Neoglycoproteins as Tools in Glycohistochemistry

Gabius, Hans‐Joachim; Bardosi, A.

doi:10.1016/s0079-6336(11)80019-7

Cited by 69 publications

(36 citation statements)

References 136 publications

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“…The specificity of each antibody was checked by Western blotting (data not shown). The neoglycoconjugates were synthesized and biotinylated as described in detail elsewhere (Bovin and Gabius, 1995;Gabius and Bardosi, 1991;Nifant'ev et al, 1994Nifant'ev et al, , 1996. The control reactions for the application of the biotinylated probes included competitive inhibitions to ascertain sugar specificity; the omission of the incubation step with a labeled marker served to exclude any staining by the binding of kit reagents such as the mannose-rich glycoproteins horseradish peroxidase and avidin.…”

Section: Histochemical Procedures For Revealing the Presence Of Lewismentioning

confidence: 99%

Binding Sites for Lewis Antigens Are Expressed by Human Colon Cancer Cells and Negatively Affect Their Migration

Hittelet

Camby

Nagy

et al. 2003

Laboratory Investigation

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SUMMARY:In colon cancer, endothelial cell selectins can promote tumor cell attachment via interactions with sialylated Lewis antigens present at the surface of tumor cells, thereby facilitating tumor cell arrest and transmigration into the extravascular space. However, it is not known whether Lewis antigens interact with colon tumor cells and modify their migration. Our aim was to detect the presence of binding sites on human tumor cells for Lewis a/x antigens and their sialylated derivatives in vitro and in vivo and to analyze their influence on migration of colon cancer cells. The immunocytochemical and histochemical levels of expression of the four Lewis antigens were quantitatively determined in four human colon cancer cell lines and in in vivo nude mice xenografts. The levels of expression of specific binding sites for these sugar epitopes were determined by synthetic neoglycoconjugates. The influence of binding of these carbohydrate ligands on cancer cell migration was quantitatively evaluated by computer-assisted phase-contrast videomicroscopy performed on Matrigel culture supports either left uncoated or coated with neoglycoconjugate presenting synthetic Lewis a , sialyl Lewis a , Lewis x , or sialyl Lewis x antigens. The influence of the calcium concentration in the culture medium on the Lewis antigen-mediated effects was checked. Human colon cancer cells expressed significant amounts of specific binding sites detected by the synthetic probes in addition to the oligosaccharide epitopes. The expression levels differed considerably between the four cell lines and between in vitro and in vivo specimens. Cell migration analysis revealed that the four Lewis antigens markedly decreased the levels of migration of the HCT-15 and LoVo cancer cells. This effect depends on the calcium concentration in the culture medium. Binding sites for Lewis epitopes are present on colon cancer cells. The functional relevance of these sites is indicated by the negative influence on cell migration of a matrix containing the oligosaccharides as ligand parts. (Lab Invest 2003, 83:777-787).

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Section: Histochemical Procedures For Revealing the Presence Of Lewismentioning

confidence: 99%

Binding Sites for Lewis Antigens Are Expressed by Human Colon Cancer Cells and Negatively Affect Their Migration

Hittelet

Camby

Nagy

et al. 2003

Laboratory Investigation

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“…The expression of the galectin-1-and galectin-3-reactive sites was assessed by using biotinylated galectin-1 and galectin-3 on the basis of routine procedures. 47 The expression of the T antigen was detected by the application of biotinylated PNA, while that of the T antigen binding sites was shown by using a biotinylated carrier-immobilized T antigen, ie. by using the synthetic T antigen derived from a chemical preparation as a p-aminophenyl derivative, as a ligand part of a biotinylated neoglycoprotein.…”

