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
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 Chen, T. Y.
Right arrow Articles by Morrison, D. C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Chen, T. Y.
Right arrow Articles by Morrison, D. C.
Right arrowPubmed/NCBI databases
*Compound via MeSH
*Substance via MeSH

The Journal of Immunology, Vol 145, Issue 1 8-12, Copyright © 1990 by American Association of Immunologists

ARTICLES

Induction of macrophage-mediated tumor cytotoxicity by a hamster monoclonal antibody with specificity for lipopolysaccharide receptor

TY Chen, SW Bright, JL Pace, SW Russell and DC Morrison
Department of Microbiology, Molecular Genetics and Immunology, University of Kansas Medical Center, Kansas City 66103.

Experiments have been carried out to assess the immunostimulatory activity of a hamster IgM mAb (mAb5D3) with specificity for an 80-kDa LPS-binding protein expressed on murine macrophages and monocytes. The addition of mAb5D3 to cultures of murine bone marrow-derived macrophages activated these cells to become tumoricidal for mastocytoma cells in vitro. The activity of mAb5D3 was enhanced in the presence of IFN-gamma. Neither mAb5D3 nor LPS were able to activate macrophages from the LPS-hyporesponsive C3H/HeJ mouse, although these cells responded normally to heat-killed Listeria monocytogenes. The results of several experiments establish that the observed LPS-like activity of mAb5D3 was not due to contaminating endotoxin: 1) the activity of mAb5D3 but not LPS was heat labile at 100 degrees C; 2) the activity of LPS but not mAb5D3, was inhibited by addition of polymyxin B; and 3) quantitative estimates of endotoxin contamination by Limulus amoebocyte lysate reactivity. These experiments thus demonstrate that mAb5D3 can serve as an agonist for LPS-dependent macrophage responses and, when considered with those of our companion paper showing specificity of mAb5D3 for the 80-kDa LPS-binding protein, provide strong support for the concept that the 80-kDa LPS-binding protein previously identified serves as a functional receptor for LPS on murine macrophages.


This article has been cited by other articles:


Home page
 J Med MicrobiolHome page
A. S. SWIERZKO, T. KIRIKAE, F. KIRIKAE, M. HIRATA, M. CEDZYNSKI, A. ZIOLKOWSKI, Y. HIRAI, S. KUSUMOTO, T. YOKOCHI, and M. NAKANO
Biological activities of lipopolysaccharides of Proteus spp. and their interactions with polymyxin B and an 18-kDa cationic antimicrobial protein (CAP18)-derived peptide
J. Med. Microbiol., February 1, 2000; 49(2): 127 - 138.
[Abstract] [Full Text] [PDF]

Home page
 Antimicrob. Agents Chemother.Home page
T. Kirikae, F. Kirikae, S. Saito, K. Tominaga, H. Tamura, Y. Uemura, T. Yokochi, and M. Nakano
Biological Characterization of Endotoxins Released from Antibiotic-Treated Pseudomonas aeruginosa and Escherichia coli
Antimicrob. Agents Chemother., May 1, 1998; 42(5): 1015 - 1021.
[Abstract] [Full Text]

Home page
 Innate ImmunityHome page
C.L. Manthey and S.N. Vogel
Taxol: a promising endotoxin research tool
Innate Immunity, September 1, 1994; 1(3): 189 - 198.
[Abstract] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
This Website Copyright © 1990 by The American Association of Immunologists, Inc. All rights reserved.
All Contents Copyright © 1990 by The American Association of Immunologists, Inc. All rights reserved.