
- D. R. Johnson and B. Mook-Kanamori (2000)
J. Biol. Chem.
275, 16643-16649
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