Disease relevance of CDase

• Transgenic expression of ceramidase suppresses retinal degeneration in Drosophila arrestin and phospholipase C mutants [1].

High impact information on CDase

• Ceramidase expression facilitates the endocytic turnover of Rh1 [1].
• Therefore, the phenotypic consequence of ceramidase expression in photoreceptors is caused by facilitation of endocytosis [1].
• Using the BLAST program, a neutral CDase homologue (AE003774) was found in the Drosophila GenBank and cloned from a cDNA library of Drosophila imaginal discs [2].
• The enzyme hydrolyzed various N-acylsphingosines but not galactosylceramide, GM1a or sphingomyelin, and exhibited a peak of activity at pH 6.5-7.5, and thus was classified as a neutral CDase [2].
• Ceramidase regulates synaptic vesicle exocytosis and trafficking [3].

Biological context of CDase

• These results indicate that SLAB ceramidase function controls presynaptic terminal sphingolipid composition to regulate vesicle fusion and trafficking, and thus the strength and reliability of synaptic transmission [3].

Anatomical context of CDase

• Here, we show that expression of ceramidase facilitates the dissolution of incompletely formed and inappropriately located elements of rhabdomeric membranes in ninaE(I17) mutants lacking the G protein receptor Rh1 in R1-R6 photoreceptor cells [1].

Associations of CDase with chemical compounds

• Suppression of degeneration in arrestin mutant flies expressing ceramidase correlated with a decrease in ceramide levels [4].

Regulatory relationships of CDase

• Consistent with a cell-nonautonomous function, overexpression of ceramidase in tissues distant from photoreceptors suppresses photoreceptor degeneration in an arrestin mutant and facilitates membrane turnover in a rhodopsin null mutant [5].

Analytical, diagnostic and therapeutic context of CDase

• We report here the molecular cloning and characterization of the Drosophila neutral ceramidase (CDase) [2].

References