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Development of intestinal alkaline sphingomyelinase in rat fetus and newborn rat

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Lipids

Abstract

Sphingomyelin metabolism is a novel signal transduction pathway related to cell differentiation, proliferation, and apoptosis. Alkaline sphingomyelinase (alk-SMase) is specifically present in the intestinal tract of many species. The enzyme is important in digestion of dietary sphingomyelin. Milk is the ony exogenous source of sphingomyelin for an infant, and digestion of milk sphingomyelin may be important for development of intestinal mucosa. It is unknown whether alk-SMase is present before birth and whether it changes after birth and during the suckling period. We studied activities, expression, and distribution of alk-SMase in rat fetus and newborn. The changes of acid and neutral SMase as well as alkaline phosphatase were analyzed for comparison. Little activity of alk-SMase was identified up to gestation day 20, but increased 10 times during the following 2 d. After birth, the activity continused to increase during the following 4 wk. Western blot using IgY antibody against rat alk-SMase failed to identify the enzyme at gestation day 20 but clearly showed the protein at day 22. The distribution pattern of the enzyme along the intestinal tract in fetus was largely the same as in adult animals, but became more pronounced after birth. Short-term weaning had no effect on alk-SMase activity. The activities of acid and neutral SMase were high at gestation day 20 and decreased significantly before birth. The changes of alk-SMase also differed from those of alkaline phosphatase, another brush border enzyme. Thus, we conclude that alk-SMase is rapidly expressed during the last days of gestation and that the newborn rat acquires the ability to digest milk sphingomyelin early in life.

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Abbreviations

alk-SMase:

alkaline sphingomyelinase

GC:

glycocholate

GCDC:

glycochenodeoxycholate

PMSF:

phenylmethylsulfonyl fluoride

SM:

sphingomyelin

SMase:

sphingomyelinase

TC:

taurocholate

TDC:

taurodeoxycholate

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Authors and Affiliations

  1. Department of Medicine, Lund University Hospital, S-221 85, Lund, Sweden

    Jan Lillienau & Åke Nilsson

  2. Gastroenterology Lab, Biomedical Center, B11, Lund University, S-221 84, Lund, Sweden

    Yajun Cheng & Rui-Dong Duan

Authors
  1. Jan Lillienau
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  2. Yajun Cheng
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  3. Åke Nilsson
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  4. Rui-Dong Duan
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Correspondence to Rui-Dong Duan.

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Lillienau, J., Cheng, Y., Nilsson, Å. et al. Development of intestinal alkaline sphingomyelinase in rat fetus and newborn rat. Lipids 38, 545–549 (2003). https://doi.org/10.1007/s11745-003-1340-1

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  • DOI: https://doi.org/10.1007/s11745-003-1340-1

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