Galectin-3 in apoptosis, a novel therapeutic target

Nangia‐Makker, Pratima; Nakahara, Susumu; Hogan, Victor; Raz, Avraham

doi:10.1007/s10863-006-9063-9

Cited by 119 publications

(103 citation statements)

References 62 publications

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“…Galectin-3 (Gal-3), a member of the carbohydrate-binding protein family, contributes to neoplastic transformation, tumor survival, angiogenesis, and metastasis [3][4][5] . Gal-3 expression is associated with tumor invasion and metastasis in various human cancers, such as gastric, colon, prostate, pancreatic, and breast cancers [6][7][8][9][10] .…”

Section: Introductionmentioning

confidence: 99%

Galectin-3 gene silencing inhibits migration and invasion of human tongue cancer cells in vitro via downregulating β-catenin

et al. 2012

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Aim: Galectin-3 (Gal-3) is a member of the carbohydrate-binding protein family that contributes to neoplastic transformation, tumor survival, angiogenesis, and metastasis. The aim of this study is to investigate the role of Gal-3 in human tongue cancer progression. Methods: Human tongue cancer cell lines (SCC-4 and CAL27) were transfected with a small-interfering RNA against Gal-3 (Gal-3-siRNA). The migration and invasion of the cells were examined using a scratch assay and BD BioCoat Matrigel Invasion Chamber, respectively. The mRNA and protein levels of β-catenin, Akt/pAkt, GSK-3β/pGSK-3β, MMP-9 in the cells were measured using RT-PCR and Western blotting, respectively. Results: Transient silencing of Gal-3 gene for 48 h significantly suppressed the migration and invasion of both SCC-4 and CAL27 cells. Silencing of Gal-3 gene significantly decreased the protein level of β-catenin, leaving the mRNA level of β-catenin unaffected. Furthermore, silencing Gal-3 gene significantly decreased the levels of phosphorylated Akt and GSK-3β, and suppressed the mRNA and protein levels of MMP-9 in the cells. Conclusion: Our data suggest that Gal-3 mediates the migration and invasion of tongue cancer cells in vitro via regulating the Wnt/ β-catenin signaling pathway and Akt phosphorylation.

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Section: Introductionmentioning

confidence: 99%

Galectin-3 gene silencing inhibits migration and invasion of human tongue cancer cells in vitro via downregulating β-catenin

et al. 2012

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“…Galectin-3 binds to various antiapoptotic proteins such as Bcl-2, activated K-Ras, Alix/A1P1, and synexin to inhibit the intrinsic apoptotic pathways. The intracellular galectin-3 can also regulate extrinsic apoptotic pathways induced through death receptors such as Fas (CD95/apo-1), tumor necrosis factor receptor-1 (TNFR-1/p55/CD120), and TRAIL (TNF-related apoptosis inducing ligand/Apo2-L; Nangia-Makker et al 2007). This study revealed that luteal cells themselves were immunoreactive for galectin-3 in old CL formed at previous estrus cycles.…”

Section: Discussionmentioning

confidence: 99%

Differential Cellular Localization of Galectin-1 and Galectin-3 in the Regressing Corpus Luteum of Mice and Their Possible Contribution to Luteal Cell Elimination

Nio‐Kobayashi

Iwanaga

2010

J Histochem Cytochem.

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S U M M A R Y Galectin-1 and galectin-3, b-galactoside-binding lectins, are predominantly expressed in the regressing corpus luteum (CL) of mouse ovary. This study revealed the expression patterns and cellular localizations of galectins during CL formation and regression by ISH and IHC. Galectin-1 mRNA expression temporarily increased in active CL, preceding the expression of progesterone degradation enzyme 20a-hydroxysteroid dehydrogenase (20a-HSD), which represents functional luteolysis. The expressions of both galectin-1 and galectin-3 remarkably increased in the structurally regressing CL, which vigorously expressed 20a-HSD and contained abundant apoptotic luteal cells. Ultrastructurally, galectin-1-and galectin-3-immunoreactive cells were identified as fibroblasts and infiltrating macrophages, respectively. In addition, some populations of luteal cells themselves expressed galectin-3 in regressing CL and formed unique demarcation membranes in the cytoplasm, showing a nontypical apoptotic feature. Ovary of adult mice with repeated estrus cycles contained CL of three different generations. Among them, the old CL formed during previous estrus cycles consisted of galectin-3-positive luteal cells. The galectin-3-positive old CL was resistant to apoptosis and seemed to be eliminated by a mechanism different from apoptosis. The stage-and cell-specific expression of galectin in CL suggests its differential contribution to luteolysis, and this expression may be mediated by major regulatory molecules of CL function, prolactin and/or prostaglandin F2a. (J Histochem Cytochem 58:741-749, 2010)

