Abstract
The alkaline sphingomyelinase (SMase) was first found in rat intestinal brush border. The important roles of this enzyme in digestion of sphingomyelin and in mucosal cell proliferation have been suggested. In the present work, the distribution of the alkaline SMase in the tissues of human beings and animals have been studied. By assaying the enzyme activity in human biopsy samples, we found that the alkaline SMase activity was absent in the stomach, increased in the duodenum, present at high levels in the small intestine, and slightly declined in the colon and rectum. High activities were found similarly in the intestinal contents of the healthy adults and infants. The activities were also found in the intestinal mucosa of rats, normal and germ-free mice, and hamsters with the same distribution pattern as in humans, but not in the intestinal mucosa of guinea pigs. Apart from the intestinal tract, a SMase activity preferring alkaline pH was identified in human and guinea pig bile, but not in the bile of rat, pig, sheep, and cow. No activity was found in either pancreatic tissue or pancreatic juice in all species tested, and none was detected in human urine and milk. In conclusion, alkaline SMase exists predominantly in the digestive system with considerable tissue and species differences.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Hunnun YA, Linardic LM: Sphingolipid breakdown products: antiproliferative and tumor-suppresser lipids. Biochim Biophys Acta 1154:223–236, 1993
Zhang Y, Kolesnick R: Signaling through the sphingomyelin pathway. Endocrinology 136:4157–4160, 1995
Spence MW: Sphingomyelinase Adv Lipid Res 26:3–23, 1994
Chatterjee S: Neutral sphingomyelinase. Adv Lipid Res 26:25–57, 1994
Brady RO, Kanfer JN, Mock MB, Fredrickson DS: The metabolism of sphingomyelin II. Evidence of an enzymatic deficiency in Niemann-Pick disease. Proc Natl Acad Sci USA 55:366–370, 1966
Nilsson Å: The presence of sphingomyelin- and ceramidecleaving enzymes in the small intestinal tract. Biochim Biophys Acta 176:339–347, 1969
Christie W, Nible RC, Davis G: Phospholipids in milk and dietary products. J Soc Dairy Technol 1:10–12, 1987
Blank ML, Cress EA, Smith ZL, Snyder F: Meats and fish consumed in the American diet contain substantial amounts of ether linked phospholipids. J Nutr 122:1656–1661, 1992
Nilsson Å: Metabolism of sphingomyelin in the intestinal tract of the rat. Biochim Biophys Acta 164:575–584, 1968
Schmelz E-M, Crell KJ, Larocque R, Dillehay DL, Merrill Jr AH: Uptake and metabolism of sphingolipids in isolated intestinal loops of mice. J Nutr 124:702–712, 1994
Duan R-D, Nyberg L, Nilsson Å: Alkaline sphingomyelinase activity in rat gastrointestinal tract: distribution and characteristics. Biochim Biophys Acta 1259:49–55, 1995
Chen H, Born E, Mathur SN, Johlin FC, Field FJ: Sphingomyelin content of intestinal cell membranes regulates cholesterol absorption. Biochem J 286:771–777, 1992
Dudeja PK, Dahiya R, Brasitus TA: The role of sphingomyelin synthetase and sphingomyelinase in 1,2-dimethylhydrazine-induced lipid alterations of rat colonic plasma membranes. Biochim Biophys Acta 863:309–312, 1986
Dillehay DL, Sebb SK, Schmelz E-M, Merrill AH Jr: Dietary sphingomyelin inhibits 1,2-dimethylhydrazine-induced colon cancer in CF-1 mice. J Nutr 124:615–620, 1994
Merrill AH Jr, Schmelz E-M, Wang E, Schroeder JJ, Dillehay DL, Riley RT: Role of dietary sphingolipids and inhibitors of sphingolipid metabolism in cancer and other diseases. J Nutr 125:16775–16823, 1995
Nyberg L, Duan R-D, Axelson J, Nilsson Å: Identification of an alkaline sphingomyelinase activity in human bile. Biochim Biophys Acta 1300:42–48, 1996
Christie W: Rapid separation and quantification of lipid by HPLC and mass (light-scattering) detection. J Lipids Res 26:507–512, 1985
Stoffel W: Chemical synthesis of choline-labeled lacithins and sphingomyelin. Methods Enzymol 36:533–541, 1975
Gatt S, Dinur T, Gerhon ZL-B: Magnesium-dependent sphingomyelinase of infantile brain. Effects of detergents and a heat stable factor. Biochim Biophys Acta 531:206–214, 1978
Hernell O, Bläckberg L: Human milk bile salt stimulated lipase: Functional and molecular aspects. J Pediatr 125:337–341, 1994
Scheele GA, Palade GE: Studies on the guinea pig pancreas. J Biol Chem 250:2660–2670, 1975
Hedlund M, Svensson M, Nilsson Å, Duan R-D, Svanborg C: Role of the ceramide signalling pathway in cytokine responses to P fimbriated Escherichia coli. J Exp Med 183:1037–1044, 1996
Quintern LE, Weitz G, Nehrkorn H, Tager JM, Schram AW, Sandhoff K: Acid sphingomyelinase from human urine: purification and characterization. Biochim Biophys Acta 922:323–336, 1987
Chatterjee S, Ghosh N: Neutral sphingomyelinase from human urine. Purification and preparation of monospecific antibodies. J Biol Chem 264:12554–12561, 1989
Bouhours J-F, Bouhours D, Hansson G: Developmental changes of glycosphingolipid composition of epithelia of rat digestive tract. Adv Lipid Res 26:353–372, 1994
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Duan, R.D., Hertervig, E., Nyberg, L. et al. Distribution of alkaline sphingomyelinase activity in human beings and animals. Digest Dis Sci 41, 1801–1806 (1996). https://doi.org/10.1007/BF02088748
Received:
Revised:
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF02088748