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


     
 

This Article
Right arrow Full Text (PDF)
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 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
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Chu, C. T.
Right arrow Articles by Pizzo, S. V.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Chu, C. T.
Right arrow Articles by Pizzo, S. V.

The Journal of Immunology, Vol 150, Issue 1 48-58, Copyright © 1993 by American Association of Immunologists

ARTICLES

Receptor-mediated antigen delivery into macrophages. Complexing antigen to alpha 2-macroglobulin enhances presentation to T cells

CT Chu and SV Pizzo
Department of Pathology, Duke University Medical Center, Durham, NC 27710.

Macrophages secrete alpha 2-macroglobulin (alpha 2M), a protein that may facilitate early Ag handling. alpha 2M is able to entrap and form covalent linkages with diverse proteins during a transient proteinase- activated state. The resulting complexes are rapidly endocytosed after binding to high affinity receptors. Such a system could be capable of efficiently delivering a multitude of proteins to macrophages. We have used T hybridoma clones that respond only to hen egg lysozyme, in a MHC- restricted manner, to probe the effect of complex formation on Ag uptake and processing by murine macrophages. Radiolabeled lysozyme was internalized more rapidly and to a greater extent when bound to alpha 2M than when unbound. Macrophages pulsed with lysozyme-alpha 2M- elastase complexes required 200 to 250 times less Ag than those pulsed with free lysozyme to achieve effective presentation to T cells. Adding equimolar amounts of alpha 2M-elastase complexes, or of alpha 2M- methylamine, to free lysozyme had no effect on basal lysozyme presentation. Receptor-recognized forms of alpha 2M, but not lysozyme or BSA, competed effectively for both uptake and presentation of lysozyme-alpha 2M-elastase complexes. These results indicate that proteinase-activated alpha 2M can enhance Ag processing by carrying Ag into macrophages through a receptor-mediated process.


This article has been cited by other articles:


Home page
 Physiol. Rev.Home page
A. P. Lillis, L. B. Van Duyn, J. E. Murphy-Ullrich, and D. K. Strickland
LDL Receptor-Related Protein 1: Unique Tissue-Specific Functions Revealed by Selective Gene Knockout Studies
Physiol Rev, July 1, 2008; 88(3): 887 - 918.
[Abstract] [Full Text] [PDF]

Home page
 J BiochemHome page
A. Banbula, L. S. Chang, W. F. Beyer, C. L. Bohra, G. J. Cianciolo, and S. V. Pizzo
The Properties of Rabbit {alpha}1-Macroglobulin upon Activation Are Distinct from Those of Rabbit and Human {alpha}2-Macroglobulins
J. Biochem., November 1, 2005; 138(5): 527 - 537.
[Abstract] [Full Text] [PDF]

Home page
 J. Immunol.Home page
J. P. Hart, M. D. Gunn, and S. V. Pizzo
A CD91-Positive Subset of CD11c+ Blood Dendritic Cells: Characterization of the APC that Functions to Enhance Adaptive Immune Responses against CD91-Targeted Antigens
J. Immunol., January 1, 2004; 172(1): 70 - 78.
[Abstract] [Full Text] [PDF]

Home page
 BloodHome page
M. Lin, D. R. Sutherland, W. Horsfall, N. Totty, E. Yeo, R. Nayar, X.-F. Wu, and A. C. Schuh
Cell surface antigen CD109 is a novel member of the alpha 2 macroglobulin/C3, C4, C5 family of thioester-containing proteins
Blood, March 1, 2002; 99(5): 1683 - 1691.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
C. L. Adlakha, J. P. Hart, and S. V. Pizzo
Kinetics of Nonproteolytic Incorporation of a Protein Ligand into Thermally Activated alpha 2-Macroglobulin. EVIDENCE FOR A NOVEL NASCENT STATE
J. Biol. Chem., November 2, 2001; 276(45): 41547 - 41552.
[Abstract] [Full Text] [PDF]

Home page
 J. Immunol.Home page
R. J. Binder, D. Karimeddini, and P. K. Srivastava
Adjuvanticity of {{alpha}}2-Macroglobulin, an Independent Ligand for the Heat Shock Protein Receptor CD91
J. Immunol., April 15, 2001; 166(8): 4968 - 4972.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
G. C. Howard, Y. Yamaguchi, U. K. Misra, G. Gawdi, A. Nelsen, D. L. DeCamp, and S. V. Pizzo
Selective Mutations in Cloned and Expressed alpha -Macroglobulin Receptor Binding Fragment Alter Binding to Either the alpha 2-Macroglobulin Signaling Receptor or the Low Density Lipoprotein Receptor-related Protein/alpha 2-Macroglobulin Receptor
J. Biol. Chem., June 14, 1996; 271(24): 14105 - 14111.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
L. G. Legrès, F. Pochon, M. Barray, F. Gay, S. Chouaib, and E. Delain
Evidence for the Binding of a Biologically Active Interleukin-2 to Human [IMAGE][IMAGE]-Macroglobulin
J. Biol. Chem., April 14, 1995; 270(15): 8381 - 8384.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
C. Falkenberg, M. Allhorn, I. B. Thøgersen, Z. Valnickova, S. V. Pizzo, G. Salvesen, B. Akerström, and J. J. Enghild
alpha(1)-Microglobulin Destroys the Proteinase Inhibitory Activity of alpha(1)-Inhibitor-3 by Complex Formation
J. Biol. Chem., March 3, 1995; 270(9): 4478 - 4483.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
G. Bhattacharjee, I. R. Asplin, S. M. Wu, G. Gawdi, and S. V. Pizzo
The Conformation-dependent Interaction of alpha 2-Macroglobulin with Vascular Endothelial Growth Factor. A NOVEL MECHANISM OF alpha 2-MACROGLOBULIN/GROWTH FACTOR BINDING
J. Biol. Chem., August 25, 2000; 275(35): 26806 - 26811.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
This Website Copyright © 1993 by The American Association of Immunologists, Inc. All rights reserved.
All Contents Copyright © 1993 by The American Association of Immunologists, Inc. All rights reserved.