Article
Secretion of acid Sphingomyelinase is affected by its polymorphic signal peptide.
Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology - 1 Jan 2014
Rhein Cosima, Reichel Martin, Mühle Christiane, Rotter Andrea, Schwab Sibylle G, Kornhuber Johannes
Abstract excerpt
BACKGROUND: Acid sphingomyelinase (ASM) catalyses the hydrolysis of sphingomyelin into ceramide, which acts as a lipid messenger that regulates important cellular functions. Deregulated ASM activity has been reported for different common diseases, but the mechanisms regulating ASM activity are still debated. ASM contains an exceptional signal peptide which is polymorphic due to a variable number of a...
Topics
- Alleles
- Cells, Cultured
- Humans
- Polymorphism, Genetic
- Protein Sorting Signals
- Sphingomyelin Phosphodiesterase
- Tumor Necrosis Factor-alpha
