Factors mediating cell—cell recognition and adhesion

Harrison, F. Lynne; Chesterton, C.J.

doi:10.1016/0014-5793(80)80428-5

Cited by 105 publications

(32 citation statements)

References 62 publications

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“…Soon similar galactoside-binding lectins were found and purified from different tissues, cultured untransformed cells and cancer cells (4,(9)(10)(11)(12)(13)(14)(15). It became clear that one tissue or even cell type could contain multiple different galactoside-binding lectins, with some often quite abundant.…”

Section: A the Originsmentioning

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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Section: A the Originsmentioning

confidence: 99%

Galectin History, Some Stories, and Some Outstanding Questions

Leffler

2018

TIGG

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“…Just as an intricate synthetic apparatus ensures to have a broad panel of 'code words' available (3)(4)(5)(6)(7)(8), the same is true for reaching diversity on the level of 'readers' of the sugar code: more than a dozen protein folds have developed the ability to specifically bind glycans (9)(10)(11)(12)(13)(14). Among them, the β-sandwich motif is a (15)(16)(17)(18)(19)(20)(21)(22)(23). Sequence divergence between (most) galectin genes in an organism does not affect the canonical specificity to galactose in glycans but modulates the activity profile, as seen in assays with synthetic and natural glycans as well as glycoconjugates (24)(25)(26)(27)(28)(29)(30)(31)(32).…”

Section: A Introductionmentioning

confidence: 99%

Members of the Galectin Network with Deviations from the Canonical Sequence Signature. 1. Galectin-Related Inter-Fiber Protein (GRIFIN)

Caballero¹,

Manning²,

Ludwig³

et al. 2018

TIGG

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Systematic databank-based sequence comparisons with the cDNA sequence for a lens-specific rat protein localized between lens fiber cells disclosed its similarity to galectins. In mammals, two sequence changes occur within the seven positions of amino acids commonly engaged in contacts to the β-galactoside core of glycans. Taking the compilation of GRIFIN genes to the level of diverse vertebrates revealed an exceptional variability: mammals shared alteration at two sites, birds and reptiles at only one site and amphibians and fish presented complete reconstitution. The homodimeric (proto-type) GRIFINs of chicken and zebrafish thus are active lectins. Crystallographical information for chicken GRIFIN illustrates the contact profile to lactose without one otherwise conserved site due to the Arg-to-Val substitution. That GRIFIN is enormously stable in vertebrate lenses, can act like a glue (or a bridge) due to its structure and interacts with α-crystallin (shown for murine GRIFIN) suggests a role in well-ordered packing of lens proteins. Referring to a likely analogy in plants, oligomeric leguminous lectins, β-sandwich proteins as galectins, are also assumed to participate in depositing and spatially organizing cell contents, here storage proteins in protein bodies and their contact to the membrane in carbohydrate-dependent and -independent manners, a likely case of structural and functional convergence. A. IntroductionThe realization of the unsurpassed capacity of glycans to store

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“…Cell surface glycoconjugates have been implicated in cell-cell adhesion in a number of biological systems (Harrison & Chesterton, 1980;Damsky et ai, 1984;Edelman et ai, 1985;Öbrink et ai, 1986;Schachner, 1989) and carbohydrate moieties appear to be directly involved in several cellular processes in mammalian reproductive biology, e.g. binding of spermatozoa to the zona pellucida (Ahuja, 1985;Wassarman, 1989), the interaction of cells in preimplantation mouse embryos (Bird & Kimber, 1984;Fendersen et ai, 1984;Kimber, 1988), the adhesion between cells of the uterine epithelium (Dutt et ai, 1987) and the initial attachment of the blastocyst to the uterine epithelium (Kimber et ai, 1988;Lindenberg et ai, 1988).…”

Section: Introductionmentioning

confidence: 99%