Multiple soluble vertebrate galactoside-binding lectins

Barondes, Samuel H.; Gitt, Michael A.; Leffler, Hakon; Cooper, Douglas N.W.

doi:10.1016/0300-9084(88)90298-2

Cited by 141 publications

(190 citation statements)

References 21 publications

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“…Furthermore, neither D121 nor N156 of ERGIC-53 are conserved in galectins (Arar et al, 1995). In galectins the carbohydrate interaction is mediated by a set of different amino acid residues that are conserved in the galectin family (Barondes et al, 1994). Having established a lectin activity and the functional homology of ERGIC-53 to leguminous lectins, we provide the first direct experimental evidence for the hypothesis of (Drickamer and Taylor, 1993).…”

Section: Elution Of Ergic-53 Is Selective For D-mannosementioning

confidence: 86%

ERGIC-53 is a functional mannose-selective and calcium-dependent human homologue of leguminous lectins.

Itin

Roche

Monsigny

et al. 1996

MBoC

166

148

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Based on sequence homologies with leguminous lectins, the intermediate compartment marker proposed to be a member of a putative new class of animal lectins associated with the secretory pathway. Independently, a promyelocytic protein, MR60, was purified by mannose-column chromatography, and a cDNA was isolated that matched MR60 peptide sequences. This cDNA was identical to that of and homologies with the animal lectin family of the galectins were noticed. Not all peptide sequences of MR60, however, were found in ERGIC-53, raising the possibility that another protein associated with ERGIC-53 may possess the lectin activity. Here, we provide the first direct evidence for a lectin function of ERGIC-53. Overexpressed ERGIC-53 binds to a mannose column in a calcium-dependent manner and also co-stains with mannosylated neoglycoprotein in a morphological binding assay. By using a sequential elution protocol we show that ERGIC-53 has selectivity for mannose and low affinity for glucose and GlcNAc, but no affinity for galactose. To experimentally address the putative homology of ERGIC-53 to leguminous lectins, a highly conserved protein family with an invariant asparagine essential for carbohydrate binding, we substituted the corresponding asparagine in ERGIC-53. This mutation, as well as a mutation affecting a second site in the putative carbohydrate recognition domain, abolished mannosecolumn binding and co-staining with mannosylated neoglycoprotein. These findings establish ERGIC-53 as a lectin and provide functional evidence for its relationship to leguminous lectins. Based on its monosaccharide specificity, domain organization, and recycling properties, we propose ERGIC-53 to function as a sorting receptor for glycoproteins in the early secretory pathway.

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Section: Elution Of Ergic-53 Is Selective For D-mannosementioning

confidence: 86%

ERGIC-53 is a functional mannose-selective and calcium-dependent human homologue of leguminous lectins.

Itin

Roche

Monsigny

et al. 1996

MBoC

166

148

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“…Several plant lectins are well known to activate lymphocytes, raising the question of the specificity of the galectin 3 drate binding specificities with galectin-3. GSL-IB4 requires (Table 1).…”

Section: -~mentioning

confidence: 99%

“…PolycloGalectin-3, also called Mac-2 surface differentiation antigen nal rabbit antisera against hamster galectin-3 N-terminal and C-termi- [1], is a member of a family of mammalian carbohydratenal domains were obtained as described [18], and shown by Western blotting to cross-react with human galectin-3. Mouse monoclonal binding proteins and is expressed widely in epithelial cells antibodies against human CD98 (clone 4F2) and CD1 lb/CDI8 (clone and some leukocytes [2,3]. Galectin-3, like other galectin faro-44) subunits were from PharMingen, Cambridge, UK.…”