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“…Galectin-3 expressed only at the villus tips may affect the shedding off and apoptosis of fully matured epithelial cells. In several in vitro studies, galectin-3 suppressed apoptosis by binding to various ligands such as Bcl-2 and Ras proteins (Nangia-Makker et al 2007). This study showed the diffuse localization of galectin-4/6 in the cytoplasm of immature enterocytes and a shift to the baso-lateral membrane in matured enterocytes, suggesting its involvement in membrane trafficking or stabilization.…”

Section: Discussionmentioning

confidence: 99%

Immunohistochemical Localization of Six Galectin Subtypes in the Mouse Digestive Tract

Nio‐Kobayashi

Takahashi-Iwanaga

Iwanaga

2008

J Histochem Cytochem.

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S U M M A R Y Galectin, an animal lectin that recognizes b-galactoside of glycoconjugates, is abundant in the gut. This IHC study showed the subtype-specific localization of galectin in the mouse digestive tract. Mucosal epithelium showed region/cell-specific localization of each galectin subtype. Gastric mucous cells exhibited intense immunoreactions for galectin-2 and galectin-4/6 with a limited localization of galectin-3 at the surface of the gastric mucosa. Electron microscopically, galectin-3 immunoreactivity coated indigenous bacteria on the gastric surface mucous cells. Epithelial cells in the small intestine showed characteristic localizations of galectin-2 and galectin-4/6 in the cytoplasm of goblet cells and the baso-lateral membrane of enterocytes in association with maturation, respectively. Galectin-3 expressed only at the villus tips was concentrated at the myosin-rich terminal web of fully matured enterocytes. Epithelial cells of the large intestine contained intense immunoreactions for galectin-3 and galectin-4/6 but not for galectin-2. The stratified squamous epithelium of the forestomach was immunoreactive for galectin-3 and galectin-7, but the basal layer lacked galectin-3 immunoreactivity. Outside the epithelium, only galectin-1 was localized in the connective tissue, smooth muscles, and neuronal cell bodies. The subtype-specific localization of galectin suggests its important roles in host-pathogen interaction and epithelial homeostasis such as membrane polarization and trafficking in the gut. GALECTIN is a b-galactoside-binding lectin, which to date consists of 15 members (galectin-1 to galectin-15) in mammals and is broadly distributed in a variety of cells and tissues (Leffler et al. 2004). Galectin is likely secreted extracellularly through a non-classical unknown pathway because it lacks a signal sequence essential for insertion into the endoplasmic reticulum (Hughes 1999). Extracellular galectin may mediate cell-cell or cell-matrix adhesion by recognizing cell surface glycoproteins and glycolipids or glycosylated extracellular matrix (Hughes 2001). It also seems capable of regulating cell signaling and membrane trafficking by cross-linking the cell surface receptors (Rabinovich et al. 2007a). A special type of galectin (galectin-3) is involved in host-pathogen interaction through the recognition of a surface carbohydrate of microorganisms (Sato and Nieminen 2004). In contrast, the predominant localization of galectin in the cytoplasm has been frequently observed, suggesting an additional possibility that galectin operates intracellularly to cell proliferation, differentiation, and apoptosis (Hsu and Liu 2004).In the mouse, nine subtypes of galectin (galectin-1, -2, -3, -4, -6, -7, -8, -9, and -12) have been reported to be expressed in a tissue/cell-specific manner. The digestive tract is one of the organs rich in galectin; we previously showed at the mRNA level that at least six subtypes of galectin (galectin-2, -3, -4, -6, -7, and -9) were intensely and continuously expressed from t...

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Galectin-3 in apoptosis, a novel therapeutic target

Cited by 119 publications

References 62 publications

Galectin-3 gene silencing inhibits migration and invasion of human tongue cancer cells in vitro via downregulating β-catenin

Galectin-3 gene silencing inhibits migration and invasion of human tongue cancer cells in vitro via downregulating β-catenin

Differential Cellular Localization of Galectin-1 and Galectin-3 in the Regressing Corpus Luteum of Mice and Their Possible Contribution to Luteal Cell Elimination

Immunohistochemical Localization of Six Galectin Subtypes in the Mouse Digestive Tract

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