JBC Oz Biosciences

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Originally published In Press as doi:10.1074/jbc.M501233200 on February 23, 2005

J. Biol. Chem., Vol. 280, Issue 18, 17573-17578, May 6, 2005
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
280/18/17573    most recent
M501233200v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Demine, R.
Right arrow Articles by Walden, P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Demine, R.
Right arrow Articles by Walden, P.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Testing the Role of gp96 as Peptide Chaperone in Antigen Processing*

Rodion Demine and Peter Walden{ddagger}

From the Charité-University Medicine Berlin, Humboldt University, Clinical Research Group Tumor Immunology, Department of Dermatology and Allergy, D-10098 Berlin, Germany

gp96 is a 96-kDa glycoprotein of the endoplasmic reticulum that is believed to be involved in antigen processing as an intermediate carrier of peptides for presentation by major histocompatibility complex (MHC) class I molecules. This function implies that gp96 carries a large array of different peptides that represent the antigenicity of the cell and can serve all MHC class I molecules. So far, the evidence regarding these peptides is largely indirect and based on experiments where mice immunized with gp96 from tumor or virus-infected cells developed T cellular immune responses with the corresponding specificities. We analyzed by mass spectrometry peptides isolated from gp96 and found a number of different peptides derived from the proteins of different cellular compartments but mostly cytoplasm and nucleus. The sequences of these peptides provide information on the specificity of antigen processing and reveal structural requirements for binding to gp96 that only partially correspond to those of peptides presented by MHC class I molecules. The yield of peptides extracted from gp96 was far substoichiometric with an estimated occupancy of this chaperone of between 0.1% and 0.4%. These results strongly argue against a regular role for gp96 as a peptide chaperone in antigen processing.


Received for publication, February 2, 2005 , and in revised form, February 18, 2005.

* This work was supported by Deutsche Forschungsgemeinschaft Grants KFO 050-TP 1, Kl 427/11-1, and FOR299/1-2-TP 4. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

{ddagger} To whom correspondence should be addressed: Charité-University Medicine Berlin, Humboldt University, Dept. of Dermatology, Schumannstr. 20/21, D-10117 Berlin, Germany. Tel.: 49-30-450-518-031; Fax: 49-30-450-518-932; E-mail: peter.walden{at}charite.de.


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


This article has been cited by other articles:


Home page
J. Immunol.Home page
J. Robert, T. Ramanayake, G. D. Maniero, H. Morales, and A. S. Chida
Phylogenetic Conservation of Glycoprotein 96 Ability to Interact with CD91 and Facilitate Antigen Cross-Presentation
J. Immunol., March 1, 2008; 180(5): 3176 - 3182.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
M. K. Callahan, M. Garg, and P. K. Srivastava
Heat-shock protein 90 associates with N-terminal extended peptides and is required for direct and indirect antigen presentation
PNAS, February 5, 2008; 105(5): 1662 - 1667.
[Abstract] [Full Text] [PDF]


Home page
Int ImmunolHome page
C. Biswas, U. Sriram, B. Ciric, O. Ostrovsky, S. Gallucci, and Y. Argon
The N-terminal fragment of GRP94 is sufficient for peptide presentation via professional antigen-presenting cells
Int. Immunol., July 1, 2006; 18(7): 1147 - 1157.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2005 by the American Society for Biochemistry and Molecular Biology.