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Sphingolipid hydrolysis enzymes in the gastrointestinal tract

Duan, Rui-Dong LU and Nilsson, Åke LU (1999) In Methods in Enzymology 311. p.276-286
Abstract
In the intestinal tract, there are enzymes that hydrolyze both endogenous and exogenous sphingolipids. The alkaline sphingomyelinases (SMase) of the gut and human bile have been most studied, and a major part of this chapter discusses these enzymes. It also discusses studies of ceramidase, glycosylceramidase, and the digestion of dietary sphingolipids. In the intestinal tract, a distinct enzyme that hydrolyzes SM was discovered in 1969 by Nilsson and named “alkaline SMase.” The alkaline SMase activity is localized specifically in the intestinal tract and is not detectable in other organs, including brain, kidney, lung, spleen, testis, pancreas, and stomach, or in milk and urine. The intestinal alkaline SMase is not bacterial in origin as... (More)
In the intestinal tract, there are enzymes that hydrolyze both endogenous and exogenous sphingolipids. The alkaline sphingomyelinases (SMase) of the gut and human bile have been most studied, and a major part of this chapter discusses these enzymes. It also discusses studies of ceramidase, glycosylceramidase, and the digestion of dietary sphingolipids. In the intestinal tract, a distinct enzyme that hydrolyzes SM was discovered in 1969 by Nilsson and named “alkaline SMase.” The alkaline SMase activity is localized specifically in the intestinal tract and is not detectable in other organs, including brain, kidney, lung, spleen, testis, pancreas, and stomach, or in milk and urine. The intestinal alkaline SMase is not bacterial in origin as similar activity is found in ordinary mice and germ-free mice and in meconium of human fetus as early as 26 weeks of gestation. In the intestines of different experimental animals, the highest activities were in rat, mouse, pig, and baboon, lower activity in rabbit, and little activity in the guinea pig. Whether these species differences indicate genetic variation or an influence of diet composition on the expression of the enzyme in the intestine is unknown. (Less)
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Contribution to journal
publication status
published
subject
in
Methods in Enzymology
volume
311
pages
11 pages
publisher
Academic Press
external identifiers
  • scopus:0032717225
ISSN
0076-6879
DOI
10.1016/S0076-6879(00)11089-4
language
English
LU publication?
yes
id
dee14e80-f02b-4913-a34f-9831f58aef69
date added to LUP
2019-02-03 16:43:40
date last changed
2024-01-15 13:35:04
@article{dee14e80-f02b-4913-a34f-9831f58aef69,
  abstract     = {{In the intestinal tract, there are enzymes that hydrolyze both endogenous and exogenous sphingolipids. The alkaline sphingomyelinases (SMase) of the gut and human bile have been most studied, and a major part of this chapter discusses these enzymes. It also discusses studies of ceramidase, glycosylceramidase, and the digestion of dietary sphingolipids. In the intestinal tract, a distinct enzyme that hydrolyzes SM was discovered in 1969 by Nilsson and named “alkaline SMase.” The alkaline SMase activity is localized specifically in the intestinal tract and is not detectable in other organs, including brain, kidney, lung, spleen, testis, pancreas, and stomach, or in milk and urine. The intestinal alkaline SMase is not bacterial in origin as similar activity is found in ordinary mice and germ-free mice and in meconium of human fetus as early as 26 weeks of gestation. In the intestines of different experimental animals, the highest activities were in rat, mouse, pig, and baboon, lower activity in rabbit, and little activity in the guinea pig. Whether these species differences indicate genetic variation or an influence of diet composition on the expression of the enzyme in the intestine is unknown.}},
  author       = {{Duan, Rui-Dong and Nilsson, Åke}},
  issn         = {{0076-6879}},
  language     = {{eng}},
  pages        = {{276--286}},
  publisher    = {{Academic Press}},
  series       = {{Methods in Enzymology}},
  title        = {{Sphingolipid hydrolysis enzymes in the gastrointestinal tract}},
  url          = {{http://dx.doi.org/10.1016/S0076-6879(00)11089-4}},
  doi          = {{10.1016/S0076-6879(00)11089-4}},
  volume       = {{311}},
  year         = {{1999}},
}