HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Supplemental Data All Versions of this Article: M600302-MCP200v1 6/5/923    most recent Submit a response Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Glossary Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Marcilla, M. Articles by López de Castro, J. A. Search for Related Content PubMed PubMed Citation Articles by Marcilla, M. Articles by López de Castro, J. A. Social Bookmarking                      What's this?

Molecular & Cellular Proteomics 6:923-938, 2007.
© 2007 by The American Society for Biochemistry and Molecular Biology, Inc.

---

Research

Proteasome-independent HLA-B27 Ligands Arise Mainly from Small Basic Proteins^*,S

Miguel Marcilla, Juan J. Cragnolini and José A. López de Castro

From the Centro de Biología Molecular Severo Ochoa (Consejo Superior de Investigaciones Científicas and Universidad Autónoma de Madrid), Facultad de Ciencias, Universidad Autónoma, 28049 Madrid, Spain

Many of the constitutive peptide ligands of HLA-B27, a molecule strongly associated with spondyloarthritis, are proteasome-independent. Stable isotope tagging, mass spectrometry, and epoxomicin-mediated inhibition were used to determine their percentage, structural features, and parental proteins. Of 104 molecular species examined, 29.8% were proteasome-independent, paralleling the level of HLA-B27 re-expression in the presence of epoxomicin after acid stripping. Proteasome-dependent and -independent ligands differed little in peptide motifs, flanking sequences, and cellular localization of the parental proteins. In contrast, whereas the former set arose from proteins whose size and isoelectric point distribution largely reflected those in the human proteome, proteasome-independent ligands, other than a few matching signal sequences, were almost totally derived from small (about 6–16.5 kDa) and basic proteins, which account for only 6.6% of the human proteome. Thus, a non-proteasomal proteolytic pathway with strong preference for small proteins is responsible for a significant fraction of the HLA-B27-bound peptide repertoire.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				P. Gomez, C. Mavian, B. Galocha, N. Garcia-Medel, and J. A. Lopez de Castro Presentation of Cytosolically Stable Peptides by HLA-B27 Is Not Dependent on the Canonic Interactions of N-Terminal Basic Residues in the A Pocket J. Immunol., January 1, 2009; 182(1): 446 - 455. [Abstract] [Full Text] [PDF]

				J. J. Cragnolini and J. A. L. de Castro Identification of Endogenously Presented Peptides from Chlamydia trachomatis with High Homology to Human Proteins and to a Natural Self-ligand of HLA-B27 Mol. Cell. Proteomics, January 1, 2008; 7(1): 170 - 180. [Abstract] [Full Text] [PDF]