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Monomeric IgE stimulates signaling pathways in mast cells that lead to cytokine production and cell survival.
Mast cell signal transduction from the high-affinity IgE receptor.
- R. Siraganian
- Biology, ChemistryCurrent opinion in immunology
- 1 December 2003
IgE‐induced histamine release from rat basophilic leukemia cell lines: isolation of releasing and nonreleasing clones
- E. Barsumian, Chaviva Isersky, M. G. Petrino, R. Siraganian
- BiologyEuropean journal of immunology
The rat basophilic leukemia cell lines were cloned and the various sublines compared for their chromosome number, IgE‐mediated histamine release and for IgE surface receptors indicating that the mutational drift in culture is toward loss of histamine‐releasing capacity.
Transfection of Syk protein tyrosine kinase reconstitutes high affinity IgE receptor-mediated degranulation in a Syk-negative variant of rat basophilic leukemia RBL-2H3 cells
- J. Zhang, E. Berenstein, R. Evans, R. Siraganian
- Biology, ChemistryThe Journal of experimental medicine
- 1 July 1996
The identification of a variant of RBL-2H3 cells that has no detectable Syk by immunoblotting and by in vitro kinase reactions demonstrates that Syk plays a critical role in the early Fc epsilon RI-mediated signaling events, and demonstrates thatSyk activation occurs downstream of receptor phosphorylation, but upstream of most of the Fc EpsilonRI-mediated protein tyrosine phosphorylations.
Mast cell signaling: The role of protein tyrosine kinase Syk, its activation and screening methods for new pathway participants
Protein tyrosine kinase Syk in mast cell signaling.
The Protein-tyrosine Phosphatase SHP-2 Associates with Tyrosine-phosphorylated Adhesion Molecule PECAM-1 (CD31)*
- K. Sagawa, Teruaki Kimura, M. Swieter, R. Siraganian
- Biology, ChemistryThe Journal of Biological Chemistry
- 5 December 1997
It is found that PECAM-1 was also transiently tyrosine-phosphoryated after adherence of these cells to fibronectin and the binding of the protein-tyrosine phosphatase SHP-2, which could regulate receptor-mediated signaling in cells.
Monoclonal antibodies that inhibit IgE binding.
Protein-tyrosine kinase p72syk in high affinity IgE receptor signaling. Identification as a component of pp72 and association with the receptor gamma chain after receptor aggregation.
Monoclonal antibody AA4, which inhibits binding of IgE to high affinity receptors on rat basophilic leukemia cells, binds to novel alpha-galactosyl derivatives of ganglioside GD1b.