Two Inositol 1,4,5-Trisphosphate Binding Sites in Rat Basophilic Leukemia Cells: Relationship between Receptor Occupancy and Calcium Release

Biochemistry ◽  
1994 ◽  
Vol 33 (47) ◽  
pp. 14359-14367 ◽  
Author(s):  
James Watras ◽  
Ion Moraru ◽  
Debra J. Costa ◽  
L. Allen Kindman
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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