Purification and some characteristics of a β‐galactoside binding soluble lectin from amphibian ovary

Cabutti, Nilda E. Fink de; Caron, Michel; Joubert, Raymonde; Elola, María T.; Bladier, Dominique; Herkovitz, Jorge

doi:10.1016/0014-5793(87)80314-9

Cited by 20 publications

(7 citation statements)

References 19 publications

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“…Other studies have also confirmed the role of laminin as a galectin-1 receptor [99,13]. Human T cell adhesion to ECM and to individual ECM components such as laminin, fibronectin and collagen IV has also been tested.…”

Section: Galectin-1 Receptorsmentioning

confidence: 86%

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Galectin-1 receptors in different cell types

et al. 2005

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Galectins are a family of animal lectins defined by two properties: shared amino acid sequences in their carbohydrate-recognizing domain, and beta-galactoside affinity. A wide variety of biological phenomena are related to galectins, i.e., development, differentiation, morphogenesis, tumor metastasis, apoptosis, RNA splicing, and immunoregulatory function. In this review, we will focus on galectin-1 receptors, and some of the mechanisms by which this lectin affects different cell types. Several galectin-1 receptors are discussed such as CD45, CD7, CD43, CD2, CD3, CD4, CD107, CEA, actin, extracellular matrix proteins such as laminin and fibronectin, glycosaminoglycans, integrins, a beta-lactosamine glycolipid, GM1 ganglioside, polypeptide HBGp82, glycoprotein 90 K/MAC-2BP, CA125 cancer antigen, and pre-B cell receptor.

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Section: Galectin-1 Receptorsmentioning

confidence: 86%

“…[10][11][12][13][14], in invertebrates [i.e. [15][16][17], in plants such as Agrocybe cylindracea and the mushroom Coprinus cinereus, and even in viruses [3].…”

mentioning

confidence: 99%

Galectin-1 receptors in different cell types

et al. 2005

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“…A number of galectins from amphibian species ( Bufo arenarum , Rana catesbeiana, X. laevis , and Ambystoma mexicanum subclasses Anura and Urodela) have been isolated and characterized from tissues ranging from embryos and tadpole larvae to adult tissues (including skin, muscle, and gonad) 6–9. Among these, taxa galectins exhibit considerable structural diversity, suggesting that structural and functional divergence in the galectin family may have occurred early in vertebrate evolution.…”

Section: Introductionmentioning

confidence: 99%

Soluble ?-galactosyl-binding lectin (galectin) from toad ovary: Crystallographic studies of two protein-sugar complexes

et al. 2000

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Galectin‐1, S‐type β‐galactosyl‐binding lectins present in vertebrate and invertebrate species, are dimeric proteins that participate in cellular adhesion, activation, growth regulation, and apoptosis. Two high‐resolution crystal structures of B. arenarum galectin‐1 in complex with two related carbohydrates, LacNAc and TDG, show that the topologically equivalent hydroxyl groups in the two disaccharides exhibit identical patterns of interaction with the protein. Groups that are not equivalent between the two sugars present in the second moiety of the disaccharide, interact differently with the protein, but use the same number and quality of interactions. The structures show additional protein‐carbohydrate interactions not present in previously reported lectin‐lactose complexes. These contacts provide an explanation for the enhanced affinity of galectin‐1 for TDG and LacNAc relative to lactose. Galectins are in dimer‐monomer equilibrium at physiological protein concentrations, suggesting that this equilibrium may be involved in organ‐specific regulation of activity. Comparison of B. arenarum with other galectin‐1 structures shows that among different galectins there are significant changes in accessible surface area buried upon dimer formation, providing a rationale for the variations observed in the free‐energies of dimerization. The structure of the B. arenarum galectin‐1 has a large cleft with a strong negative potential that connects the two binding sites at the surface of the protein. Such a striking characteristic suggests that this cleft is probably involved in interactions of the galectin with other intra or extra‐cellular proteins. Proteins 2000;40:378–388. © 2000 Wiley‐Liss, Inc.

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“…Lectin activities have been detected in several kinds of frog eggs (Kawauchi et al 1975), and from them several lectins were isolated (Roberson and Barondes 1982;Nishihara et al 1986;Fink de Cabutti et al 1987;Nitta et al 1987) and characterized (Nitta et al 1994;Iwama et al 2001) including some from Xenopus laevis. From R. catesbeiana egg, two lectins were reported and RCG1 has been the only galectin reported until now.…”

Section: Discussionmentioning

confidence: 98%

Antiproliferative effects of galectin-1 from Rana catesbeiana eggs on human leukemia cells and its binding proteins in human cells

Yasumitsu

Mochida

Yasuda

et al. 2011

In Vitro Cell.Dev.Biol.-Animal

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Galectin-1 from American bullfrog, RCG1, was isolated to high purity, and its growth inhibitory properties against human cells were examined. The results demonstrated that highly purified RCG1 induced large cell aggregates and revealed cell-type-specific growth inhibition. It significantly inhibited all human leukemia cell lines tested such as HL-60, U937, and K562 cells but did not inhibit human colon cancer cell line, Colo 201, or mouse mammary tumor cell line FM3A cells. Although most of the galectin-induced growth inhibitions are known to be apoptic, RCG1 induced growth arrest and neither apoptosis nor necrosis. RCG1-mediated growth inhibition was specifically suppressed by the corresponding sugar, lactose, but not by sucrose or even the structurally similar sugar, melibiose. Several studies have reported that galectin-mediated biological functions were modulated by charge modification. Since the high purity of RCG1 was demonstrated but a moderate degree of growth inhibition occurred, it is possible protein charge modification was examined by isoelectric focusing, and it was found to be highly heterogeneous in charge. RCG1 binding proteins in human cells were analyzed by lectin blotting using biotinylated RCG1, and lectin blotting revealed that in human cell extracts the specific proteins at molecular weight 37 and 50 kDa possessed the responsive features of RCG1 binding and lactose competition.

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Purification and some characteristics of a β‐galactoside binding soluble lectin from amphibian ovary

Cited by 20 publications

References 19 publications

Galectin-1 receptors in different cell types

Galectin-1 receptors in different cell types

Soluble ?-galactosyl-binding lectin (galectin) from toad ovary: Crystallographic studies of two protein-sugar complexes

Antiproliferative effects of galectin-1 from Rana catesbeiana eggs on human leukemia cells and its binding proteins in human cells

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