Antigen binding to receptors on immunocompetent cells

1977 ◽  
Vol 28 (2) ◽  
pp. 416-426 ◽  
Author(s):  
Charles DeLisi ◽  
Ajit K. Thakur
1974 ◽  
Vol 10 (3) ◽  
pp. 415-431 ◽  
Author(s):  
George I. Bell ◽  
Charles P. DeLisi

1971 ◽  
Vol 134 (5) ◽  
pp. 1083-1094 ◽  
Author(s):  
Hansruedy Ramseier ◽  
Jean Lindenmann

The possibility that a rat alloantiserum DA anti-Lewis possesses similar recognition structures for Lewis transplantation antigens, as do DA immunocompetent cells, was investigated by raising an antiserum against this alloantiserum in (Lewis x DA)F1 hosts. This antiserum, as well as one provoked by injecting DA lymphoid cells, was active against recognition structures for Lewis antigens of DA immunocompetent cells. The anti-(DA anti-Lewis) antiserum displayed the same degree of specificity as was found previously for anti-recognition structure sera prepared by injecting parental strain lymphoid cells into F1 hosts. Since the activities of antisera raised against cell-bound receptors or against the antigen-binding region of an immunoglobulin were indistinguishable, it was concluded that the functional part of cell-associated receptors might be structurally similar to the variable portion of an immunoglobulin.


Author(s):  
R.F. Stump ◽  
J.R. Pfeiffer ◽  
JC. Seagrave ◽  
D. Huskisson ◽  
J.M. Oliver

In RBL-2H3 rat basophilic leukemia cells, antigen binding to cell surface IgE-receptor complexes stimulates the release of inflammatory mediators and initiates a series of membrane and cytoskeletal events including a transformation of the cell surface from a microvillous to a lamellar topography. It is likely that dynamic properties of the IgE receptor contribute to the activation of these responses. Fewtrell and Metzger have established that limited crosslinking of IgE-receptor complexes is essential to trigger secretion. In addition, Baird and colleagues have reported that antigen binding causes a rapid immobilization of IgE-receptor complexes, and we have demonstrated an apparent increase with time in the affinity of IgE-receptor complexes for antigen.


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