The Journal of Experimental Medicine
Avanti Polar Lipids, Inc.
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents

Published 19 August 2002. doi:10.1084/jem.20020327
This Article
Right arrow Full Text
Right arrow Full Text (PDF, 305K)
Right arrow PPT slides of all figures
Right arrow Alert me when this article is cited
Right arrow Citation Map
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new content in the JEM
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Lennon-Duménil, A.-M.
Right arrow Articles by Lagaudrière-Gesbert, C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Lennon-Duménil, A.-M.
Right arrow Articles by Lagaudrière-Gesbert, C.
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?
© Rockefeller University Press, 0022-1007/2002/8/529/ $5.00
The Journal of Experimental Medicine, Volume 196, Number 4, August 19, 2002 529-540

Analysis of Protease Activity in Live Antigen-presenting Cells Shows Regulation of the Phagosomal Proteolytic Contents During Dendritic Cell Activation

Ana-Maria Lennon-Duménil1, Arnold H. Bakker1, René Maehr1, Edda Fiebiger1, Herman S. Overkleeft1, Mario Rosemblatt2, Hidde L. Ploegh1 and Cécile Lagaudrière-Gesbert1

1 Department of Pathology, Harvard Medical School, Boston, MA 02115
2 Departamento de Biologia, Facultad de Ciencias, Universidad de Chile, 6842301 Santiago, Chile

Address correspondence to Hidde L. Ploegh, Department of Pathology, 200 Longwood Avenue, Building 2, Room 137, Boston, MA 02115. Phone: 617-432-4777; Fax: 617-432-4775; E-mail: ploegh{at}hms.harvard.edu

Here, we describe a new approach designed to monitor the proteolytic activity of maturing phagosomes in live antigen-presenting cells. We find that an ingested particle sequentially encounters distinct protease activities during phagosomal maturation. Incorporation of active proteases into the phagosome of the macrophage cell line J774 indicates that phagosome maturation involves progressive fusion with early and late endocytic compartments. In contrast, phagosome biogenesis in bone marrow–derived dendritic cells (DCs) and macrophages preferentially involves endocytic compartments enriched in cathepsin S. Kinetics of phagosomal maturation is faster in macrophages than in DCs. Furthermore, the delivery of active proteases to the phagosome is significantly reduced after the activation of DCs with lipopolysaccharide. This observation is in agreement with the notion that DCs prevent the premature destruction of antigenic determinants to optimize T cell activation. Phagosomal maturation is therefore a tightly regulated process that varies according to the type and differentiation stage of the phagocyte.

Key Words: antigen processing • cathepsin • active site–directed probe • phagocytosis • phagosomal maturation


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 | Help | Feedback | Subscriptions | Archive | Search
TABLE OF CONTENTS