Alkaline sphingomyelinase (NPP7) in hepatobiliary diseases : A field that needs to be closely studied
(2018) In World Journal of Hepatology 10(2). p.246-253- Abstract
Alkaline sphingomyelinase cleaves phosphocholine from sphingomyelin, platelet-activating factor, lysophosphatidylcholine, and less effectively phosphatidylcholine The enzyme shares no structure similarities with acid or neutral sphingomyelinase but belongs to ectonucleotide pyrophosphatase/phosphodiesterase (NPP) family and therefore is also called NPP7 nowadays. The enzyme is expressed in the intestinal mucosa in many species and additionally in human liver. The enzyme in the intestinal tract has been extensively studied but not that in human liver. Studies on intestinal alkaline sphingomyelinase show that it inhibits colonic tumorigenesis and inflammation, hydrolyses dietary sphingomyelin, and stimulates cholesterol absorption. The... (More)
Alkaline sphingomyelinase cleaves phosphocholine from sphingomyelin, platelet-activating factor, lysophosphatidylcholine, and less effectively phosphatidylcholine The enzyme shares no structure similarities with acid or neutral sphingomyelinase but belongs to ectonucleotide pyrophosphatase/phosphodiesterase (NPP) family and therefore is also called NPP7 nowadays. The enzyme is expressed in the intestinal mucosa in many species and additionally in human liver. The enzyme in the intestinal tract has been extensively studied but not that in human liver. Studies on intestinal alkaline sphingomyelinase show that it inhibits colonic tumorigenesis and inflammation, hydrolyses dietary sphingomyelin, and stimulates cholesterol absorption. The review aims to summarize the current knowledge on liver alkaline sphingomyelinase in human and strengthen the necessity for close study on this unique human enzyme in hepatobiliary diseases.
(Less)
- author
- Duan, Rui Dong LU
- organization
- publishing date
- 2018-02-01
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Alkaline sphingomyelinase, Autotaxin, Cholangiocarcinoma, Gallstone, Liver diseases, Nucleotide pyrophosphatase/phosphodiesterase 7, Platelet-activating factor, Sphingomyelin
- in
- World Journal of Hepatology
- volume
- 10
- issue
- 2
- pages
- 8 pages
- publisher
- Baishideng Publishing Group
- external identifiers
-
- pmid:29527260
- pmid:29527260
- scopus:85042758274
- ISSN
- 1948-5182
- DOI
- 10.4254/wjh.v10.i2.246
- language
- English
- LU publication?
- yes
- id
- e3bdf21d-d22b-4fec-af67-bf6682034d1e
- date added to LUP
- 2018-03-26 16:30:53
- date last changed
- 2024-10-16 00:05:49
@article{e3bdf21d-d22b-4fec-af67-bf6682034d1e,
abstract = {{<p>Alkaline sphingomyelinase cleaves phosphocholine from sphingomyelin, platelet-activating factor, lysophosphatidylcholine, and less effectively phosphatidylcholine The enzyme shares no structure similarities with acid or neutral sphingomyelinase but belongs to ectonucleotide pyrophosphatase/phosphodiesterase (NPP) family and therefore is also called NPP7 nowadays. The enzyme is expressed in the intestinal mucosa in many species and additionally in human liver. The enzyme in the intestinal tract has been extensively studied but not that in human liver. Studies on intestinal alkaline sphingomyelinase show that it inhibits colonic tumorigenesis and inflammation, hydrolyses dietary sphingomyelin, and stimulates cholesterol absorption. The review aims to summarize the current knowledge on liver alkaline sphingomyelinase in human and strengthen the necessity for close study on this unique human enzyme in hepatobiliary diseases.</p>}},
author = {{Duan, Rui Dong}},
issn = {{1948-5182}},
keywords = {{Alkaline sphingomyelinase; Autotaxin; Cholangiocarcinoma; Gallstone; Liver diseases; Nucleotide pyrophosphatase/phosphodiesterase 7; Platelet-activating factor; Sphingomyelin}},
language = {{eng}},
month = {{02}},
number = {{2}},
pages = {{246--253}},
publisher = {{Baishideng Publishing Group}},
series = {{World Journal of Hepatology}},
title = {{Alkaline sphingomyelinase (NPP7) in hepatobiliary diseases : A field that needs to be closely studied}},
url = {{http://dx.doi.org/10.4254/wjh.v10.i2.246}},
doi = {{10.4254/wjh.v10.i2.246}},
volume = {{10}},
year = {{2018}},
}