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Department of Molecular and Experimental Medicine, Scripps Research Institute, La Jolla, CA 92037
Cross-linking of Fc
RI on rat basophilic leukemia (RBL) cells
initiates a signaling cascade leading to degranulation of the cells and
the release of inflammatory mediators. Inhibitors that disrupt
microfilaments, such as latrunculin and cytochalasin D, do not cause
any degranulation on their own, but they do enhance FcRI-mediated
degranulation. Dose-response studies show a good correlation between
inhibition of actin polymerization and increased degranulation. In RBL
cells, latrunculin causes a decrease in basal levels of filamentous
actin (F-actin), while cytochalasin D does not. This is particularly
evident in the Triton-insoluble pool of F-actin which is highly
cross-linked and associated with the plasma membrane. A concentration
of 500 nM latrunculin decreases the basal level of Triton-insoluble
F-actin by 60–70% and total F-actin levels by 25%. Latrunculin
increases both the rate and extent of Ag-induced degranulation while
having no effect on pervanadate-induced degranulation. Pervanadate
activates the signaling pathways directly and bypasses the
cross-linking of the receptor. RBL cells, activated through FcRI in
the presence of latrunculin, show increased phospholipase activity as
well as increased tyrosine phosphorylation of Syk and increased
tyrosine phosphorylation of the receptor itself by the tyrosine kinase
Lyn. This indicates that the very earliest signaling events after
receptor cross-linking are enhanced. These results suggest that actin
microfilaments may interact, either directly or indirectly, with the
receptor itself and that they may regulate the signaling process at the
level of receptor phosphorylation. Microfilaments may possibly act by
uncoupling Lyn from the cross-linked receptor.
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