A better understanding of multimolecular interactions involved in tumor dissemination is required to identify new effective therapies for advanced prostate cancer (PCa). Several groups investigated protein-glycan interactions as critical factors for crosstalk between prostate tumors and their microenvironment. This review both discusses whether the “galectin-signature” might serve as a reliable biomarker for the identification of patients with high risk of metastasis and assesses the galectin-glycan lattices as potential novel targets for anticancer therapies. The ultimate goal of this review is to convey how basic findings related to galectins could be in turn translated into clinical settings for patients with advanced PCa. 1. Introduction Prostate cancer (PCa) is the second most common cancer in men and represents a significant cause of mortality worldwide [1]. About 15%–20% of men with PCa will certainly develop metastatic disease and die. Early diagnosis and rapid treatment play a critical role in the final outcome of the disease. At present, surgical and radiation treatments are efficient against clinically localized PCa, whereas androgen ablation is mainly recommended for advanced PCa [2]. However, metastatic cancer is essentially fatal due to disease evolution towards a castration-resistant PCa (CRPC). Novel alternative approaches are therefore essential to prevent tumor dissemination and progression to this incurable stage. Effective cancer therapies for PCa typically capitalize on molecular differences between healthy and neoplastic tissues that can be targeted with drugs [3]. In the past years, delineating gene and protein expression profiles has been critical in dissecting the molecular underpinnings of cellular function; the arising information has been exploited for the design of rational therapeutic strategies. In the postgenomic era, the study of the “glycome” has enabled the association of specific glycan structures with the transition from normal to neoplastic tissue [4]. Glycans abundantly decorate the surface of all mammalian cells and the extracellular matrix with which they interact [5]. In general, mammalian glycans are the product of a repertoire of glycosyltransferases and glycosidases acting sequentially and dictating the glycosylation signature of each cell type [6]. It has been recognized that the structure of cell surface glycans can change under different physiological and pathological conditions. In fact, malignant transformation is associated with abnormal glycosylation resulting in the synthesis of altered glycan
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