Abstract
IgE-binding protein (ε{lunate}BP) is a β-galactoside-binding animal lectin identified by its affinity for IgE. We have reported that ε{lunate}BP also binds the mast cell high-affinity IgE receptor (Fcε{lunate}RI), via lectin-carbohydrate interaction. We have now studied the physiological significance of ε{lunate}BP-IgE-Fcε{lunate}RI interactions in mast cell activation using rat basophilic leukemia (RBL) cells as the model system. We report here that both unsensitized and IgE-sensitized RBL cells are activated upon exposure to ε{lunate}BP-coated surfaces. Activation of RBL cells by the lectin ε{lunate}BP can be significantly inhibited by appropriate saccharides. Exposure of RBL cells to ε{lunate}BP-coated surfaces caused cell spreading similar to that caused from adherence to fibronectin-coated surfaces. However, ε{lunate}BP by itself caused mediator release whereas fibronectin only potentiated antigen-mediated activation of RBL cells. Under appropriate conditions, ε{lunate}BP, therefore, has the potential to activate mast cells culminating in augmentation of an inflammatory response.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 1-12 |
| Number of pages | 12 |
| Journal | Cellular Immunology |
| Volume | 156 |
| Issue number | 1 |
| DOIs | |
| State | Published - Jun 1994 |
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ASJC Scopus subject areas
- Immunology
- Cell Biology
Cite this
Activation of Rat Basophilic Leukemia Cells by ε{lunate}BP, an IgE-Binding Endogenous Lectin. / Zuberi, Riaz I.; Frigeri, Luciano G.; Liu, Fu-Tong.
In: Cellular Immunology, Vol. 156, No. 1, 06.1994, p. 1-12.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Activation of Rat Basophilic Leukemia Cells by ε{lunate}BP, an IgE-Binding Endogenous Lectin
AU - Zuberi, Riaz I.
AU - Frigeri, Luciano G.
AU - Liu, Fu-Tong
PY - 1994/6
Y1 - 1994/6
N2 - IgE-binding protein (ε{lunate}BP) is a β-galactoside-binding animal lectin identified by its affinity for IgE. We have reported that ε{lunate}BP also binds the mast cell high-affinity IgE receptor (Fcε{lunate}RI), via lectin-carbohydrate interaction. We have now studied the physiological significance of ε{lunate}BP-IgE-Fcε{lunate}RI interactions in mast cell activation using rat basophilic leukemia (RBL) cells as the model system. We report here that both unsensitized and IgE-sensitized RBL cells are activated upon exposure to ε{lunate}BP-coated surfaces. Activation of RBL cells by the lectin ε{lunate}BP can be significantly inhibited by appropriate saccharides. Exposure of RBL cells to ε{lunate}BP-coated surfaces caused cell spreading similar to that caused from adherence to fibronectin-coated surfaces. However, ε{lunate}BP by itself caused mediator release whereas fibronectin only potentiated antigen-mediated activation of RBL cells. Under appropriate conditions, ε{lunate}BP, therefore, has the potential to activate mast cells culminating in augmentation of an inflammatory response.
AB - IgE-binding protein (ε{lunate}BP) is a β-galactoside-binding animal lectin identified by its affinity for IgE. We have reported that ε{lunate}BP also binds the mast cell high-affinity IgE receptor (Fcε{lunate}RI), via lectin-carbohydrate interaction. We have now studied the physiological significance of ε{lunate}BP-IgE-Fcε{lunate}RI interactions in mast cell activation using rat basophilic leukemia (RBL) cells as the model system. We report here that both unsensitized and IgE-sensitized RBL cells are activated upon exposure to ε{lunate}BP-coated surfaces. Activation of RBL cells by the lectin ε{lunate}BP can be significantly inhibited by appropriate saccharides. Exposure of RBL cells to ε{lunate}BP-coated surfaces caused cell spreading similar to that caused from adherence to fibronectin-coated surfaces. However, ε{lunate}BP by itself caused mediator release whereas fibronectin only potentiated antigen-mediated activation of RBL cells. Under appropriate conditions, ε{lunate}BP, therefore, has the potential to activate mast cells culminating in augmentation of an inflammatory response.
UR - http://www.scopus.com/inward/record.url?scp=0028237187&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0028237187&partnerID=8YFLogxK
U2 - 10.1006/cimm.1994.1148
DO - 10.1006/cimm.1994.1148
M3 - Article
C2 - 8200029
AN - SCOPUS:0028237187
VL - 156
SP - 1
EP - 12
JO - Cellular Immunology
JF - Cellular Immunology
SN - 0008-8749
IS - 1
ER -