{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nUDP‐glucose ceramide glucosyltransferase (UGCG) is the sole enzyme responsible for the conversion of ceramide to glucosylceramide—the first and rate‐limiting step in de novo glycosphingolipid biosynthesis. In doing so, UGCG controls the levels of glucosylceramide, which subsequently serves as the precursor for a variety of complex glycosphingolipids that are essential for proper membrane structure, cell signaling, and barrier function. Altered UGCG activity or expression has been implicated in lysosomal storage disorders such as Gaucher disease and Fabry disease, and its modulation can also affect epidermal ceramide composition and the formation of an effective skin permeability barrier."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "4"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nA wealth of studies in various cancer models indicates that aberrantly high UGCG expression contributes to multidrug resistance by shunting ceramide—a lipid mediator with potent pro‐apoptotic activity—into the non‐cytotoxic glucosylceramide pool. This enzyme‐mediated detoxification of ceramide has been linked to chemoresistance in multiple malignancies including breast, ovarian, thyroid, leukemia, and hepatocellular cancers. UGCG overexpression is frequently associated with enhanced expression of drug efflux transporters (e.g. MDR1/P‐glycoprotein), defective apoptotic signaling (such as impaired p53 function) and a remodeled glycosphingolipid profile that promotes tumor aggressiveness and metastasis. In experimental models, both genetic silencing and pharmacologic inhibition of UGCG have been shown to resensitize tumor cells to cytotoxic agents, thereby underscoring its potential as a therapeutic target."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "5", "end_ref": "28"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its prominent role in cancer biology, UGCG also modulates broader aspects of cellular metabolism and signaling. Changes in UGCG expression can redirect metabolic fluxes—such as increased glutamine oxidation and enhanced mitochondrial turnover—as well as influence oncogenic signaling cascades (including c‐Src/β‐catenin pathways) that regulate proliferation, differentiation, and survival. In addition, UGCG activity has been linked to the regulation of innate immune responses by affecting type I interferon production in plasmacytoid dendritic cells, while its expression is dynamically controlled by factors such as the aryl hydrocarbon receptor and ADP ribosylation factor 6. These diverse roles underscore the enzyme’s importance not only in tumor cell survival but also in processes ranging from antiviral defense and neurobiology to the pathogenesis of inflammatory and mood disorders."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "29", "end_ref": "35"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Ernest Beutler, Carol West "}, {"type": "b", "children": [{"type": "t", "text": "Polymorphisms in glucosylceramide (glucocerebroside) synthase and the Gaucher disease phenotype."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Isr Med Assoc J (2002)"}]}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12489486"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12489486"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Federica Di Sano, Barbara Fazi, Gennaro Citro, et al. 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