Abstract
We have identified the aspartic protease cathepsin D as a novel intracellular target protein for the lipid second messenger ceramide. Ceramide specifically binds to and induces CTSD proteolytic activity. A-SMase deficient cells derived from Niemann-Pick patients show decreased CTSD activity that was reconstituted by transfection with A-SMase cDNA. Ceramide accumulation in cells derived from A-ceramidase defective Farber patients correlates with enhanced CTSD activity. These findings suggest that A-SMase-derived ceramide targets endolysosomal CTSD.
Original language | English |
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Pages (from-to) | 305-315 |
Number of pages | 11 |
Journal | Advances in Experimental Medicine and Biology |
Volume | 477 |
State | Published - 2000 |
Externally published | Yes |
Keywords
- Acid Sphingomyelinase
- Cathepsin D
- Ceramide
- TID-Ceramide