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) Data Supplement All Versions of this Article: jimmunol.0900861v1 183/2/1083    most recent Alert me when this article is cited Alert me if a correction is posted Citation Map Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Google Scholar Articles by Pang, B. Articles by Neefjes, J. PubMed PubMed Citation Articles by Pang, B. Articles by Neefjes, J.

Direct Antigen Presentation and Gap Junction Mediated Cross-Presentation during Apoptosis¹

Baoxu Pang^2,*, Joost Neijssen^2,*, Xiaohang Qiao^*,, Lennert Janssen^*, Hans Janssen^*, Christoph Lippuner^3,* and Jacques Neefjes^4,*

^* Division of Cell Biology, The Netherlands Cancer Institute, Amsterdam, The Netherlands; and Center for Infection and Immunity, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China, and the Graduate School of the Chinese Academy of Sciences, Beijing, China

MHC class I molecules present peptides from endogenous proteins. Ags can also be presented when derived from extracellular sources in the form of apoptotic bodies. Cross-presentation of such Ags by dendritic cells is required for proper CTL responses. The fate of Ags in cells initiated for apoptosis is unclear as is the mechanism of apoptosis-derived Ag transfer into dendritic cells. Here we show that novel Ags can be generated by caspases and be presented by MHC class I molecules of apoptotic cells. Since gap junctions function until apoptotic cells remodel to form apoptotic bodies, transfer and cross-presentation of apoptotic peptides by neighboring and dendritic cells occurs. We thus define a novel phase in classical Ag presentation and cross-presentation by MHC class I molecules: presentation of Ags created by caspase activities in cells in apoptosis.

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.

¹ This work was supported by a grant from the Dutch Cancer Society (KWF).

² B.P. and J.N. contributed equally to this work.

³ Current address: Vetsuisse Faculty, University Zürich, and Institute of Parasitology and Section of Herd Health Management (Department of Farm Animals), Winterthurerstrasse 266a, CH-8057 Zürich, Switzerland.

⁴ Address correspondence and reprint requests to Dr. Jacques Neefjes, Division of Cell Biology, The Netherlands Cancer Institute, Plesmanlaan 121, 1066CX Amsterdam, The Netherlands. E-mail address: j.neefjes{at}nki.nl

⁵ Abbreviations used in this paper: DRiP, defective ribosomal product; BMDC, bone marrow-derived dendritic cell; CLSM, confocal laser scanning microscopy; Cx43, connexin43; DC, dendritic cell; F-Casp9, FKBP-caspase-9-IRES-GFP; FKBP, FK506 binding protein; FRAP, fluorescence recovery after photobleaching; PARP, poly(ADP-ribose) polymerase.

⁶ The online version of this article contains supplemental material.