title: Alteration of the cytoplasmic/nuclear expression pattern of galectin-3 correlates with prostate carcinoma progression.
abstract: Galectin-3, a member of the beta-galactoside-binding lectin family, is involved in a variety of biological events including interactions with galactose-containing glycoconjugates, cell proliferation, differentiation and apoptosis. Galectin-3 appears to intervene during tumor progression and altered expression patterns have been reported in a variety of malignancies. In our study, we have examined the expression of galectin-3 in a population of 145 prostate carcinoma samples using immunohistochemistry. We found that most of the non-tumoral prostatic glands exhibited moderate immunostaining for galectin-3 localized in both nucleus and cytoplasm. In prostatic cancer cells, galectin-3 was usually not expressed or decreased compared with the normal glands. Interestingly, when galectin-3 was detected in the cancer cells, it was consistently excluded from the nucleus and only present in the cytoplasmic compartment. The latter observation was also made for prostatic intraepithelial neoplasia (PIN) cells. Furthermore, we found that the levels of galectin-3 expression in the cancer cells were significantly associated with prostate-specific antigen (PSA) relapse in univariate analysis (p = 0.044). Cytoplasmic expression of galectin-3 in the carcinoma cells was an independent predictor of disease progression in multivariate analysis, after the pathological stage and the Gleason score. Our data demonstrate that galectin-3 is generally down-regulated in human prostate carcinoma cells, and consistently excluded from the nucleus. Interestingly, specific cytoplasmic expression of galectin-3 in a subset of lesions is associated with disease progression. These results suggest that galectin-3 might play anti-tumor activities when present in the nucleus, whereas it could favor tumor progression when expressed in the cytoplasm. Further studies should determine the exact role and mechanisms by which galectin-3 differentially affects cell behavior in the different locations where it is expressed.
authors.affiliation: Metastasis Research Laboratory University Hospital, University of Liège, Liège, Belgium. f.vandenbrule@chu.ulg.ac.be
authors.forename: F A
authors.initials: FA
authors.lastname: van den Brûle
authors.forename: D
authors.initials: D
authors.lastname: Waltregny
authors.forename: F T
authors.initials: FT
authors.lastname: Liu
authors.forename: V
authors.initials: V
authors.lastname: Castronovo
mesh_terms: D000368:Aged; D000943:Antigens, Differentiation / Q000096:biosynthesis* / Q000235:genetics; D014408:Biomarkers, Tumor / Q000096:biosynthesis* / Q000235:genetics; D002277:Carcinoma / Q000235:genetics / Q000378:metabolism* / Q000473:pathology; D002467:Cell Nucleus / Q000378:metabolism; D003593:Cytoplasm / Q000378:metabolism; D018450:Disease Progression; D015536:Down-Regulation; D004848:Epithelium / Q000378:metabolism; D037502:Galectin 3; D015972:Gene Expression Regulation, Neoplastic; D006801:Humans; D007150:Immunohistochemistry; D008297:Male; D008562:Membrane Glycoproteins / Q000096:biosynthesis* / Q000235:genetics; D008875:Middle Aged; D009367:Neoplasm Staging; D011467:Prostate / Q000378:metabolism; D019048:Prostatic Intraepithelial Neoplasia / Q000378:metabolism / Q000473:pathology; D011471:Prostatic Neoplasms / Q000235:genetics / Q000378:metabolism* / Q000473:pathology; D013194:Staining and Labeling
chemical_list: D000943:Antigens, Differentiation; D014408:Biomarkers, Tumor; D037502:Galectin 3; D008562:Membrane Glycoproteins