Title : Identification and characterization of murine mitochondria-associated neutral sphingomyelinase (MA-nSMase), the mammalian sphingomyelin phosphodiesterase 5.

Pub. Date : 2010 Jun 4

PMID : 20378533






3 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Neutral SMase (N-SMase) isoforms, which catalyze hydrolysis of sphingomyelin (SM) to ceramide and phosphocholine, have been found in the mitochondria of yeast and zebrafish, yet their existence in mammalian mitochondria remains unknown. Ceramides sphingomyelin phosphodiesterase 2 Homo sapiens
2 Neutral SMase (N-SMase) isoforms, which catalyze hydrolysis of sphingomyelin (SM) to ceramide and phosphocholine, have been found in the mitochondria of yeast and zebrafish, yet their existence in mammalian mitochondria remains unknown. Ceramides sphingomyelin phosphodiesterase 2 Homo sapiens
3 Importantly, overexpression of MA-nSMase in HEK293 cells significantly increased in vitro N-SMase activity and also modulated the levels of SM and ceramide, indicating that the identified cDNA encodes a functional SMase. Ceramides sphingomyelin phosphodiesterase 2 Homo sapiens