ELSEVIER Biochimica et Biophysica Acta 1259 (1995) 49-55
BB
Biochi~ic~a
et Biophysica A~ta
Alkaline sphingomyelinase activity in rat gastrointestinal tract:
distribution and characteristics
Rui-Dong Duan a,*, Lena Nyberg b, Ake Nilsson c
~ Department of Cell Biology 1, Experimental Research Center, University Hospital ofLund, Lund, Sweden
b Research Park ldeon, Swedish Dairies Association, Land, Sweden
c Gastroenterology Division, Department of Medicine, University Hospital ofLund, Lund, Sweden
Received 6 March 1995; accepted 8 June 1995
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 phospho-
choline. 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. Ca 2+, Mg 2÷ 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.
Keywords: Sphingomyelinase; Alkaline; Intestine; Bile salt
1. Introduction
The interest in sphingomyelin (SM) metabolism has
been greatly increased recently, mainly because the hydrol-
ysis products of SM have been found to have important
signalling effects on cell proliferation and differentiation
[1-3]. The first step of hydrolysis of SM is catalysed by
sphingomyelinase (SMase), which cleaves SM to ceramide
and phosphocholine. Two types of SMase have been iden-
tified, characterized, and purified [4]. The first one is the
acid SMase which is predominantly localized in lyso-
somes, with optimum pH being 4.5 to 5.5 [4-6]. It digests
cellular SM and also SM associated with low-density
lipoproteins that is endocytosed into the cells. The other
known SMase is the neutral SMase with an optimum pH
of 7.5. The neutral SMase is characterized as Mg2+-depen -
* Corresponding author. Fax: +46 46 137277.
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dent and its activity was abolished by EDTA [7-10]. The
neutral SMase is located in plasma membrane and is
believed to be important in generating lipid messengers to
regulate cellular functions including proliferation, differen-
tiation, and apoptosis [1-3].
About 25 years ago, Nilsson [11,12] found another type
of SMase which was located in intestinal mucosa and was
different from the known acid and neutral SMases with its
alkaline optimal pH of 9.2. However, the distribution and
the characters of the alkaline SMase has not been specifi-
cally studied in detail. Such studies are of considerable
interest for at least two reasons. First, SM is a component
of normal diet [13-15] and the enzyme responsible for
digestion and absorption of dietary SM has not been well
documented. Second, the digestion of SM may potentially
have clinical implications, as indicated by the findings that
the amount of SM in the enterocytes may regulate the
absorption of cholesterol [16], and that administration of
dietary SM was able to inhibit the promotion of colon
cancers in mice exposed to a chemical carcinogen [17].