Section: Introductionmentioning

confidence: 99%

Galectin‐3 stimulates uptake of extracellular Ca²⁺ in human Jurkat T‐cells

Dong¹,

Hughes²

1996

FEBS Letters

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RL388 monoclonal antibodies in human [13,14] and rodent Abstract Galectin-3, a mammalian galaetoside-binding protein, is not expressed in the Jurkat T-lymphoblastoid cell line.[15,16] cells, respectively. CD98 antigen is expressed on most However, Jurkat cells express surface glycoprotein receptors cell lines in culture as well as on monocytic cells. Interestingly, for galectin-3, one of which is shown to be the glycosylated heavy CD98 is also expressed on activated human lymphocytes chain of CD98 (4F2 antigen), a T-cell activation marker, although not on resting T and B lymphocytes. Although preAddition of galectin-3 to Jurkat cells triggers a sustained influx liminary evidence [17] suggests that lymphocytes do not exof extracellular Ca 2+ in a concentration dependent manner. The press galectin-3, we were prompted by these findings to examinduced increase in eytosollc [Ca2+]i is blocked by sugar hapten ine whether lymphocytes bind exogenous lectin. In this report, inhibitors of galectin-3. The galectin-3-induced effect is insensiwe show that exogenous galectin-3 binds to surface glycoprotire to voltage-gated Ca 2+ channel antagonists such as teins, including CD98, of the human lymphoblastoid Jurkat prenylamlne, nifedipine and diltiazem and to pertussis toxin but T-cell line. Furthermore, surface ligation of these cells triggers is inhibited by cholera toxin. The results suggest that galectin-3 released by accessory cells such as macrophages may bind in vivo an increase in intracellular Ca 2+, suggesting that activated to T-cell activation antigens and also participate in Ca 2+ lymphocytes may be responsive to galectin 3 released from signalling, other cell types.

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“…Galectin-3 is a member of a family of carbohydrate-binding proteins consisting so far of 14 reported members, characterized by a conserved amino acid sequence defined by structural similarities in their carbohydrate-binding domain and affinity for β-galactoside containing glycoconjugates (Barondes et al, 1994). Galectin-3 is the unique member of this family having a chimeric structure consisting of a amino terminal domain of 12 amino acids containing a serine phosphorylation site that regulates its cellular targeting, a α-collagen like sequence of about 110 amino acids that serves as a substrate for matrix metalloproteases, and a carboxy terminal domain of about 130 amino acids that contains a single carbohydrate recognition domain (Barondes et al, 1994;Ochieng et al, 1994;Gong et al, 1999).…”

Section: Introductionmentioning

confidence: 99%

Galectin-3 in apoptosis, a novel therapeutic target

Nangia‐Makker

Nakahara

Hogan

et al. 2007

J Bioenerg Biomembr

119

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During the past decade, extensive progress has been made toward understanding the molecular basis for the regulation of apoptosis. In mammalian cells undergoing apoptosis, two distinct mechanisms or pathways are operated and are triggered by cell death stimuli from intra-or extracellular environments, namely the intrinsic or extrinsic pathways, resulting in mitochondrial membrane depolarization. Several lines of evidence from our laboratories and others have indicated that galectin-3 plays an important role in these pathways by binding to various ligands. Here the authors provide a brief discussion on the role of endogenous or extra-cellular galectin-3 in the regulation of apoptosis and how it could be used as a therapeutic target using natural plant products as its functional inhibitors.

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Multiple soluble vertebrate galactoside-binding lectins

Cited by 141 publications

References 21 publications

ERGIC-53 is a functional mannose-selective and calcium-dependent human homologue of leguminous lectins.

ERGIC-53 is a functional mannose-selective and calcium-dependent human homologue of leguminous lectins.

Galectin‐3 stimulates uptake of extracellular Ca²⁺ in human Jurkat T‐cells

Galectin-3 in apoptosis, a novel therapeutic target

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Multiple soluble vertebrate galactoside-binding lectins

Cited by 141 publications

References 21 publications

ERGIC-53 is a functional mannose-selective and calcium-dependent human homologue of leguminous lectins.

ERGIC-53 is a functional mannose-selective and calcium-dependent human homologue of leguminous lectins.

Galectin‐3 stimulates uptake of extracellular Ca2+ in human Jurkat T‐cells

Galectin-3 in apoptosis, a novel therapeutic target

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Galectin‐3 stimulates uptake of extracellular Ca²⁺ in human Jurkat T‐cells