Back to Search
Start Over
Selective release of some invariant chain-derived peptides from HLA-DR1 molecules at endosomal pH.
- Source :
-
The Journal of experimental medicine [J Exp Med] 1994 Aug 01; Vol. 180 (2), pp. 751-5. - Publication Year :
- 1994
-
Abstract
- The predominant peptides bound to major histocompatibility complex class II molecules expressed on human B cells are derived from a relatively limited number of self proteins. To determine whether any of the prebound self peptides might be released in endosomes during recycling, water-soluble HLA-DR1 molecules were incubated with a high affinity synthetic peptide at pH 4.0 and 7.0 at 37 degrees C. The resulting bound peptide repertoire was then acid extracted, and separated by reversed-phase high performance liquid chromatography. Using a combination of mass spectrometry and ultraviolet spectroscopy, prebound self peptides and newly bound synthetic peptide were characterized. Most self peptides bound to HLA-DR1 were not appreciably released during extended exposure to pH 4.0. However, some invariant chain-derived peptides were uniquely released at this pH.
Details
- Language :
- English
- ISSN :
- 0022-1007
- Volume :
- 180
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- The Journal of experimental medicine
- Publication Type :
- Academic Journal
- Accession number :
- 8046351
- Full Text :
- https://doi.org/10.1084/jem.180.2.751