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Alpha-mannosidase 2C1 (MAN2C1) is a cytosolic glycosidase enzyme that trims alpha 1,2-, alpha 1,3-, and alpha 1,6-linked mannose residues from free oligosaccharides generated by N-glycoprotein degradation pathways in mammalian cells[2][5][7]. MAN2C1 is unique among glycosidases for its dual functions: it not only participates in the catabolism of free glycans but also acts as a modulator of apoptotic signaling, independently of its catalytic activity[1]. In cancer biology, MAN2C1 is a negative regulator of PTEN—binding to PTEN, inhibiting its phosphatase activity, thereby enhancing AKT activation and promoting cell survival and tumorigenesis, especially in prostate cancer[3]. Overexpression of MAN2C1 has been linked to multiple tumor types and is used as a biomarker in imaging breast tumors[4]. Genetic defects in MAN2C1 are associated with congenital disorders of deglycosylation and intellectual disability[2]. It represents a potential therapeutic target for cancer and other glycosylation-related diseases, though no approved drugs currently target MAN2C1 directly[2][3][4].
Enzyme inhibitors—(potential strategy: inhibition would block mannose trimming and lead to accumulation of free oligosaccharides, affecting glycoprotein degradation and cell signaling) Fluorescent probe substrates—(used for imaging by binding and being catalytically processed by MAN2C1 in tumor tissue)
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