n-azidoacetylmannosamine and Prostatic-Neoplasms

Sialylated glycans are found at elevated levels in many types of cancer and have been implicated in disease progression. However, the specific glycoproteins that contribute to the cancer cell-surface sialylation are not well characterized, specifically in bona fide human disease tissue. Metabolic and bioorthogonal labeling methods have previously enabled the enrichment and identification of sialoglycoproteins from cultured cells and model organisms. Herein, we report the first application of this glycoproteomic platform to human tissues cultured ex vivo. Both normal and cancerous prostate tissues were sliced and cultured in the presence of the azide-functionalized sialic acid biosynthetic precursor Ac

Topics: Azides; Biotinylation; Carbocyanines; Hexosamines; Humans; In Vitro Techniques; Male; Mass Spectrometry; Microscopy, Fluorescence; Principal Component Analysis; Prostatic Neoplasms; Proteomics; Sialoglycoproteins; Voltage-Dependent Anion Channel 1