Alkaline sphingomyelinase activity is decreased in human colorectal carcinoma
(1997) In Cancer 79(3). p.448-453- Abstract
- BACKGROUND: The metabolism of sphingomyelin generates important signals regulating cell proliferation and apoptosis. Previous studies found that the administration of colon carcinoma carcinogen was associated with an accumulation of membrane sphingomyelin, and that dietary sphingomyelin inhibited promotion of experimental colon carcinoma in mice, indicating that the abnormal metabolism of sphingomyelin is linked to colon carcinoma development. However, the changes in sphingomyelinase (SMase) activity in colon carcinoma have not been directly studied. The authors identified, specifically in the intestine, a distinctive alkaline SMase that differs from the known acidic and neutral SMases. The functions and clinical implications of the enzyme... (More)
- BACKGROUND: The metabolism of sphingomyelin generates important signals regulating cell proliferation and apoptosis. Previous studies found that the administration of colon carcinoma carcinogen was associated with an accumulation of membrane sphingomyelin, and that dietary sphingomyelin inhibited promotion of experimental colon carcinoma in mice, indicating that the abnormal metabolism of sphingomyelin is linked to colon carcinoma development. However, the changes in sphingomyelinase (SMase) activity in colon carcinoma have not been directly studied. The authors identified, specifically in the intestine, a distinctive alkaline SMase that differs from the known acidic and neutral SMases. The functions and clinical implications of the enzyme are unknown. This study examined the changes in all three SMase activities in human colorectal carcinoma. METHODS: Tissue samples were taken from colorectal carcinoma and normal mucosa from 18 patients. After homogenization, the activities of acidic, neutral, and alkaline SMase, as well as ceramidase and alkaline phosphatase, were determined. The enzyme activities in cancer tissue were compared with normal tissue from the same patients. RESULTS: In the normal tissue, there is an activity gradient from the ascending colon to the rectum for neutral and alkaline SMases but not for acidic SMase. In colorectal carcinoma, alkaline SMase activity was preferentially decreased by 75%, whereas acidic and neutral SMase activity decreased by 30% and 50%, respectively. No changes could be found for either ceramidase or alkaline phosphatase activity. CONCLUSIONS: Alkaline SMase activity preferentially decreases in human colorectal carcinoma, suggesting a regulatory role of the enzyme in colon mucosa cell proliferation. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1112157
- author
- Hertervig, Erik LU ; Nilsson, Åke LU ; Nyberg, Lena and Duan, Rui-Dong LU
- organization
- publishing date
- 1997
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- sphingomyelinase, ceramidase, colorectal carcinoma, humans
- in
- Cancer
- volume
- 79
- issue
- 3
- pages
- 448 - 453
- publisher
- John Wiley & Sons Inc.
- external identifiers
-
- pmid:9028353
- scopus:0031023763
- ISSN
- 1097-0142
- DOI
- 10.1002/(SICI)1097-0142(19970201)79:3<448::AID-CNCR4>3.0.CO;2-E
- language
- English
- LU publication?
- yes
- id
- a6a0391a-be9d-4983-80c8-9d53c7e49586 (old id 1112157)
- date added to LUP
- 2016-04-01 12:05:20
- date last changed
- 2024-01-08 07:51:30
@article{a6a0391a-be9d-4983-80c8-9d53c7e49586,
abstract = {{BACKGROUND: The metabolism of sphingomyelin generates important signals regulating cell proliferation and apoptosis. Previous studies found that the administration of colon carcinoma carcinogen was associated with an accumulation of membrane sphingomyelin, and that dietary sphingomyelin inhibited promotion of experimental colon carcinoma in mice, indicating that the abnormal metabolism of sphingomyelin is linked to colon carcinoma development. However, the changes in sphingomyelinase (SMase) activity in colon carcinoma have not been directly studied. The authors identified, specifically in the intestine, a distinctive alkaline SMase that differs from the known acidic and neutral SMases. The functions and clinical implications of the enzyme are unknown. This study examined the changes in all three SMase activities in human colorectal carcinoma. METHODS: Tissue samples were taken from colorectal carcinoma and normal mucosa from 18 patients. After homogenization, the activities of acidic, neutral, and alkaline SMase, as well as ceramidase and alkaline phosphatase, were determined. The enzyme activities in cancer tissue were compared with normal tissue from the same patients. RESULTS: In the normal tissue, there is an activity gradient from the ascending colon to the rectum for neutral and alkaline SMases but not for acidic SMase. In colorectal carcinoma, alkaline SMase activity was preferentially decreased by 75%, whereas acidic and neutral SMase activity decreased by 30% and 50%, respectively. No changes could be found for either ceramidase or alkaline phosphatase activity. CONCLUSIONS: Alkaline SMase activity preferentially decreases in human colorectal carcinoma, suggesting a regulatory role of the enzyme in colon mucosa cell proliferation.}},
author = {{Hertervig, Erik and Nilsson, Åke and Nyberg, Lena and Duan, Rui-Dong}},
issn = {{1097-0142}},
keywords = {{sphingomyelinase; ceramidase; colorectal carcinoma; humans}},
language = {{eng}},
number = {{3}},
pages = {{448--453}},
publisher = {{John Wiley & Sons Inc.}},
series = {{Cancer}},
title = {{Alkaline sphingomyelinase activity is decreased in human colorectal carcinoma}},
url = {{http://dx.doi.org/10.1002/(SICI)1097-0142(19970201)79:3<448::AID-CNCR4>3.0.CO;2-E}},
doi = {{10.1002/(SICI)1097-0142(19970201)79:3<448::AID-CNCR4>3.0.CO;2-E}},
volume = {{79}},
year = {{1997}},
}