Section: Immunohistochemistry and Ligand Histochemistrymentioning

confidence: 99%

Galectin-1 and Galectin-3 Binding Pattern Expression in Renal Cell Carcinomas

et al. 1999

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A b s t r a c t We studied 2 families of molecules whose role remains uncharacterized or obscure in the progress of renal cell carcinoma (RCC): galectins, a major class of glycoproteins, and the Thomsen-Friedenreich (T) One field of study offers a great deal of hope for the discovery of new RCC prognosticators. This field relates to the identification of specific molecules that have major roles in tumor (and thus abnormal) cell-cell and cell-extracellular matrix (ECM) interactions. ECMs in kidney essentially include glycoproteins, such as laminins and fibronectins, and also various types of collagens.Laminins and fibronectins are the natural binding sites for various types of integrins. These integrins are the molecular links between ECMs and several proteins (eg, vinculin, talin, zyxin, tensin, paxillin) A specific group of proteins, ie, cadherins and their related catenins, also have a major role in cell-cell interactions in RCCs. Indeed, a loss of cell adhesion is a critical 1 9 4

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“…This group also includes interleukin-2, which can physically link its receptor to the CD3-T-cell receptor complex via recognition of an oligomannosidic epitope (Zanetta et al, 1996;Zanetta, 1997). One of the examples given also calls attention to the nuclear localization of lectins, which can be further elaborated with neoglycoconjugates (Hubert et al, 1989;Gabius and Bardosi, 1991). The principle of modulating the structural properties of a lectin by sugar binding is not restricted to mammalian galectins but can also be found in other lectin (C-type) and animal (invertebrate) groups (Komano et al, 1992;Hatakeyama et al, 1996).…”

Section: Galectinsmentioning

confidence: 99%

“…They hereby prevent the necessary formation of Schiff bases between reaction partners on opposing cell surfaces (Rhodes et al, 1992). Addressing the possibility of pitfalls by adequate controls, custom-made neoglycoconjugates have proved especially to be valuable tools for detection of lectin activity as well as lectin localization, purification and characterization, detailed technical protocols for versatile applications being available (Stowell and Lee, 1980;Gabius, 1988Gabius, , 1991Monsigny et al, 1988;Kojima et al, 1990;Gabius and Gabius, 1991 Lee andLee, 1994, 1997;Bovin and Gabius, 1995;Danguy et al, 1995Danguy et al, , 1997Kiessling and Pohl, 1996;Roy, 1996 ;Kannan and Nair, 1997). The advances in this field, made possible by access to sophisticated techniques including genetic engineering and computer-assisted homology searches, have already ushered in an era of classification of animal lectins on the molecular level.…”

mentioning

confidence: 99%

Animal Lectins

Gabius

1997

European Journal of Biochemistry

435

342

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Protein and lipid glycosylation is no longer considered as a topic whose appeal is restricted to a limited number of analytical experts perseveringly pursuing the comprehensive cataloguing of structural variants. It is in fact arousing curiosity in various areas of basic and applied bioscience. Well founded by the conspicuous coding potential of the sugar part of cellular glycoconjugates which surpasses the storage capacity of oligonucleotide-or oligopeptide-based code systems, recognition of distinct oligosaccharide ligands by endogenous receptors, i.e. lectins and sugar-binding enzymes or antibodies, is increasingly being discovered to play salient roles in animal physiology. Having inevitably started with a descriptive stage, research on animal lectins has now undubitably reached maturity. Besides listing the current categories for lectin classification and providing presentations of the individual families and their presently delineated physiological significance, this review places special emphasis on tracing common structural and functional themes which appear to reverberate in nominally separated lectin and animal categories as well as lines of research which may come to fruition for medical sciences.Keywords: lectin ; glycoprotein; glycolipid; cell adhesion ; molecular recognition ; inflammation; infection ; fertilization ; signal transduction ; tumor biology.The putative multiplicity of functional implications for protein and lipid glycosylation has fueled vigorous and prolific research activities in the last decade. Although glycobiologists continue to be afflicted with the problem of precisely defining the physiological significance of the puzzling variability and complex pattern of carrier-attached saccharide chains, the notion of inherent ligand properties for recognitive protein-carbohydrate interactions is already well established

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Neoglycoproteins as Tools in Glycohistochemistry

Cited by 69 publications

References 136 publications

Binding Sites for Lewis Antigens Are Expressed by Human Colon Cancer Cells and Negatively Affect Their Migration

Binding Sites for Lewis Antigens Are Expressed by Human Colon Cancer Cells and Negatively Affect Their Migration

Galectin-1 and Galectin-3 Binding Pattern Expression in Renal Cell Carcinomas

Animal Lectins

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