Alkaline sphingomyelinase activity in rat gastrointestinal tract: distribution and characteristics.
(1995) In Biochimica et Biophysica Acta 1259(1). p.49-55- Abstract
- Previous studies indicated that there was an alkaline sphingomyelinase (SMase) activity in small intestine, but its properties have not been studied in detail. In the present work, we studied the distribution of this enzyme activity in rat gastrointestinal tract and characterized it in intestinal mucosal homogenates. Little alkaline SMase activity was detected in the stomach and the duodenum. The activity in both mucosa and intestinal content increased in the small intestine and reached the maximum at the distal jejunum, then declined in the ileum and slightly increased again in the colon. The activity distribution pattern differed markedly from those of acid SMase and alkaline phosphatase. Little alkaline SMase activity could be found in... (More)
- Previous studies indicated that there was an alkaline sphingomyelinase (SMase) activity in small intestine, but its properties have not been studied in detail. In the present work, we studied the distribution of this enzyme activity in rat gastrointestinal tract and characterized it in intestinal mucosal homogenates. Little alkaline SMase activity was detected in the stomach and the duodenum. The activity in both mucosa and intestinal content increased in the small intestine and reached the maximum at the distal jejunum, then declined in the ileum and slightly increased again in the colon. The activity distribution pattern differed markedly from those of acid SMase and alkaline phosphatase. Little alkaline SMase activity could be found in bile, liver and pancreas before or after treatment with trypsin. The optimum pH of the alkaline SMase was 9. It specifically hydrolyzed sphingomyelin (SM), not phosphatidylcholine, to ceramide and phosphocholine. The alkaline SMase was bile salt dependent and was optionally activated by 3 mM bile salts. Triton X-100 could not mimic the effect of bile salt, rather dose-dependently inhibited the enzyme activity. Ca2+, Mg2+ did not change the alkaline SMase activity in the presence of bile salts, and reduced the activity in the absence of bile salt. Trypsin inactivated acid SMase in pancreas, liver and duodenum but had no influence on intestinal alkaline SMase activity. In conclusion, the intestinal alkaline SMase has a specific distribution pattern and the characters of it differ in several respects from the known acid and neutral SMases. (Less)
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https://lup.lub.lu.se/record/bb74bc29-fc83-42e6-a7d0-4b243b4fe575
- author
- Duan, Rui-Dong LU ; Nyberg, L and Nilsson, Åke LU
- publishing date
- 1995
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Biochimica et Biophysica Acta
- volume
- 1259
- issue
- 1
- pages
- 7 pages
- publisher
- Elsevier
- external identifiers
-
- scopus:0028862061
- ISSN
- 0006-3002
- DOI
- 10.1016/0005-2760(95)00137-2
- language
- English
- LU publication?
- no
- id
- bb74bc29-fc83-42e6-a7d0-4b243b4fe575
- date added to LUP
- 2019-02-03 10:38:07
- date last changed
- 2021-10-23 04:03:06
@article{bb74bc29-fc83-42e6-a7d0-4b243b4fe575,
abstract = {{Previous studies indicated that there was an alkaline sphingomyelinase (SMase) activity in small intestine, but its properties have not been studied in detail. In the present work, we studied the distribution of this enzyme activity in rat gastrointestinal tract and characterized it in intestinal mucosal homogenates. Little alkaline SMase activity was detected in the stomach and the duodenum. The activity in both mucosa and intestinal content increased in the small intestine and reached the maximum at the distal jejunum, then declined in the ileum and slightly increased again in the colon. The activity distribution pattern differed markedly from those of acid SMase and alkaline phosphatase. Little alkaline SMase activity could be found in bile, liver and pancreas before or after treatment with trypsin. The optimum pH of the alkaline SMase was 9. It specifically hydrolyzed sphingomyelin (SM), not phosphatidylcholine, to ceramide and phosphocholine. The alkaline SMase was bile salt dependent and was optionally activated by 3 mM bile salts. Triton X-100 could not mimic the effect of bile salt, rather dose-dependently inhibited the enzyme activity. Ca2+, Mg2+ did not change the alkaline SMase activity in the presence of bile salts, and reduced the activity in the absence of bile salt. Trypsin inactivated acid SMase in pancreas, liver and duodenum but had no influence on intestinal alkaline SMase activity. In conclusion, the intestinal alkaline SMase has a specific distribution pattern and the characters of it differ in several respects from the known acid and neutral SMases.}},
author = {{Duan, Rui-Dong and Nyberg, L and Nilsson, Åke}},
issn = {{0006-3002}},
language = {{eng}},
number = {{1}},
pages = {{49--55}},
publisher = {{Elsevier}},
series = {{Biochimica et Biophysica Acta}},
title = {{Alkaline sphingomyelinase activity in rat gastrointestinal tract: distribution and characteristics.}},
url = {{http://dx.doi.org/10.1016/0005-2760(95)00137-2}},
doi = {{10.1016/0005-2760(95)00137-2}},
volume = {{1259}},
year = {{1995}},
}