Galectin-1 prefers to bind with the branched N-glycans of cell-surface glycoproteins and mediates a glycosylation-dependent angiogenesis.91,100–103 It has been reported that increased secretion of Galectin-1 in the ECM facilitates cancer cell proliferation and resistance to cancer therapy in prostate cancer104 and Kaposi’s sarcoma.105 Mechanistic investigation has revealed that Galectin-1 can bind to N-glycans on VEGFR2 to activate VEGF-like signaling in anti-VEGF-A refractory tumors, promoting tumor progression. This evidence concerns the gene VEGFA and neoplasm.