Galectin LEC-6 Interacts with Glycoprotein F57F4.4 to Cooperatively Regulate the Growth of Caenorhabditis elegans

Takeuchi, Tomoharu; Nemoto-Sasaki, Yoko; Arata, Yoichiro; Kasai, Ken‐ichi

doi:10.1248/bpb.34.1139

Cited by 14 publications

(9 citation statements)

References 21 publications

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“…3B), because some previous reports suggested possible roles for the interaction between the Galb1-4Fuc unit of endogenous glycans and LEC-6 in the growth of C. elegans. 12,14 However, no significant differences were observed in the pattern of bands stained by the antibody among different developmental stages. Although this preliminary experiment did not support our previous findings, more detailed analysis such as at the level of individual proteins, and localization at the cellular and tissue levels, etc., are necessary.…”

Section: Western Blotting Analysis Using the Anti-galb1-4fuc Antibodymentioning

confidence: 91%

“…10e13 Others and we also demonstrated that interaction between LEC-6 and Galb1-4Fuc, which is located in the Nglycan(s) of glycoprotein F57F4.4, promotes growth in C. elegans. 12,14 On the other hand, an endogenous glycan ligand for another C. elegans galectin LEC-8 was reported to be devoid of this unit. 15 However, affinity for Galb1-4Fuc was confirmed in the majority of other C. elegans galectins and also in annexins, which were reported to bind both phospholipids and glycosaminoglycans, 16e18 by experiments using a chemically synthesized Galb1-4Fuc derivative.…”

Section: Introductionmentioning

confidence: 99%

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Preparation of a polyclonal antibody that recognizes a unique galactoseβ1-4fucose disaccharide epitope

Takeuchi

Nishiyama

Saito

et al. 2015

Carbohydrate Research

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Section: Western Blotting Analysis Using the Anti-galb1-4fuc Antibodymentioning

confidence: 91%

Section: Introductionmentioning

confidence: 99%

Preparation of a polyclonal antibody that recognizes a unique galactoseβ1-4fucose disaccharide epitope

Takeuchi

Nishiyama

Saito

et al. 2015

Carbohydrate Research

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“…Endogenous glycoproteins that bind to LEC-6 have been reported previously. [20][21][22][23] We recently suggested that F57F4.4 is the major glycoprotein ligand for LEC-6.…”

Section: Discussionmentioning

confidence: 99%

The DC2.3 Gene in Caenorhabditis elegans Encodes a Galectin That Recognizes the Galactose.BETA.1.RAR.4Fucose Disaccharide Unit

Nemoto-Sasaki

Takaı̈

Takeuchi

et al. 2011

Biological & Pharmaceutical Bulletin

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Galectins comprise a large family of b b-galactoside-binding proteins in animals and fungi. We previously isolated cDNAs of 10 galectin and galectin-like genes (lec-1 to lec-6 and lec-8 to lec-11) from Caenorhabditis elegans and characterized the carbohydrate-binding properties of their recombinant proteins. In the present study, we isolated cDNA corresponding to an open reading frame of the DC2.3a gene from C. elegans total RNA; this cDNA encodes another potential galectin. A recombinant DC2.3a protein was expressed in Escherichia coli and used for analysis. The protein displayed hemagglutinating activity against rabbit erythrocytes, bound to an asialofetuin-Sepharose column, and was eluted with lactose. Furthermore, frontal affinity chromatography (FAC) analysis confirmed that DC2.3a recognized oligosaccharides with a non-reducing terminal galactose. According to these results, we designated DC2.3 as lec-12. The carbohydrate-binding property of the recombinant DC2.3a/LEC-12a was essentially similar to that of LEC-6. Additionally, DC2.3a/LEC-12a and LEC-6 showed higher affinities for the galactoseb b1→ →4fucose (Galb b1→ →4Fuc) disaccharide than for N-acetyllactosamine. This suggests that the principal recognition unit is the Galb b1→ →4Fuc disaccharide as in the case of the C. elegans galectins. However, the recombinant DC2.3a/LEC-12a showed weak affinity for N-glycan E3, which was previously shown to be a preferential endogenous ligand for LEC-6. The DC2.3a/LEC-12a endogenous ligand structures appear to be somewhat different but contain the same galactose-fucose recognition motif.

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“…The preparation of a mouse gastric mucous fraction was performed as previously described. 23) Isolation and Analysis of Possible mGal-2-Ligands in Gastric Mucus by LC-MS/MS The preparation of an mGal-2-immobilized column was performed as previously described. 15) Gastric mucous fractions from three mice were treated with phosphate buffered saline (PBS) and 5% 2-mercaptoethanol overnight at 4°C and then disrupted by sonication.…”

Section: Preparation Of a Mouse Gastric Mucous Fractionmentioning

confidence: 99%

Potential Interaction between Galectin-2 and MUC5AC in Mouse Gastric Mucus

Tamura

Tanaka

Fujii

et al. 2020

Biological & Pharmaceutical Bulletin

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Galectins are a group of animal lectins characterized by their specificity for β-galactosides. Of these, galectin-2 (Gal-2) is predominantly expressed in the gastrointestinal tract. In the current study, we used a mouse gastric mucous fraction to investigate whether Gal-2 is secreted from epithelial cells and identify its potential ligands in gastric mucus. Gal-2 was detected in the mouse gastric mucous fraction and could be eluted from it by the addition of lactose. Affinity chromatography using recombinant mouse galectin-2 (mGal-2)-immobilized adsorbent and subsequent LC-MS/MS identified MUC5AC, one of the major gastric mucin glycoproteins, as a potential ligand of mGal-2. Furthermore, MUC5AC was detected in the mouse gastric mucous fraction by Western blotting, and recombinant mGal-2 was adsorbed to this fraction in a carbohydrate-dependent manner. These results suggested that Gal-2 and MUC5AC in mouse gastric mucus interact in a β-galactoside-dependent manner, resulting in a stronger barrier structure protecting the mucosal surface.

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Galectin LEC-6 Interacts with Glycoprotein F57F4.4 to Cooperatively Regulate the Growth of Caenorhabditis elegans

Cited by 14 publications

References 21 publications

Preparation of a polyclonal antibody that recognizes a unique galactoseβ1-4fucose disaccharide epitope

Preparation of a polyclonal antibody that recognizes a unique galactoseβ1-4fucose disaccharide epitope

The DC2.3 Gene in Caenorhabditis elegans Encodes a Galectin That Recognizes the Galactose.BETA.1.RAR.4Fucose Disaccharide Unit

Potential Interaction between Galectin-2 and MUC5AC in Mouse Gastric Mucus

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