scholarly journals Fine specificity of domain-I of recombinant tandem-repeat-type galectin-4 from rat gastrointestinal tract (G4-N)

2002 ◽  
Vol 367 (3) ◽  
pp. 653-664 ◽  
Author(s):  
Albert M. WU ◽  
June H. WU ◽  
Ming-Sung TSAI ◽  
Jia-Hau LIU ◽  
Sabine ANDRÉ ◽  
...  
Keyword(s):  
Blood Group ◽  
Lectin Binding ◽  
Binding Properties ◽  
Lectin Domain ◽  
Cell Matrix ◽  
Endogenous Lectins ◽  
Differential Binding ◽  
Definition Of ◽  
Domain I ◽  
Blood Group Abh

Galectins, a family of β-galactoside-specific endogenous lectins, are involved in regulating diverse activities such as proliferation/apoptosis, cell—cell (matrix) interaction and cell migration. It is presently unclear to what extent the carbohydrate fine specificities of the combining sites of mammalian galectins overlap. To address this issue, we performed an analysis of the carbohydrate-recognition domain (CRD-I) near the N-terminus of recombinant rat galectin-4 (G4-N) by the biotin/avidin-mediated microtitre plate lectin-binding assay with natural glycoproteins (gps)/polysaccharide and by the inhibition of galectin—glycan interactions with a panel of glycosubstances. Among the 35 glycans tested for lectin binding, G4-N reacted best with human blood group ABH precursor gps, and asialo porcine salivary gps, which contain high densities of the blood group Ii determinants Galβ1-3GalNAc (the mucin-type sugar sequence on the human erythrocyte membrane) and/or GalNAcα1-Ser/Thr (Tn), whereas this lectin domain reacted weakly or not at all with most sialylated gps. Among the oligosaccharides tested by the inhibition assay, Galβ1-3GlcNAcβ1-3Galβ1-4Glc was the best. It was 666.7 and 33.3 times more potent than Gal and Galβ1-3GlcNAc, respectively. G4-N has a preference for the β-anomer of Gal at the non-reducing ends of oligosaccharides with a Galβ1-3 linkage, over Galβ1-4 and Galβ1-6. The fraction of Tn glycopeptide from asialo ovine submandibular glycoprotein was 8.3 times more active than Galβ1-3GlcNAc. The overall carbohydrate specificity of G4-N can be defined as Galβ1-3GlcNAcβ1-3Galβ1-4Glc (lacto-N-tetraose)>Galβ1-4GlcNAcβ1-3Galβ1-4Glc (lacto-N-neo-tetraose) and Tn clusters>Galβ1-4Glc and GalNAcβ1-3Gal>Galβ1-3GalNAc>Galβ1-3GlcNAc>Galβ1-4GlcNAc>GalNAc>Gal. The definition of this binding profile provides the basis to detect differential binding properties relative to the other galectins with ensuing implications for functional analysis.

Carbohydrate specificity of a galectin from chicken liver (CG-16)

2001 ◽  
Vol 358 (3) ◽  
pp. 529-538 ◽  
Author(s):  
Albert M. WU ◽  
June H. WU ◽  
Ming-Sung TSAI ◽  
Herbert KALTNER ◽  
Hans-J. GABIUS
Keyword(s):  
Binding Site ◽  
Binding Assay ◽  
Lectin Binding ◽  
Chicken Liver ◽  
Inhibition Assay ◽  
Microtitre Plate ◽  
Animal Tissues ◽  
Binding Properties ◽  
Lectin Family ◽  
Definition Of

Owing to the expression of more than one type of galectin in animal tissues, the delineation of the functions of individual members of this lectin family requires the precise definition of their carbohydrate specificities. Thus, the binding properties of chicken liver galectin (CG-16) to glycoproteins (gps) and Streptococcus pneumoniae type 14 polysaccharide were studied by the biotin/avidin-mediated microtitre-plate lectin-binding assay and by the inhibition of lectin–glycan interactions with sugar ligands. Among 33 glycans tested for lectin binding, CG-16 reacted best with human blood group ABO (H) precursor gps and their equivalent gps, which contain a high density of d-galactopyranose(β1–4)2-acetamido-2-deoxy-d-glucopyranose [Gal(β1–4)GlcNAc] and Gal(β1–3)GlcNAc residues at the non-reducing end, but this lectin reacted weakly or not at all with A-,H-type and sialylated gps. Among the oligosaccharides tested by the inhibition assay, the tri-antennary Gal(β1–4)GlcNAc (Tri-II) was the best. It was 2.1×103 nM and 3.0 times more potent than Gal and Gal(β1–4)GlcNAc (II)/Gal(β1–3)GlcNAc(β1–3)Gal(β1–4)Glc (lacto-N-tetraose) respectively. CG-16has a preference for the β-anomer of Gal at the non-reducing end of oligosaccharides with a Gal(β1–4) linkage >Gal(β1–3)Gal(β1–6). From the results, it can be concluded that the combining site of this agglutinin should be a cavity type, and that a hydrophobic interaction in the vicinity of the binding site for sugar accommodation increases the affinity. The binding site of CG-16 is as large as a tetrasaccharide of the β-anomer of Gal, and is most complementary to lacto-N-tetraose and Gal(β1–4)GlcNAc related sequences.

Leguminous glycosidases: Hydrophobic and lectin binding properties

1989 ◽  
Vol 28 (2) ◽  
pp. 355-357 ◽  
Author(s):  
Wolfgang Einhoff ◽  
Harold Rüdiger
Keyword(s):  
Lectin Binding ◽  
Binding Properties

scholarly journals Improved procedure for the construction of neoglycolipids having antigenic and lectin-binding activities, from reducing oligosaccharides

1988 ◽  
Vol 256 (2) ◽  
pp. 661-664 ◽  
Author(s):  
M S Stoll ◽  
T Mizuochi ◽  
R A Childs ◽  
T Feizi
Keyword(s):  
Monoclonal Antibodies ◽  
Blood Group ◽  
Concanavalin A ◽  
Lectin Binding ◽  
Blood Group A ◽  
Naturally Occurring ◽  
Group A ◽  
High Mannose ◽  
B Blood Group

Conditions have been established for the rapid and efficient conjugation of reducing oligosaccharides (di- to deca-saccharides) to dipalmitoyl phosphatidylethanolamine. The resulting neoglycolipids derived from several naturally occurring oligosaccharides and a series of N-linked high-mannose-type oligosaccharides released by hydrazinolysis from RNAase B showed specific and potent reactivities, as appropriate, with monoclonal antibodies to blood group Lewis(b), blood group A or a stage-specific embryonic (SSEA-1) antigen, or the lectin concanavalin A.

Newly established human pancreatic carcinoma cell lines and their lectin binding properties

1993 ◽  
Vol 13 (1) ◽  
pp. 31-41
Author(s):  
Nobuyuki Nishimura ◽  
Seiji Saito ◽  
Yoshiki Kubota ◽  
Nan-yo Moto-o ◽  
Kuniko Taguchi ◽  
...  
Keyword(s):  
Pancreatic Carcinoma ◽  
Cell Lines ◽  
Carcinoma Cell ◽  
Lectin Binding ◽  
Binding Properties ◽  
Carcinoma Cell Lines ◽  
Human Pancreatic Carcinoma Cell

Differential binding properties of some opiates and opioid peptides

1979 ◽  
pp. 366-374 ◽  
Author(s):  
Ian Creese ◽  
Steven R. Childers ◽  
Rabi Simantov ◽  
Solomon H. Snyder
Keyword(s):  
Opioid Peptides ◽  
Binding Properties ◽  
Differential Binding
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