Endogenous Lectins and Cell Adhesion in Embryonic Cells

Zalik, Sara E.; Milos, Nadine C.

doi:10.1007/978-1-4613-2141-5_5

Cited by 10 publications

(8 citation statements)

References 190 publications

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“…While most lectins have the ability to agglutinate cells, not all lectins are necessarily agglutinins. Although lectins were first described in plants in relation to their cell agglutinating properties (see Goldstein and Hayes 1978;Sharon and Lis 1989; for reviews), research in the last fifteen years research has shown that these molecules are also widespread in animal tissues of embryonic and adult origin, and in tumor cell lines (Barondes 1986;Gabius et al 1986;Lotan and Raz 1988;Lotan 1990;Zalik and Milos 1986). Animal lectins have been found associated with the cell surface, the cytoplasm and the cell nucleus (Barondes 1986;Jia and Wang 1988).…”

Section: Introductionmentioning

confidence: 99%

On the possible role of endogenous lectins in early animal development

Zalik

1991

Anat Embryol

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In this review I have tried to summarize the information available on the lectins of developing embryos. The emerging evidence indicates that during fertilization carbohydrate-binding proteins play a role in sperm adhesion and in the reorganization of the extracellular matrix of the fertilized egg. Results also indicate that in adult tissues lectins participate in cell recognition and adhesion, and that several galactose-binding lectins function as receptors for laminin and, in principle could also interact with polylactosamine groups of other extracellular matrix glycoproteins. Since in developing embryos lectins are located at the cell surface, and colocalize with extracellular matrix glycoproteins, they could play a role in transitory adhesive interactions and in the segregation of organ primordia. On the basis of experiments in cultured cell lines, it has been suggested that lectins are involved in lysosomal and nuclear glycoprotein transport. These carbohydrate-binding proteins could also regulate development by modulating these processes in the embryo. Since galactose-binding lectins are mitogenic, and are present in high concentration in the chick yolk sac, these proteins could be released into the embryonic circulation, bind to cells expressing appropriate receptors, and act as growth regulators, by modulating cell division of specific cell lineages.

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Section: Introductionmentioning

confidence: 99%

On the possible role of endogenous lectins in early animal development

Zalik

1991

Anat Embryol

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“…Secretion of lectins has been reported from muscle cells after fusion, and may play a role in adhesion at the surface of the muscle fiber (Ceri et al 1979;Barondes and Haywood-Reid 1981). It has also been suggested that endogenous muscle cell lectins are involved in fusion itself, but this is a matter of some controversy (reviewed by Zalik and Milos 1986).…”

Section: Discussionmentioning

confidence: 96%

“…This developmental regulation of lectin levels has led to suggestions that lectins may have important stage-specific roles in embryogenesis, by binding to their specific carbohydrate-bearing receptors. In particular, embryonic lectins have been suggested to function in cellular adhesion, either by forming or modulating adhesive bonds between cells, or by ordering the extracellular matrix (reviewed by Zalik and Milos 1986).…”

Section: Introductionmentioning

confidence: 99%

Localization of endogenous galactoside-binding lectin during morphogenesis ofXenopus laevis

Milos

Varma

et al. 1990

Anat Embryol

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A monoclonal antibody has been produced against Xenopus laevis galactoside-binding neural-crest-stage lectin. This antibody inhibits lectin-mediated hemagglutination. Using this antibody in conjunction with immunohistochemical techniques, lectin deposition has been studied in embryos and tadpoles at different stages of morphogenesis, from initial neural crest migration, up to the formation of a swimming tadpole. Lectin levels change during development in different regions of the embryo and tadpole, decreasing in migratory cells, and increasing in sites where cells become more adhesive to one another. The results suggest that galactoside-binding lectins may be an important class of cellular adhesion molecules during these stages of development.

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“…Sara Zalik et al published many studies 1979-1999 on galectins during early chick embryogenesis (78,83). In the later studies she reported interesting morphological disturbances from adding simple galectin inhibitors like thiodigalactoside or lactose (84,85).…”

Section: E Some Early Galectin-storiesmentioning

confidence: 99%

Galectin History, Some Stories, and Some Outstanding Questions

Leffler

2018

TIGG

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The proteins now called galectins were discovered about 1975 based on their galactoside-binding activity, in a quest to find proteins that decode complex cell-surface glycans, to take part in cell adhesion. They were defined and named in 1994 based on conserved β-galactoside binding sites found within their characteristic ~130 amino acid (aa) carbohydrate recognition domains (CRDs). However, already at their initial discovery, it was also realized that galectins reside in the cytosol or nucleus for much of their life time, and reach their galactoside ligands only after non-classical secretion that bypasses the Golgi apparatus. Here some of the early studies (mainly before 1994) will be summarized, and exemplified with some galectin stories. The phylogenetic relationships of vertebrate galectins will be summarized as a background. The galectin field has developed rapidly after 1994 in many directions. A few basic outstanding questions will be raised and briefly discussed. What determines galectin binding affinity and specificity for natural glycoconjugate ligands? What is the functional role of galectin fine specificity for carbohydrates? Is there a functional connection between on one hand the cytosolic and nuclear galectin functions and on the other extracellular/intravesicular activities? Are there regulatory loops? A. The OriginsThe first protein now named galectin was reported in 1975 and named electrolectin (1). It was isolated from the electric organ of electric eel, at the time a favored model tissue and source for analysis of nerve cell interactions and receptors because of its many multiplied synapses. The finding of abundant complex carbohydrates at cell surfaces in many tissues including the nervous system, combined with the discoveries of carbohydrates as plant lectin receptors, microbial receptors and blood-group antigens, had stimulated the thought of some glycocode (2-6). Carbohydrates would determine specificities in cell-cell recognition, and there should be proteins binding and recognizing them for this. So, to look for such proteins in the electric organ, Teichberg et al. tested the hemagglutination by tissue extracts, an activity well known for plant lectins, and considered a surrogate marker for possible ability to mediate cell-cell interaction. Having found hemagglutination activity, he tested the ability of various readily available sugars to inhibit it, and found specificity for terminal β-galactose with lactose and thiodigalactoside (TDG) to be most potent inhibitors. Based on this he then used specially treated agarose, with exposed galactose residues, to purify the protein by affinity chromatography. He also found hemagglutination activity with similar profile of inhibitory sugars in many mammalian tissues.Barondes et al., among pioneers in the area, had already found lectins (named discoidins) in cellular slime molds, a model of regulated cell-cell adhesion, using an analogues strategy (7,8).However, they did not at first find the lectin(s) found by Teichberg in animal tissues...

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Endogenous Lectins and Cell Adhesion in Embryonic Cells

Cited by 10 publications

References 190 publications

On the possible role of endogenous lectins in early animal development

On the possible role of endogenous lectins in early animal development

Localization of endogenous galactoside-binding lectin during morphogenesis ofXenopus laevis

Galectin History, Some Stories, and Some Outstanding Questions

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