Hydrolysis of micellar phosphatidylcholine accelerates cholesterol absorption in rats and caco-2 cells

Tadateru Hamada, Ikuo Ikeda, Kayoko Takashima, Makoto Kobayashi, Yoko Kodama, Takashi Inoue, Ryosuke Matsuoka, Katsumi Imaizumi

Research output: Contribution to journalArticlepeer-review

18 Citations (Scopus)


Lymphatic recovery of cholesterol infused into the duodenum as bile salt micelles containing phosphatidylcholine (PC) was accelerated by the co-administration of phospholipase A2 in bile and pancreatic juice diverted rats. Previously we observed that cholesterol esterase, which has the ability to hydrolyze PC, caused the same effect under a similar experimental condition (Ikeda et al., Biochim. Biophys. Acta, 1571, 34-44 (2002)). Accelerated cholesterol absorption was also observed when a part of micellar PC was replaced by lysophosphatidylcholine (LysoPC) and oleic acid. Phospholipase A2 facilitated the incorporation of micellar cholesterol into Caco-2 cells in a dose-dependent manner. There was a highly negative correlation between the incorporation of cholesterol into Caco-2 cells and the content of micellar PC remaining in the culture medium. The release of cholesterol as a monomer from bile salt micelles was enhanced when a part of micellar PC was replaced with LysoPC and oleic acid. These results strongly suggest that the release of monomer cholesterol from bile salt micelles is accelerated by hydrolysis of PC in bile salt micelles and hence that cholesterol absorption is enhanced.

Original languageEnglish
Pages (from-to)1726-1732
Number of pages7
JournalBioscience, Biotechnology and Biochemistry
Issue number9
Publication statusPublished - 2005


  • Cholesterol esterase
  • Intestinal cholesterol absorption
  • Phosphatidylcholine
  • Phospholipase A

ASJC Scopus subject areas

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry


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