Table 2.

Involvement of glycosylation in prostate cancer biology. The step of glycosylation is stated on the top of each rectangle and examples are schematically depicted. The prostate cancer processes affected are listed on the bottom of rectangles.

Sialylation O-linked glycans: in vitro proliferation, migration, apoptosis; tumor size in mouse model [30]; cell adhesion [99]; N-linked glycans: in vitro proliferation, migration, invasion [101].	Fucosylation Self-assembly of spheroids [102]; EGFR signaling; cell survival in androgen-depleted conditions [31]; vesicles secreted by PCa cells [32]; PSA expression [34]; metastasis to bone [103].	Biosynthesis of1,6 GlcNAc-Branched N-glycans In vitro invasion; tumor growth in xenograft models [104].	Mannose Trimming of N-glycans Essential for cell viability [105].
Regulation of N-glycosylation Substrate Specificity In vitro proliferation, migration and invasion; xenograft growth in a PTEN negative background; ER structure and stress response; Akt signaling [106].	O-Linked N-Acetylgalactosamine Addition Essential for cell viability [105].	O-Linked N-Acetylglucosamine Addition Essential process in androgen-independency [33]; metabolism [107].	Generation of the Common Core 1 O-glycan Structure Castration resistance and metastasis [108,109].
Core-2-branched O-linked glycosylation Tumor growth in mouse model [110,111]; cell adhesion [110]; resistance to NK cell immunity [112]; LNCaP susceptibility to apoptosis induced by Galectin-1 [113].	Core-3 O-linked glycan formation Tumor formation andmetastasis of PC-3 and LNCaP cells through downregulation of α2β1 integrin complex [114].	I-branching Migration and invasion; integrin signaling via indirect mechanisms; in DU145 cells appears to largely occur on glycolipids and partially on O-glycans [115].	Legend:    N-acetylglucosamine    N-acetylgalactosamine             Galactose              Mannose             Sialic acid              Fucose