Expression of a functional sphingomyelinase of Pseudomonas sp. TK4 in mammalian cells.
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.
Horibata
Yasuhiro
Y
Department of Bioscience and Biotechnology, Graduate School of Bioresource and Bioenvironmental Sciences, Kyushu University, Fukuoka, Japan.
Sueyoshi
Noriyuki
N
Ito
Makoto
M
D000135:Acid Phosphatase / Q000378:metabolism; D000818:Animals; D016466:CHO Cells; D006224:Cricetinae; D003412:Cricetulus; D004269:DNA, Bacterial / Q000096:biosynthesis / Q000235:genetics; D005260:Female; D049452:Green Fluorescent Proteins / Q000096:biosynthesis / Q000235:genetics; D008247:Lysosomes / Q000201:enzymology; D011549:Pseudomonas / Q000201:enzymology*; D013108:Sphingomyelin Phosphodiesterase / Q000096:biosynthesis*; D013109:Sphingomyelins / Q000378:metabolism
D004269:DNA, Bacterial; D013109:Sphingomyelins; D049452:Green Fluorescent Proteins; D000135:Acid Phosphatase; D013108:Sphingomyelin Phosphodiesterase