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.

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.

scholarly journals Definition of a major p53 binding site on Ad2E1B58K protein and a possible nuclear localization signal on the Ad12E1B54K protein

Oncogene ◽  
1999 ◽  
Vol 18 (4) ◽  
pp. 955-965 ◽  
Author(s):  
Roger JA Grand ◽  
Julian Parkhill ◽  
Tadge Szestak ◽  
Susan M Rookes ◽  
Sally Roberts ◽  
...  
Keyword(s):  
Binding Site ◽  
Nuclear Localization ◽  
Nuclear Localization Signal ◽  
Localization Signal ◽  
Definition Of

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 A yeast protein possesses the DNA-binding properties of the adenovirus major late transcription factor.

1989 ◽  
Vol 9 (2) ◽  
pp. 820-822 ◽  
Author(s):  
L A Chodosh ◽  
S Buratowski ◽  
P A Sharp
Keyword(s):  
Transcription Factor ◽  
Dna Binding ◽  
Binding Site ◽  
Upstream Stimulatory Factor ◽  
Binding Properties ◽  
Yeast Saccharomyces Cerevisiae ◽  
Human Promoter ◽  
Late Transcription ◽  
Stimulatory Factor ◽  
Dna Binding Properties

The adenovirus major late transcription factor (MLTF), or upstream stimulatory factor, is a human promoter-specific transcription factor which recognizes the near-palindromic sequence GGCCACGTGACC (R. W. Carthew, L. A. Chodosh, and P. A. Sharp, Cell 43:439-448, 1985; L. A. Chodosh, R. W. Carthew, and P. A. Sharp, Mol. Cell. Biol. 6:4723-4733, 1986; M. Sawadogo and R. G. Roeder, Cell 43:165-175, 1985). We describe here a protein found in the yeast Saccharomyces cerevisiae which possesses DNA-binding properties that are virtually identical to those of human MLTF. These two proteins recognize the same DNA-binding site, make the same purine nucleotide contacts, and are affected in the same manner by mutations in the MLTF-binding site.

scholarly journals Characterization of the promoter elements required for hepatic and intestinal transcription of the human apoB gene: definition of the DNA-binding site of a tissue-specific transcriptional factor.

1990 ◽  
Vol 10 (6) ◽  
pp. 2653-2659 ◽  
Author(s):  
D Kardassis ◽  
M Hadzopoulou-Cladaras ◽  
D P Ramji ◽  
R Cortese ◽  
V I Zannis ◽  
...  
Keyword(s):  
Binding Site ◽  
Regulatory Elements ◽  
Apob Gene ◽  
Mobility Shift ◽  
Promoter Elements ◽  
Nuclear Extracts ◽  
Dna Binding Site ◽  
Gene Definition ◽  
Definition Of ◽  
Electrophoretic Mobility Shift Assays

The promoter elements important for intestinal and hepatic transcription of the human apoB gene have been localized downstream of nucleotide -150. Footprinting analysis using hepatic nuclear extracts identified four protected regions, -124 to -100, -97 to -93, -86 to -33, and +33 to +52. Gel electrophoretic mobility shift assays showed that multiple factors interact with the apoB sequence -86 to -33, while the region -88 to -61 binds a single nuclear factor. Methylation interference analysis and nucleotide substitution mutagenesis identified the binding site of the factor between residues -78 and -68. Binding competition experiments indicate that this factor recognizes the regulatory elements of other liver-specific genes.

Characterization of a specific binding site for angiotensin II in chicken liver

1997 ◽  
Vol 75 (6) ◽  
pp. 568-575 ◽  
Author(s):  
R Bouley ◽  
M Gosselin ◽  
H Plante ◽  
G Servant ◽  
J Pérodin ◽  
...  
Keyword(s):  
Angiotensin Ii ◽  
Binding Site ◽  
Specific Binding ◽  
Chicken Liver

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

scholarly journals FcαRI binding at the IgA1 CH2–CH3 interface induces long-range conformational changes that are transmitted to the hinge region

2018 ◽  
Vol 115 (38) ◽  
pp. E8882-E8891 ◽  
Author(s):  
Monica T. Posgai ◽  
Sam Tonddast-Navaei ◽  
Manori Jayasinghe ◽  
George M. Ibrahim ◽  
George Stan ◽  
...  
Keyword(s):  
Binding Site ◽  
Long Range ◽  
Conformational Changes ◽  
Lectin Binding ◽  
Coarse Grained ◽  
Alanine Scanning Mutagenesis ◽  
Long Distance ◽  
Receptor Binding Site ◽  
Binding Interface ◽  
Functional Dynamics

IgA effector functions include proinflammatory immune responses triggered upon clustering of the IgA-specific receptor, FcαRI, by IgA immune complexes. FcαRI binds to the IgA1–Fc domain (Fcα) at the CH2–CH3 junction and, except for CH2 L257 and L258, all side-chain contacts are contributed by the CH3 domain. In this study, we used experimental and computational approaches to elucidate energetic and conformational aspects of FcαRI binding to IgA. The energetic contribution of each IgA residue in the binding interface was assessed by alanine-scanning mutagenesis and equilibrium surface plasmon resonance (SPR). As expected, hydrophobic residues central to the binding site have strong energetic contributions to the FcαRI:Fcα interaction. Surprisingly, individual mutation of CH2 residues L257 and L258, found at the periphery of the FcαRI binding site, dramatically reduced binding affinity. Comparison of antibody:receptor complexes involving IgA or its precursor IgY revealed a conserved receptor binding site at the CH2–CH3 junction (or its equivalent). Given the importance of residues near the CH2–CH3 junction, we used coarse-grained Langevin dynamics simulations to understand the functional dynamics in Fcα. Our simulations indicate that FcαRI binding, either in an asymmetric (1:1) or symmetric (2:1) complex with Fcα, propagated long-range conformational changes across the Fc domains, potentially impacting the hinge and Fab regions. Subsequent SPR experiments confirmed that FcαRI binding to the Fcα CH2–CH3 junction altered the kinetics of HAA lectin binding at the IgA1 hinge. Receptor-induced long-distance conformational transitions have important implications for the interaction of aberrantly glycosylated IgA1 with anti-glycan autoantibodies in IgA nephropathy.

Sign in / Sign up

Export Citation Format

Share Document