Soluble galactoside-binding vertebrate lectins: A protein family with common properties

Caron, Michel; Bladier, Dominique; Joubert, Raymonde

doi:10.1016/0020-711x(90)90226-s

Cited by 76 publications

(30 citation statements)

References 54 publications

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“…Galectin-9 is a member of the h-galactoside-binding galectin family of proteins (5)(6)(7)(8). Among the members of the galectin family, galectin-1 (9) and galectin-3 (10 -13) contribute to tissue invasion by and metastasis of several types of cancer cells, including breast cancer cells.…”

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confidence: 99%

Galectin-9 as a Prognostic Factor with Antimetastatic Potential in Breast Cancer

Irie¹,

Yamauchi

Kontani³

et al. 2005

Clinical Cancer Research

172

152

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Purpose: Galectin-9, a member of the h-galactoside^binding galectin family, induces aggregation of certain cell types.We assessed the contribution of galectin-9 to the aggregation of breast cancer cells as well as the relation between galectin-9 expression in tumor tissue and distant metastasis in patients with breast cancer. Experimental Design: Subclones of MCF-7 breast cancer cells with high or low levels of galectin-9 expression were established and either cultured on plastic dishes or transplanted into nude mice. The tumors of 84 patients with breast cancer were tested for galectin-9 expression by immunohistochemistry. The patients were followed up for 14 years. Results: MCF-7 subclones with a high level of galectin-9 expression formed tight clusters during proliferation in vitro, whereas a subclone (K10) with the lowest level of galectin-9 expression did not. However, K10 cells stably transfected with a galectin-9 expression vector aggregated in culture and in nude mice. Ectopic expression of galectin-9 also reduced MCF-7 cell adhesion to extracellular matrix proteins.Tumors of 42 of the 84 patients were galectin-9 positive, and those of 19 of the 21patients with distant metastasis were galectin-9 negative. None of the13 patients with galectin-9^positive tumors and lymph node metastasis up to level II manifested distant metastasis.The cumulative disease-free survival ratio for galectin-9^positive patients was more favorable than that for the galectin-9^negative group (P < 0.0001). Multivariate analysis revealed that galectin-9 status influenced distant metastasis independently of and to a greater extent than lymph node metastasis. Conclusions: Galectin-9 is a possible prognostic factor with antimetastatic potential in breast cancer.Distant metastasis is a major clinical determinant of the survival of individuals with breast cancer. The number of lymph node metastases (node status) has long been used to predict distant metastasis in breast cancer. The various biological markers proposed for the prediction of distant metastasis in breast cancer include loss of nm23 expression (1, 2), with increased expression of this gene induced by inhibition of DNA methylation also having been found to prevent distant metastasis (3). The levels of both total and low molecular weight cyclin E, as determined by immunoblot analysis, are also correlated with survival in patients with breast cancer, especially in those with node-negative cancer (4).However, none of these biological markers is as effective as node status in the prediction of distant metastasis or is suitable as an indicator of the need for adjuvant chemotherapy.Galectin-9 is a member of the h-galactoside-binding galectin family of proteins (5-8). Among the members of the galectin family, galectin-1 (9) and galectin-3 (10 -13) contribute to tissue invasion by and metastasis of several types of cancer cells, including breast cancer cells. Galectin-3 also serves as a marker for preoperative diagnosis of nodular thyroid lesions (14). We have recently shown ...

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mentioning

confidence: 99%

Galectin-9 as a Prognostic Factor with Antimetastatic Potential in Breast Cancer

Irie¹,

Yamauchi

Kontani³

et al. 2005

Clinical Cancer Research

172

152

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“…It is based on the conservation of a series of amino acid residues with relevance for the topology of the CRD (Caron et al, 1990;Harrison, 1991 ;Barondes et al, 1994;Kasai and Hirabayashi, 1996;Ohannesian and Lotan, 1997). The former designation S-type lectins should be abandoned due to a lack of precision.…”

Section: Galectinsmentioning

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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“…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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Soluble galactoside-binding vertebrate lectins: A protein family with common properties

Cited by 76 publications

References 54 publications

Galectin-9 as a Prognostic Factor with Antimetastatic Potential in Breast Cancer

Galectin-9 as a Prognostic Factor with Antimetastatic Potential in Breast Cancer

Animal Lectins

Members of the Galectin Network with Deviations from the Canonical Sequence Signature. 1. <i>G</i>alectin-<i>R</i>elated <i>I</i>nter-<i>F</i>iber Prote<i>in</i> (GRIFIN)

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