Abstract
ε{lunate}BP (IgE-binding protein) is a 31,000 Mr protein originally identified in rat basophilic leukemia (RBL) cells. The protein is composed of two domains with the amino-terminal domain containing a highly conserved repetitive sequence and the carboxyl-terminal domain containing consensus sequences shared by other β-galactoside-binding soluble lectins. The protein has wide tissue distribution, is found on cell surfaces and in extracellular milieu. By combined efforts from several research groups including ours a multifunctional nature of this lectin began to emerge. This review emphasizes the following characteristics of ε{lunate}BP: (i) ε{lunate}BP is secreted by cells such as macrophages; (ii) like many other lectins, ε{lunate}BP functions at least bivalently; (iii) ε{lunate}BP has specificity for distinct oligosaccharide structures that have a terminal galactose not masked by sialic acids; and (iv) in addition to binding IgE, ε{lunate}BP binds to surfaces of various cell types via lectin-carbohydrate interaction. Importantly, ε{lunate}BP binds to the IgE receptor on mast cells. We propose that ε{lunate}BP can function as a modulatory protein on various cells by cross-linking critical cell surface glycoproteins. The proposed action of ε{lunate}BP on mast cells is presented as a model.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 187-195 |
| Number of pages | 9 |
| Journal | Immunopharmacology |
| Volume | 26 |
| Issue number | 3 |
| DOIs | |
| State | Published - 1993 |
Fingerprint
Keywords
- Animal lectin
- Glycobiology
- IgE
- Mast cell
- ε{lunate}-BP
ASJC Scopus subject areas
- Pharmacology
Cite this
Expression and function of an IgE-binding animal lectin (ε{lunate}BP) in mast cells. / Liu, Fu-Tong; Frigeri, Luciano G.; Gritzmacher, Christine A.; Hsu, Daniel K.; Robertson, Michael W.; Zuberi, Riaz I.
In: Immunopharmacology, Vol. 26, No. 3, 1993, p. 187-195.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Expression and function of an IgE-binding animal lectin (ε{lunate}BP) in mast cells
AU - Liu, Fu-Tong
AU - Frigeri, Luciano G.
AU - Gritzmacher, Christine A.
AU - Hsu, Daniel K.
AU - Robertson, Michael W.
AU - Zuberi, Riaz I.
PY - 1993
Y1 - 1993
N2 - ε{lunate}BP (IgE-binding protein) is a 31,000 Mr protein originally identified in rat basophilic leukemia (RBL) cells. The protein is composed of two domains with the amino-terminal domain containing a highly conserved repetitive sequence and the carboxyl-terminal domain containing consensus sequences shared by other β-galactoside-binding soluble lectins. The protein has wide tissue distribution, is found on cell surfaces and in extracellular milieu. By combined efforts from several research groups including ours a multifunctional nature of this lectin began to emerge. This review emphasizes the following characteristics of ε{lunate}BP: (i) ε{lunate}BP is secreted by cells such as macrophages; (ii) like many other lectins, ε{lunate}BP functions at least bivalently; (iii) ε{lunate}BP has specificity for distinct oligosaccharide structures that have a terminal galactose not masked by sialic acids; and (iv) in addition to binding IgE, ε{lunate}BP binds to surfaces of various cell types via lectin-carbohydrate interaction. Importantly, ε{lunate}BP binds to the IgE receptor on mast cells. We propose that ε{lunate}BP can function as a modulatory protein on various cells by cross-linking critical cell surface glycoproteins. The proposed action of ε{lunate}BP on mast cells is presented as a model.
AB - ε{lunate}BP (IgE-binding protein) is a 31,000 Mr protein originally identified in rat basophilic leukemia (RBL) cells. The protein is composed of two domains with the amino-terminal domain containing a highly conserved repetitive sequence and the carboxyl-terminal domain containing consensus sequences shared by other β-galactoside-binding soluble lectins. The protein has wide tissue distribution, is found on cell surfaces and in extracellular milieu. By combined efforts from several research groups including ours a multifunctional nature of this lectin began to emerge. This review emphasizes the following characteristics of ε{lunate}BP: (i) ε{lunate}BP is secreted by cells such as macrophages; (ii) like many other lectins, ε{lunate}BP functions at least bivalently; (iii) ε{lunate}BP has specificity for distinct oligosaccharide structures that have a terminal galactose not masked by sialic acids; and (iv) in addition to binding IgE, ε{lunate}BP binds to surfaces of various cell types via lectin-carbohydrate interaction. Importantly, ε{lunate}BP binds to the IgE receptor on mast cells. We propose that ε{lunate}BP can function as a modulatory protein on various cells by cross-linking critical cell surface glycoproteins. The proposed action of ε{lunate}BP on mast cells is presented as a model.
KW - Animal lectin
KW - Glycobiology
KW - IgE
KW - Mast cell
KW - ε{lunate}-BP
UR - http://www.scopus.com/inward/record.url?scp=0027427294&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0027427294&partnerID=8YFLogxK
U2 - 10.1016/0162-3109(93)90034-N
DO - 10.1016/0162-3109(93)90034-N
M3 - Article
C2 - 8288440
AN - SCOPUS:0027427294
VL - 26
SP - 187
EP - 195
JO - Immunopharmacology
JF - Immunopharmacology
SN - 0162-3109
IS - 3
ER -