Production and characterization of a monoclonal antibody able to discriminate galectin-1 from galectin-2 and galectin-3

Cornillot, Jean Denis; Pontet, Michel; Dupuy, Catherine; Chadli, Ahmed; Caron, Michel; Joubert‐Caron, Raymonde; Bourin, Philippe; Bladier, Dominique

doi:10.1093/glycob/8.5.425

Cited by 5 publications

(3 citation statements)

References 47 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The potential for cross-reactivities had been noticed in initial studies (Cerra et al 1984;Carding et al 1985a, b;Hinek et al 1988;Wasano and Yamamoto 1989). Rigorous controls to exclude side reactions with homologous proteins on cells and in tissues are thus necessary, as done for galectin-1 and -3 (Cornillot et al 1998;Kopitz et al 1998;Schwarz et al 1999). Having made suitable tools available, we herein extend our study of galectins in bovine development.…”

Section: Introductionmentioning

confidence: 81%

Galectin-1 and galectin-3 in fetal development of bovine respiratory and digestive tracts

Kaltner

Heck

et al. 2002

Cell and Tissue Research

View full text Add to dashboard Cite

Histochemical monitoring of developmental processes is presently centered on protein-protein interactions. However, oligosaccharides have the potential to store and transmit biological information. Carbohydrate chains of cellular glycoconjugates present determinants for binding of endogenous lectins. This interaction can be relevant for developmental processes. In fact, beta-galactosides and their derivatives serve as ligands for members of the lectin family of galectins. Since it is unclear to what extent functions of different galectins differ or overlap, hereby introducing redundancy into this system, monitoring of galectin presence during tissue maturation should include more than one type of galectin (galectin fingerprinting). Here, we focus on the two most frequently described ones, namely the homodimeric prototype galectin-1 and the chimera-type galectin-3, the latter one so far not characterized from bovine tissue. In the first step, we have detected its presence biochemically in addition to the abundant galectin-1 in bovine respiratory and digestive tracts during development. Evidently, diversification of the primitive foregut will not lead to an alteration of this property. Immunohistochemistry revealed clear differences in the galectins' localization profiles. Galectin-1 expression is strong in mesenchymal cells, especially smooth muscle cells, while epithelial lining harbors galectin-3. A gradual increase in staining intensity with development is especially observed in the case of galectin-3. Notably, this change is accompanied by a shift from primarily nuclear localization to the cytoplasm, an alteration not seen for galectin-1. However, nuclear presence of galectin-1 is encountered. Thus, the delineation of differences in expression of galectin-1 and -3 with respect to cell types and in the developmental course of subcellular localization argues in favor of mediation of nonoverlapping functions by these two homologous, endogenous lectins.

show abstract

Section: Introductionmentioning

confidence: 81%

Galectin-1 and galectin-3 in fetal development of bovine respiratory and digestive tracts

Kaltner

Heck

et al. 2002

Cell and Tissue Research

View full text Add to dashboard Cite

show abstract

“…Do they reflect protein modifications or splice variants? It has been reported that a monoclonal antibody raised against human brain galectin-1 specifically reacted with the two most acidic isoforms of galectin-1 amongst the three identified by 2-DE [27]. Moreover, galectin-1 isolated from bovine heart yielded four isoforms ranging from pI 4.53-4.73 [28], probably indicating that the three spots of galectin-1 may represent different isoforms.…”

Section: Discussionmentioning

confidence: 98%

Mass Spectrometrical Analysis of Galectin Proteins in Primary Rat Cerebellar Astrocytes

et al. 2006

View full text Add to dashboard Cite

Galectins are a family of animal lectins with specificity for beta-galactosides and are involved in a host of cellular activities, ranging from development to cancer. The molecules are expressed by neural and non-neural cells intracellularly as well as extracellularly. Using two-dimensional gel electrophoresis coupled to tandem mass spectrometry, the present work aimed to identify and characterize galectins in primary rat cerebellar astrocytes. The protein-chemical method identified nine spots representing two members of the galectin family, namely galectin-1 and galectin-3. These findings suggest that high abundant expression of galectin in astrocytes is limited to the two abundant galectin family members. As these family members are linked to human astrocytic tumors, their reliable detection in astrocytes by proteomic techniques would enable us to further understand their role in neural development, injury, and regeneration in general and astrocytoma in particular.

show abstract

“…The protein was purified by affinity chromatography on a lactosyl-divinylsulfone-agarose column. Antibodies against human Gal1 were generated as described in [35] and [36]. The immunolocalization of Gal1 was carried out as described for K562 cells [24].…”

Section: Methodsmentioning

confidence: 99%

Effect of 5-azacytidine and galectin-1 on growth and differentiation of the human b lymphoma cell line bl36

et al. 2001

View full text Add to dashboard Cite

Background5-AzaCytidine (AzaC) is a DNA demethylating drugs that has been shown to inhibit cell growth and to induce apoptosis in certain cancer cells. Induced expression of the galectin1 (Gal1) protein, a galactoside-binding protein distributed widely in immune cells, has been described in cultured hepatoma-derived cells treated with AzaC and this event may have a role in the effect of the drug. According to this hypothesis, we investigated the effect of AzaC and Gal1 on human lymphoid B cells phenotype.MethodsThe effect of AzaC and Gal1 on cell growth and phenotype was determined on the Burkitt lymphoma cell line BL36. An immunocytochemical analysis for detection of Gal1 protein expression was performed in AzaC-treated cells. To investigate the direct effects of Gal1, recombinant Gal1 was added to cells.ResultsTreatment of lymphoid B cells with AzaC results in: i) a decrease in cell growth with an arrest of the cell cycle at G0/G1 phase, ii) phenotypic changes consistent with a differentiated phenotype, and iii) the expression of p16, a tumor-suppressor gene whose expression was dependent of its promoter demethylation, and of Gal1. A targeting of Gal 1 to the plasma membrane follows its cytosolic expression. To determine which of the effects of AzaC might be secondary to the induction of Gal1, recombinant Gal1 was added to BL36 cells. Treated cells displayed growth inhibition and phenotypic changes consistent with a commitment toward differentiation.ConclusionsAltered cell growth and expression of the cell surface plasma cell antigen, CD138 are detectable in BL36 cells treated by AzaC as well as by Gal1. It seems that AzaC-induced Gal1 expression and consequent binding of Gal1 on its cell membrane receptor may be, in part, involved in AzaC-induced plasmacytic differentiation.

show abstract

Production and characterization of a monoclonal antibody able to discriminate galectin-1 from galectin-2 and galectin-3

Cited by 5 publications

References 47 publications

Galectin-1 and galectin-3 in fetal development of bovine respiratory and digestive tracts

Galectin-1 and galectin-3 in fetal development of bovine respiratory and digestive tracts

Mass Spectrometrical Analysis of Galectin Proteins in Primary Rat Cerebellar Astrocytes

Effect of 5-azacytidine and galectin-1 on growth and differentiation of the human b lymphoma cell line bl36

Contact Info

Product

Resources

About