Development of complex organisms requires specific temporospatial differentiation and expression of the correct phenotype through activation of a variety of genes. Galectins are mammalian lectins able to interact with various extracellular matrix glycoconjugates and have been implicated in several b
Galectin-1 and galectin-3 expression in human bladder transitional-cell carcinomas
β Scribed by Luca Cindolo; Giovanna Benvenuto; Paola Salvatore; Raffaela Pero; Gaetano Salvatore; Vincenzo Mirone; Domenico Prezioso; Vincenzo Altieri; Carmelo Bruno Bruni; Lorenzo Chiariotti
- Publisher
- John Wiley and Sons
- Year
- 1999
- Tongue
- French
- Weight
- 133 KB
- Volume
- 84
- Category
- Article
- ISSN
- 0020-7136
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β¦ Synopsis
Galectin-1 and galectin-3 are galactoside-binding proteins involved in different steps of tumor progression and potential targets for therapy. We have investigated the expression of these galectins in 38 human bladder transitional-cell carcinomas of different histological grade and clinical stage and in 5 normal urothelium samples. Galectin-1 mRNA levels were highly increased in most high-grade tumors compared with normal bladder or low-grade tumors. Western blot and immuno-histochemical analysis of normal and neoplastic tissues revealed a higher content of galectin-1 in tumors. Galectin-3 mRNA levels were also increased in most tumors compared with normal urothelium, but levels were comparable among tumors of different histological grade.
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Galectins are a family of β€-galactoside-binding animal lectins. In particular, a widely studied member galectin-3, previously designated as βBP, CBP35, Mac-2, L-29 and L-34, has been associated with assorted processes such as cell growth, tumor transformation and metastasis. Galectin-3 is expressed
Galectin-3 is a member of the galectin family of β€-galactoside-specific animal lectins. Here we show that galectin-3 is constitutively expressed in 15 out of 16 glioma cell lines tested, but not by normal or reactive astrocytes, oligodendrocytes, glial O-2A progenitor cells and the oligodendrocyte p
Lysosomal-membrane-associated glycoproteins (Lamps) 1 and 2 are rarely found on the plasma membranes of normal cells. There is evidence suggesting an increase in their cellsurface expression in tumor cells, with some data indicating that the adhesion of some cancer cells to the extracellular matrix
Galectin-1 and galectin-3 are β€-galactoside-binding proteins thought to be important for cellular interactions, growth regulation and differentiation. Alterations in cellular content of galectins have been associated with differentiation, transformation and malignant progression. We examined the mod