Expression of Binding Properties of Gal/GalNAc Reactive Lectins by Mammalian Glycotopes

Wu, Albert M.

doi:10.1007/978-1-4615-1267-7_4

Cited by 32 publications

(38 citation statements)

References 47 publications

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“…It is intriguing that reactive glycotopes for this lectin are widely distributed in the mammalian digestive system [5,6]. The results of this study show that this galectin is able to preferentially interact with distinct sets of β-galactosides from the panel of natural glycotopes [40,47,49].…”

Section: Discussionmentioning

confidence: 91%

“…For example, structure II, a common sequence recognized specifically by the galectin family, is about 16 times less active than L in G4-N (Figure 6a, curve 6 versus curve 13 and Table 3). Thus it is evident that the individual galectin has its own characteristic binding preferences as documented for Gal\GalNAc-specific plant lectins [40,49].…”

Section: Discussionmentioning

confidence: 93%

“…Fine-specificity differences may well be translated into distinct spectra of bound glycans, as noted for plant lectins [40], presumably connecting the presence of a certain endogenous lectin with, at least in part, expression of a characteristic set of cognate oligosaccharides. Besides employing oligosaccharides as inhibitors of ligand binding, determination of their avidity towards determinants in natural glycans is useful to map the profile of their reactive structures (geometrical parameters).…”

Section: Discussionmentioning

confidence: 99%

“…Numbers in parentheses indicate the sites of attachment for the human blood group A, B, H, Le a and Le b determinants (Table 1). These determinants as well as the structural units at the non-reducing end are the sources of lectin-reactive A/A h , B, I/II, T and Tn determinants [40,43,48] (for definitions and structures of these see the text). A megalosaccharide of 24 sugars has not been isolated.…”

Section: Figure 1 Proposed Representative Carbohydrate Side Chains Ofmentioning

confidence: 99%

“…Lac (curve 32, Figure 5) is 7872.9 ng and equal to 23 nmol ; Gal (curve 33, Figure 5) is 3.6i10 5 ng and equal to 2000 nmol. The symbols in parentheses indicate the human blood group activity and/or lectin determinants [40,49], which are shown in bold : …”

Section: Table 2 Binding Of Crd-i Of Galectin-4 Lectin To Human Bloodmentioning

confidence: 99%

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

Tsai

et al. 2002

Biochemical Journal

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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 carbohydraterecognition 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)\poly-saccharide 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, Galβ

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Section: Discussionmentioning

confidence: 91%

Section: Discussionmentioning

confidence: 93%

Section: Discussionmentioning

confidence: 99%

Section: Figure 1 Proposed Representative Carbohydrate Side Chains Ofmentioning

confidence: 99%

Section: Table 2 Binding Of Crd-i Of Galectin-4 Lectin To Human Bloodmentioning

confidence: 99%

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

Tsai

et al. 2002

Biochemical Journal

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Galactosides in glycoconjugates of Xenopus laevis testis shown by lectin histochemistry

Valbuena

Alonso

Madrid

et al. 2011

Microscopy Res & Technique

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The implication of galactosides and other glycoconjugates on spermatogenesis has been previously reported. Glycans show such a complex structure that it makes them very difficult to analyze. Lectin histochemistry is a helpful tool for the study of glycan composition. Lectin histochemistry can be combined with deglycosylation pretreatments to explore the glycan type to which carbohydrates are linked. The aim of the present work was the localization of galactose (Gal)-containing glycoconjugates in the testis of Xenopus laevis, a species widely used in cell, molecular and developmental biology. Gal specific lectins BPL, PNA, BSI-B4, MAA-I, and RCA-I, were used in combination with deglycosylation procedures. Except for BPL, all the lectins were reactive for several testicular tissues. Some of the lectins showed a different reactivity depending on the stage of spermatogenic development, suggesting that cell glycoconjugates are modified during spermatogenesis. The surface of primary spermatocytes was strongly labeled with lectins from peanut (PNA) and castor bean (RCA-I), which agrees with the presence of galactosyl-glycolipids reported in the cell membrane of mammalian spermatocytes. The acrosome was unexpectedly negative to all the lectins tested, whereas the acrosome of mammals and other amphibians has shown a high expression of glycoconjugates, including galactosides. The results obtained after deglycosylation by β-elimination or incubation with PNGase F, which respectively remove O- and N-linked oligosaccharides, allowed us to elucidate the nature of the labeled glycans. The strong expression of galactosides at the cell surface of spermatocytes and spermatids suggests the involvement of these glycans in cell adhesion mechanisms during spermatogenesis.

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Glycopeptide dendrimers. Part I

Niederhafner

Šebestı́k

Ježek

2007

Journal of Peptide Science

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Glycopeptide dendrimers are branched structures containing both carbohydrates and peptides. Various classes of these compounds differing in composition and structure are mentioned, together with their practical use spanning from catalysis, transport vehicles to synthetic vaccines. The main stress is given to glycopeptide dendrimers, namely multiple antigen glycopeptides (MAGs). In MAGs, the core, branches or both are composed of amino acids or peptides. Other classes of glycodendrimers (PAMAM, polypropylene imine, cyclodextrin, calixarene, etc.) are mentioned too, but to a smaller extent. Their syntheses, physicochemical properties and biological activities are given with many examples. Glycopeptide dendrimers can be used as inhibitors of cell surface protein-carbohydrate interactions, intervention with bacterial adhesion, for studying of recognition processes, diagnostics, imaging and contrast agents, mimetics, for complexation of different cationts, as site-specific molecular delivery systems, for therapeutic purposes, as immunodiagnostics and in drug design. Biomedical applications of glycopeptide dendrimers as drug and gene delivery systems are also given.

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Expression of Binding Properties of Gal/GalNAc Reactive Lectins by Mammalian Glycotopes

Cited by 32 publications

References 47 publications

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

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

Galactosides in glycoconjugates of Xenopus laevis testis shown by lectin histochemistry

Glycopeptide dendrimers. Part I

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