|
|
||||||||
The Journal of Immunology, Vol 140, Issue 8 2585-2588, Copyright © 1988 by American Association of Immunologists
ARTICLES |
S Kitani, D Kraft, C Fischler, SE Mergenhagen and RP Siraganian
Laboratory of Microbiology and Immunology, National Institute of Dental Research, Bethesda, MD 20892.
A mAb that reacts with the high affinity IgE-R on the rat basophilic leukemia cells (RBL-2H3) was used to inhibit allergic reactions. In vitro, the intact mAb BA3 and its Fab fragment inhibited radiolabeled IgE binding to the RBL-2H3 cells. The mAb binds to the IgE-R with a higher affinity than does IgE. Whereas the intact mAb released histamine from the RBL-2H3 cells, the Fab was inactive. The addition of the Fab fragments to RBL-2H3 inhibited the IgE-mediated histamine release reaction. The Fab fragments also inhibited in vivo passive cutaneous reactions in rats when injected intradermally either before or after IgE. The injection of the mAb Fab i.v. before the injection of the IgE into the skin sites also inhibited reactions, although it was less effective. The results demonstrate that anti-R antibodies can be used as a model for inhibiting immediate hypersensitivity reactions.
This article has been cited by other articles:
![]() |
B. A. Helm, I. Sayers, A. Higginbottom, D. C. Machado, Y. Ling, K. Ahmad, E. A. Padlan, and A. P. M. Wilson Identification of the High Affinity Receptor Binding Region in Human Immunoglobulin E J. Biol. Chem., March 29, 1996; 271(13): 7494 - 7500. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |