Abstract
Galectins are carbohydrate-binding proteins overexpressed in bladder cancer (BCa) cells. Dendritic galactose moieties have a high affinity for galectin-expressing tumor cells. We radiolabeled a dendritic galactose carbohydrate with 18F (18F-labeled galactodendritic unit 4) and examined its potential in imaging urothelial malignancies. Methods: The 18F-labeled first-generation galactodendritic unit 4 was obtained from its tosylate precursor. We conducted in vivo studies in a galectin-expressing UMUC3 orthotopic BCa model to determine the ability of 18F-labeled galactodendritic unit 4 to image BCa. Results: Intravesical administration of 18F-labeled galactodendritic unit 4 allowed specific accumulation of the carbohydrate radiotracer in galectin-1–overexpressing UMUC3 orthotopic tumors when imaged with PET. The 18F-labeled galactodendritic unit 4 was not found to accumulate in nontumor murine bladders. Conclusion: The 18F-labeled galactodendritic unit 4 and similar analogs may be clinically relevant and exploitable for PET imaging of galectin-1–overexpressing bladder tumors.
Highlights
Bladder cancer (BCa) is the tenth most prevalent cancer worldwide [1]
18F-FDG PET imaging in BCa is hampered by 18F-FDG renal excretion
Bladder tumor imaging with 18F-FDG PET is limited because not all malignant cells take up glucose
Summary
Bladder cancer (BCa) is the tenth most prevalent cancer worldwide [1]. The GLOBOCAN 2018 estimated globally nearly 549,000 new BCa cases and about 200,000 deaths [1]. Tumor-targeting vectors bound to a positron-emitting radionuclide (e.g., 18F) are widely used in oncology diagnostic imaging [8] In this context, the glucose analog 18F-FDG accumulates in tumor cells as a result of their high glucose uptake mediated by glucose transporters. Pereira et al previously developed a dendritic galactose unit to be conjugated with porphyrinoids [14] with high affinity for galectin1–overexpressing BCa cells [16,17]. Such a galactose dendritic molecule allows high affinity to tumor cells due to the ability of galectin-1 to establish multivalent interactions with the galactose units of the dendritic unit. We demonstrate the utility of the radiolabeled galactodendritic unit, 18F-labeled galactodendritic unit 4, to image galectin-1–overexpressing UMUC3 cells that were derived from human urinary BCa and orthotopically implanted in the murine bladder
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