Expression of the endogenous galactose-binding protein galectin-3 correlates with the malignant potential of tumors in the central nervous system

Bresalier, Robert S.; Yan, Peisha; Byrd, James C.; Lotan, Reuban; Raz, Avraham

doi:10.1002/(sici)1097-0142(19970815)80:4<776::aid-cncr17>3.0.co;2-q

Cited by 154 publications

(92 citation statements)

References 23 publications

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“…H-Ras and galectin-1 are members of two families of proteins known to be associated with human malignancies (Andre et al, 1999;Barondes et al, 1994;Bresalier et al, 1997;Hadari et al, 2000;Kopitz et al, 1998;Ohannesian et al, 1995;Polyak et al, 1997;van den Brule et al, 1995;Wells and Mallucci, 1991;Yamaoka et al, 1991Yamaoka et al, , 2000. Perhaps it is not less important to note that both Ras proteins (Bar-Sagi and Hall, 2000;Downward, 1998;Shields et al, 2000) and galectins (Hughes, 1999;Perillo et al, 1998), share in common a number of regulatory activities including regulation of cell growth, apoptosis, cell adhesion cell migration and metastasis.…”

Section: Discussionmentioning

confidence: 99%

Galectin-1 binds oncogenic H-Ras to mediate Ras membrane anchorage and cell transformation

et al. 2001

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Section: Discussionmentioning

confidence: 99%

Galectin-1 binds oncogenic H-Ras to mediate Ras membrane anchorage and cell transformation

et al. 2001

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“…3C) using galectin-3 antisense RNA (galectin-3 AS). Previous experiments showed that galectin-3 AS specifically down-regulates the expression of galectin-3 (33) but not of galectin-1 (21). We co-transfected the cells with galectin-3 AS and GFP-K-Ras or GFP-H-Ras, then stimulated the co-transfectants with EGF and measured the time-dependent change in Ras-GTP levels.…”

Section: Galectin-3 Augments the Basal And Egf-induced Increase In Gfmentioning

confidence: 99%

Galectin-3 Augments K-Ras Activation and Triggers a Ras Signal That Attenuates ERK but Not Phosphoinositide 3-Kinase Activity

Elad-Sfadia

Haklai

Balan

et al. 2004

Journal of Biological Chemistry

273

269

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Depending on the cellular context, Ras can activate characteristic effectors by mechanisms still poorly understood. Promotion by galectin-1 of Ras activation of Raf-1 but not of phosphoinositide 3-kinase (PI3-K) is one such mechanism. In this report, we describe a mechanism controlling selectivity of K-Ras4B (K-Ras), the most important Ras oncoprotein. We show that galectin-3 acts as a selective binding partner of activated K-Ras. Galectin-3 co-immunoprecipitated significantly better with KRas-GTP than with K-Ras-GDP, H-Ras, or N-Ras and colocalized with green fluorescent protein-K-Ras(G12V), not with green fluorescent protein-H-Ras(G12V), in the cell membrane. Co-transfectants of K-Ras/galectin-3, but not of H-Ras/galectin-3, exhibited enhanced and prolonged epidermal growth factor-stimulated increases in Ras-GTP, Raf-1 activity, and PI3-K activity. Extracellular signal-regulated kinase (ERK) activity, however, was attenuated in K-Ras/galectin-3 and in K-Ras(G12V)/galectin-3 co-transfectants. Galectin-3 antisense RNA inhibited the epidermal growth factor-stimulated increase in K-Ras-GTP but enhanced ERK activation and augmented K-Ras(G12V) transformation activity. Thus, unlike galectin-1, which prolongs Ras activation of ERK and inhibits PI3-K, K-Ras-GTP/galectin-3 interactions promote, in addition to PI3-K and Raf-1 activation, a third inhibitory signal that attenuates active ERK. These experiments established a novel and specific mechanism controlling the duration and selectivity of signals of active K-Ras, which is extremely important in many human tumors.

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“…Galectin-3 is present in abnormally high levels in many cancers and plays an important role in the growth, survival and spread of cancer cells (Bresalier et al, 1997;Johnson et al, 2007). Galectin-3 is highly expressed on tumor cell surfaces and a variety of metastatic cancer cells and is closely related to cell to cell adhesion, aggregation of cancer cells in vitro, tumor growth and metastasis in vivo (Bresalier et al, 1997;Dumic et al, 2006;Krzeslak and Lipinska, 2004). A notable feature of galectin-3 is its implication in neoplastic transformation and cancer progression.…”

Section: Pectin Mcp and Their Molecular Interaction In Cancermentioning

confidence: 99%

Plant Pectin: A Potential Source for Cancer Suppression

Niture¹

2013

American Journal of Pharmacology and Toxicology

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Pectin is a branched polysaccharide present widely in a variety of fruits. It has been of high interest to cancer biologists due to its involvement in metal/carcinogen detoxification and its anti-carcinogenic properties. In particular, Citrus Pectin (CP) and Modified Citrus Pectin (MCP) have been shown to have a significant inhibitory role in cancer cell metastasis, invasion, angiogenesis and survival. The interactions and inactivation of oncogenes by CP and MCP in prostate, breast, liver, lung, melanoma and multiple myeloma cancers suggest that CP and MCP could play an important role in cancer chemotherapy and chemoprevention. In this review, we focus on the biological function of pectin with respect to its properties, sources, structure and its potential role in carcinogen detoxification and cancer suppression.

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Expression of the endogenous galactose-binding protein galectin-3 correlates with the malignant potential of tumors in the central nervous system

Abstract: Galectin-3 expression correlates with the malignant potential of tumors in the central nervous system.

Cited by 154 publications

References 23 publications

Galectin-1 binds oncogenic H-Ras to mediate Ras membrane anchorage and cell transformation

Galectin-1 binds oncogenic H-Ras to mediate Ras membrane anchorage and cell transformation

Galectin-3 Augments K-Ras Activation and Triggers a Ras Signal That Attenuates ERK but Not Phosphoinositide 3-Kinase Activity

Plant Pectin: A Potential Source for Cancer Suppression

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