Two messenger RNAs and five isoforms for Po66-CBP, a galectin-8 homolog in a human lung carcinoma cell line

Bidon, Nathalie; Brichory, Franck; Hanash, Samir M.; Bourguet, P.; Dazord, L.; Pennec, J

doi:10.1016/s0378-1119(01)00598-4

Cited by 41 publications

(28 citation statements)

References 32 publications

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“…16,26 It has been described that multiple isoforms of this galectin exist as a result of complex alternative mRNA splicing. 4,27 This leads to deletions within the linker peptide that influence the biological function of the protein 28,29 and might affect susceptibility to proteolysis. 30 Because our main objective was to evaluate overall expression of galectins by endothelial cells, we did not focus on all different galectin-8 isoforms.…”

Section: Discussionmentioning

confidence: 99%

The Galectin Profile of the Endothelium

Thijssen

Hulsmans

Griffioen³

2008

The American Journal of Pathology

181

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We previously identified overexpression of galectin-1 in activated tumor endothelium. Currently, the tumor vasculature is a target for therapeutic approaches. Little is known about galectin expression and regulation in the tumor vasculature. Here, we report the expression of galectin-1/-3/-8/-9 in the endothelium as determined by quantitative PCR, Western blot, flow cytometry, and immunohistochemistry. Galectin-2/-4/-12 were detectable at the mRNA level, albeit very low. Galectin-8 and -9 displayed alternative splicing. Immunohistochemistry of normal tissues revealed a broad but low expression of galectin-1 in the vasculature, whereas the expression levels and localization of the other galectins varied. Endothelial cell activation in vitro significantly increased the expression of galectin-1 (5.32 ؎ 1.97; P ‫؍‬ 0.04) and decreased the expression of both galectin-8 (0.59 ؎ 0.12; P < 0.04) and galectin-9 (0.32 ؎ 0.06; P < 0.002). Galectin-3 expression was unaltered. Although a portion of these proteins is expressed intracellularly, the membrane protein level of galectin-1/-8/-9 was significantly increased on cell activation in vitro, 6-fold (P ‫؍‬ Galectins are a family of proteins that share a binding affinity for ␤-galactoside-containing carbohydrates. Several members of this family are emerging as targets for cancer therapy. Apart from a direct role in cell transformation, their main contribution to tumor progression involves modification of the antitumor immune response and enhancement of the metastatic potential of tumor cells.1 There are several reports showing altered galectin expression profiles in tumor cells of different origin, [2][3][4] and compounds that interfere with galectin function in tumor cells are therefore considered for cancer therapy.An attractive site for therapeutic applications is the endothelium, ie, the monolayer of endothelial cells lining blood vessels. Endothelial cells in the tumor vasculature are easily accessible and less prone to become drug resistant, and disrupting the tumor endothelium results in massive death of tumor cells.5 Moreover, tumor endothelial cells express molecules that allow specific targeting independent of the tumor type eg, integrin ␣V␤3, CD44v3, and CD105.6 -9 Recently, we identified galectin-1 as a target molecule in the tumor endothelium. Activated tumor endothelial cells increase the expression of galectin-1, and ablation of its expression in vitro and in vivo results in impaired endothelial cell function and hampered tumor angiogenesis.10 Whether other galectins are also directly involved in endothelial cell biology and tumor angiogenesis is less well studied (for review, see Ref. 11). In the current study, we analyzed the expression of all known human galectins in the endothelium to get more insight in their possible function in endothelial cell biology. We show that multiple galectins and galectin isoforms are expressed by endothelial cells. Furthermore, the expression and distribution of endothelial galectins is altered on cell activation. These obser...

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Section: Discussionmentioning

confidence: 99%

The Galectin Profile of the Endothelium

Thijssen

Hulsmans

Griffioen³

2008

The American Journal of Pathology

181

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“…1; for details of amino acid sequences, see Fig. S1) (17,18). Because the functional impact of this change has not yet been defined, the expression pattern appears to be stochastic in nature (17).…”

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confidence: 99%

Unraveling functional significance of natural variations of a human galectin by glycodendrimersomes with programmable glycan surface

Zhang

Moussodia

Vértesy

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

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Surface-presented glycans (complex carbohydrates) are docking sites for adhesion/growth-regulatory galectins within cell-cell/ matrix interactions. Alteration of the linker length in human galectin-8 and single-site mutation (F19Y) are used herein to illustrate the potential of glycodendrimersomes with programmable glycan displays as a model system to reveal the functional impact of natural sequence variations in trans recognition. Extension of the linker length slightly reduces lectin capacity as agglutinin and slows down aggregate formation at low ligand surface density. The mutant protein is considerably less active as agglutinin and less sensitive to low-level ligand presentation. The present results suggest that mimicking glycan complexity and microdomain occurrence on the glycodendrimersome surface can provide key insights into mechanisms to accomplish natural selectivity and specificity of lectins in structural and topological terms.adhesion | agglutination | glycobiology | membrane mimic | self-assembly

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“…The complexity of the galectin family and in particular of galectin-8 is only slowly understood. To this date 6 isoforms of galectin-8 have been revealed what makes it a subfamily within the galectin family [24,28,29] . As in other immunohistochemical studies, we did not discriminate between the galectin-8 isoforms as no commercially available antibodies could be found.…”

Section: Discussionmentioning

confidence: 99%

Decreased Galectin-8 Is a Strong Marker for Recurrence in Urothelial Carcinoma of the Bladder

et al. 2011

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Objective: To investigate galectin-8 expression patterns in normal urothelium and bladder cancer specimens and to elucidate its prognostic value. Materials and Methods: 162 samples of non-muscle-invasive transitional cell carcinoma, 25 samples of muscle-invasive transitional cell carcinoma and 10 samples of normal urothelium were investigated by immunohistochemistry using tissue microarrays. Complete patient and tumor characteristics were compared with galectin-8 staining patterns. The likelihood of tumor recurrence and progression was analyzed based on a 3-year follow-up. Results: Loss of galectin-8 was associated with the likelihood of tumor recurrence in univariate (p < 0.05) and multivariate analyses (p < 0.01). No significance was observed for tumor progression. Patients whose specimens showed weak galectin-8 expression had a shorter recurrence-free interval (42 vs. 12 months; p < 0.01, log-rank test). All of the 10 normal urothelium samples showed high galectin-8 expression. Decreased staining was found to be associated with higher tumor stages and grades (p < 0.0001, one-way ANOVA). A significant difference was found comparing normal urothelium with any tumor stage (p < 0.01), pTa vs. pT1 tumors (p < 0.05) and non-muscle-invasive vs. muscle-invasive tumors (p < 0.0001). Conclusions: Loss of galectin-8 might be an early step in the development of malignant lesions of the bladder and is a significant independent predictor of recurrence.

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Two messenger RNAs and five isoforms for Po66-CBP, a galectin-8 homolog in a human lung carcinoma cell line

Cited by 41 publications

References 32 publications

The Galectin Profile of the Endothelium

The Galectin Profile of the Endothelium

Unraveling functional significance of natural variations of a human galectin by glycodendrimersomes with programmable glycan surface

Decreased Galectin-8 Is a Strong Marker for Recurrence in Urothelial Carcinoma of the Bladder

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