Secretion of Acid Sphingomyelinase is Affected by its Polymorphic Signal Peptide | Zendy

Cosima Rhein | Zendy; Martin Reichel | Zendy; Christiane Mühle | Zendy; Andrea Rotter | Zendy; Sibylle G. Schwab | Zendy; Johannes Kornhuber | Zendy

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Secretion of Acid Sphingomyelinase is Affected by its Polymorphic Signal Peptide

Author(s) -

Cosima Rhein,

Martin Reichel,

Christiane Mühle,

Andrea Rotter,

Sibylle G. Schwab,

Johannes Kornhuber

Publication year - 2014

Publication title -

cellular physiology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.486

H-Index - 87

eISSN - 1421-9778

pISSN - 1015-8987

DOI - 10.1159/000366345

Subject(s) - secretion , signal peptide , acid sphingomyelinase , biology , sphingomyelin , ceramide , allele , peptide , gene , microbiology and biotechnology , peptide sequence , biochemistry , cholesterol , apoptosis

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 hexanucleotide sequence that determines the length of the hydrophobic core. We investigated the impact of the signal peptide polymorphism on the regulation of ASM activity and secretion in vivo and in vitro.

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