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Expression of a Functional Sphingomyelinase ofPseudomonassp. TK4 in Mammalian Cells
Author(s) -
Yasuhiro Horibata,
Noriyuki Sueyoshi,
Makoto Ito
Publication year - 2007
Publication title -
bioscience biotechnology and biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.509
H-Index - 116
eISSN - 1347-6947
pISSN - 0916-8451
DOI - 10.1271/bbb.60544
Subject(s) - acid sphingomyelinase , sphingomyelin , ceramide , sphingolipid , pseudomonas , microbiology and biotechnology , biochemistry , sphingomyelin phosphodiesterase , biology , chemistry , bacteria , membrane , genetics , apoptosis
We report here the expression of a bacterial sphingomyelinase in mammalian cells as a functionally active form. A chimeric Pseudomonas sphingomyelinase fused with the lysosomal sorting motif of lysosomal acid phosphatase was sorted to lysosomes in mammalian cells. As expected, the chimeric SMase hydrolyzed sphingomyelin in vivo to produce ceramide, part of which was converted to glucosylceramide.

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