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Ceramidase is a lipid hydrolase enzyme that catalyzes the hydrolysis of ceramide into sphingosine and a fatty acid[1][3][4]. Multiple isoforms exist in mammals (acid, neutral, and alkaline ceramidases) encoded by distinct genes (e.g., ASAH1 for acid ceramidase)[1]. Ceramidase activity regulates the balance of ceramide, sphingosine, and sphingosine-1-phosphate—key bioactive lipids controlling cell fate, differentiation, apoptosis, and signaling[1][4]. Dysregulation or mutation of ceramidase leads to diverse pathologies, including Farber disease, cancer, neurodegeneration, and inflammation[1][2][3]. Ceramidase is considered a promising, but challenging, therapeutic target for cancer and other diseases driven by sphingolipid metabolism[1].
Competitive inhibition of ceramide conversion to sphingosine; modulation of sphingolipid rheostat (balance between ceramide, sphingosine, and sphingosine-1-phosphate); experimental drugs inhibit ceramidase to increase ceramide-induced apoptosis in cancer[1][2]
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