Evidence That Lactose Binding to CBP35 Disrupts Its Interaction with CBP70 in Isolated HL60 Cell Nuclei

Sève, Annie-Pierre; Hadj-Sahraoui, Yasmina; Felin, Murielle; Doyennette-Moyne, Marie-Agnès; Auger, Michèle; Hubert, Jean

doi:10.1006/excr.1994.1190

Cited by 14 publications

(11 citation statements)

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“…However, since ␤-galactosides are not detectable in the cytoplasm, the intracellular galectin ligands must be of another nature, probably proteins. Indeed, interaction between galectin-3 and a nuclear glucose-binding protein of 70 kDa (CBP70) has been demonstrated (35), and most recently galectin-3 was shown to associate with Bcl-2, a well known intracellular suppressor of apoptosis (36). Both of these associations occur via protein-protein interactions but are inhibited by lactose, indicating direct or indirect involvement of the galectin carbohydrate binding site.…”

Section: Discussionmentioning

confidence: 99%

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Strikingly Different Localization of Galectin-3 and Galectin-4 in Human Colon Adenocarcinoma T84 Cells

Huflejt¹,

Jordan

Gitt

et al. 1997

Journal of Biological Chemistry

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Two ␤-galactoside-binding proteins were found to be prominently expressed in the human colon adenocarcinoma T84 cell line. Cloning and sequencing of one, a 36-kDa protein, identified it as the human homolog of galectin-4, a protein containing two carbohydrate binding domains and previously found only in the epithelial cells of the rat and porcine alimentary tract. The other, a 29-kDa protein, is galectin-3, containing a single carbohydrate binding domain, previously found in a number of different cell types including human intestinal epithelium. Despite the marked similarities in the carbohydrate binding domains of these two galectins, their cellular distribution patterns are strikingly different and vary with cellular conditions. In confluent T84 cells, galectin-4 is mostly cytosolic and concentrated at the basal membrane, whereas galectin-3 tends to be concentrated in large granular inclusions mostly at the apical membrane. In subconfluent T84 cells, each galectin is distributed to specific domains of lamellipodia, with galectin-4 concentrated in the leading edge and galectin-3 more proximally. Such different localization of galectins-4 and -3 within T84 cells implies different targeting mechanisms, ligands, and functions. The localization of galectin-4 suggests a role in cell adhesion which is also supported by the ability of immobilized recombinant galectin-4 to stimulate adhesion of T84 cells.

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Section: Discussionmentioning

confidence: 99%

“…35 S-protein labeling mix EXPRE 35 S 35 S (Ͼ1,000 Ci/ mmol) was purchased from DuPont NEN. Sepharose CL-2B was obtained from Pharmacia Biotech Inc., and protein G-Sepharose was obtained from Zymed (South San Francisco, CA).…”

Section: Materials-anmentioning

confidence: 99%

Strikingly Different Localization of Galectin-3 and Galectin-4 in Human Colon Adenocarcinoma T84 Cells

Huflejt¹,

Jordan

Gitt

et al. 1997

Journal of Biological Chemistry

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“…Galectin-12 may directly modulate these signaling events through physical interactions with relevant components of the signaling pathway. In fact, galectins have been shown to interact with other proteins independent of binding to carbohydrates, although these interactions are often lactoseinhibitable and involve their CRDs (22,67,68). The clear divergence of the C-terminal domain of galectin-12 from traditional galectin CRDs (31) makes it more likely that this domain is not utilized for binding to lactose, but to ligands of another nature instead.…”

Section: Galectin-12 In Adipogenesis3bmentioning

confidence: 99%

Galectin-12 Is Required for Adipogenic Signaling and Adipocyte Differentiation

Yang

Hsu

et al. 2004

Journal of Biological Chemistry

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“…While some binding interactions rely on the carbohydrate-binding domain of Gal-3, many Gal-3 binding partners depend on N-terminal protein-protein interaction. In the intracellular compartment, there are also many ligands, which bind mainly with Gal-3 through protein-protein interaction (7). Gal-3 is involved in multiple biological activities dependent on its wide distribution and abundant ligands, such as cell growth, cell differention, cell apoptosis, pre-mRNA splicing, cell adhesion, cell migration, angiogenesis, chemo attraction, immune activities and so on (8, 9).…”

Section: Introductionmentioning

confidence: 99%

Galectin-3 induces cell migration via a calcium-sensitive MAPK/ERK1/2 pathway

et al. 2014

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The presence and level of circulating galectin-3 (Gal-3), a member of the galectin family, is associated with diverse diseases ranging from heart failure, immune disorders to cancer metastasis and serves as a biomarker of diagnosis and treatment response. However, the mechanisms by which exogenous Gal-3 affects pathobiology events remain elusive. In the current study, we found that exogenous Gal-3 slightly delays, while prolonging tyrosine phosphorylation of extracellular signal-regulated kinase 1/2 (ERK1/2) in HeLa cells through a calcium-sensitive and PKC-dependent signaling pathway. The activation was dependent on the sugar-binding properties of Gal-3, since the antagonist lactose could inhibit it. The sugar-binding motif of Gal-3 was required for the activation of ERK1/2. The activation of ERK1/2 was necessary for the initiation and induction of cell migration associated with the phosphorylation of paxillin. All the results presented in this study suggest a novel calcium-sensitive and PKC-dependent pathway through which circulating Gal-3 promotes cell migration and activating the ERK1/2. Taken together, the data depicted here propose a biological function and a target for the diseases' associated circulating Gal-3.

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Evidence That Lactose Binding to CBP35 Disrupts Its Interaction with CBP70 in Isolated HL60 Cell Nuclei

Cited by 14 publications

References 0 publications

Strikingly Different Localization of Galectin-3 and Galectin-4 in Human Colon Adenocarcinoma T84 Cells

Strikingly Different Localization of Galectin-3 and Galectin-4 in Human Colon Adenocarcinoma T84 Cells

Galectin-12 Is Required for Adipogenic Signaling and Adipocyte Differentiation

Galectin-3 induces cell migration via a calcium-sensitive MAPK/ERK1/2 pathway

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