Interaction of monoclonal antibodies with the IgE-receptor on rat mast cells and rat basophilic leukemia (RBL) cells

1986 ◽  
Vol 17 (5-6) ◽  
pp. 418-426 ◽  
Author(s):  
G. Micklefield ◽  
W. König ◽  
Ph. Pfeiffer ◽  
A. Bohn
1987 ◽  
Vol 20 (3-4) ◽  
pp. 216-218 ◽  
Author(s):  
H. Repke ◽  
N. Rossow ◽  
S. Savoly ◽  
J. Odarjuk ◽  
L. Karawajew ◽  
...  

1997 ◽  
Vol 110 (6) ◽  
pp. 771-780 ◽  
Author(s):  
J.R. Apgar

Rat basophilic leukemia cells will adhere to and spread out on fibronectin coated surfaces in an integrin dependent manner. Adhesion and spreading on fibronectin leads to increased degranulation, inositol phosphate production, phospholipase D activation, and increased production of prostaglandin D2 and leukotriene C4 when the cells are activated through the high affinity IgE receptor. Rat basophilic leukemia cells will also adhere to surfaces coated with anti-rat class I antibodies, poly-L-lysine, and a lectin purified from Tetragonolobus purpureas. In all cases, antigen activated cells, which were adherent, displayed increased signaling, degranulation and eicosanoid production as compared to cells which were non-adherent. Cells which adhere to either anti-rat class I antibodies or poly-L-lysine also spread even though this is not mediated through integrins. In contrast, adhesion to the lectin from Tetragonolobus did not cause any appreciable spreading unless the cells were also triggered through the IgE receptor. Cells were also able to bind to fibronectin immobilized on polystyrene beads which mimics adhesion but does not allow spreading. However, these cells exhibited no increased signaling, degranulation, or eicosanoid production. Furthermore, rat basophilic leukemia cells can be modified by incubating them in the presence of biotinylated-phosphatidylserine which becomes incorporated into the membrane. These modified cells will adhere to streptavidin coated plates while unmodified cells will not. However, these modified cells do not spread, even after activation with antigen, and they show no increased degranulation or production of eicosanoids. These results indicate that adhesion itself is not sufficient for upregulation of the cells in response to antigen and that spreading of the cells may be the critical component.


1991 ◽  
Vol 2 (3) ◽  
pp. 181-191 ◽  
Author(s):  
J R Apgar

Crosslinking of the IgE receptor on the surface of rat basophilic leukemia (RBL) cells by multivalent antigen induces an association of these receptors with the detergent-insoluble membrane skeleton. Detergent insolubility of the receptor can also be induced on purified plasma membranes isolated from RBL cells by the use of either IgE oligomers or IgE monomers plus multivalent antigen. The critical event in initiating this interaction between the receptor and the membrane skeleton is cross-linking of the receptor. This association is rapid, and, when triggered by multivalent antigen, it is quickly reversed by the addition of excess monovalent antigen. The fact that this association occurs with the use of purified plasma membranes indicates that all of the components necessary for this interaction are present in the plasma membrane and that intracellular components are not required. Although crosslinking of the receptor activates phospholipase C and phospholipase A2 leading to the generation of several second messengers, none of these signaling mechanisms appears to be involved in IgE receptor interaction with the membrane skeleton. This interaction cannot be induced by phorbol 12-myristate 13-acetate (PMA), ionomycin, or a combination of these two reagents, although this will result in degranulation. Furthermore, receptor detergent insolubility is temperature independent when triggered by multivalent antigen, thus indicating that enzyme-catalyzed reactions are not important. This was verified by the fact that a variety of inhibitors that block phosphatidylinositol metabolism, arachidonic acid metabolism, Ca2+ influx, and protein kinase C (PKC) activation had no effect on antigen-induced association of the receptor with the membrane skeleton. These results indicate that the signaling mechanisms leading to the degranulation response are not involved in the association of the crosslinked receptor with the membrane skeleton.


1994 ◽  
Vol 111 (4) ◽  
pp. 1179-1183 ◽  
Author(s):  
U.G. Friis ◽  
T. Johansen ◽  
N.A. Hayes ◽  
J.C. Foreman

1979 ◽  
Vol 9 (3) ◽  
pp. 219-224 ◽  
Author(s):  
Horst Mossmann ◽  
Balthasar Schmitz ◽  
Wolfgang Lauer ◽  
Uta Staufier ◽  
Marina Gehrung ◽  
...  

1983 ◽  
Vol 80 (10) ◽  
pp. 3050-3053 ◽  
Author(s):  
B. L. Hempstead ◽  
C. W. Parker ◽  
A. Kulczycki

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