![[Feedback]](/icons/banner/feedbackACT.gif){kind=icon}
![[For Subscribers]](/icons/banner/subscriberACT.gif){kind=icon}
![[Archive]](/icons/banner/archiveACT.gif){kind=icon}
![[Search]](/icons/banner/searchACT.gif){kind=icon}
![[Contents]](/icons/banner/tocACT.gif){kind=icon}
|
|
|
|
|
||
,2
* Division of Food Science, Incorporated Administrative Agency, National Institute of Health and Nutrition, 1–23-1 Toyama, Shinjuku-ku, Tokyo 162-8636, Japan;
Japan Society for the Promotion of Science, Tokyo 102-8471, Japan; and
** Department of Bioresource Science, Obihiro University of Agriculture and Veterinary Medicine, Obihiro, Hokkaido 080-8555, Japan
2To whom correspondence should be addressed. E-mail: sugawara{at}nih.go.jp.
We investigated the digestion of cerebrosides of plant origin prepared from maize, focusing especially on the digestive fates of trans-4, cis-8- and trans-4, trans-8-sphingadienine, which are common in higher plants. In the small intestinal mucosa and cecal contents of rats, the cerebrosidase activity at pH 5.2 toward the glucosyl linkage in maize cerebrosides (glucosylceramides) was similar to that in cerebrosides of mammalian origin. Similarly, the ceramidase activity toward the amide linkage in ceramides prepared from maize cerebrosides at pH 7.0 was the same as that toward ceramides of mammalian origin. In addition, maize cerebrosides were hydrolyzed to ceramide and free sphingoid bases in the digestive tract of rats after oral administration. To further evaluate the uptake by enterocytes of 4,8-sphingadienine, we used differentiated Caco-2 cells, derived from human colonic carcinoma, as a model of intestinal epithelial cells. The accumulation of sphingoid bases in Caco-2 cells incubated with each isomer of sphingadienine was lower than that after incubation with sphingosine (P < 0.05). Verapamil, a P-glycoprotein inhibitor, increased the accumulation of each sphingadienine but not of sphingosine, suggesting that the efflux of sphingadienine of plant origin, but not sphingosine of mammalian origin, was affected by P-glycoprotein. The digestibility of maize cerebrosides appears similar to that of cerebrosides of mammalian origin, but the metabolic fate of sphingoid bases of plant origin within enterocytes differs from that of sphingosine. Isomers of 4,8-sphingadienine degraded from dietary plant cerebrosides appear to be poorly absorbed from the digestive tract.
KEY WORDS: • Caco-2 cells • ceramide • cerebroside • sphingadienine • sphingolipids
This article has been cited by other articles:
|
|
 |
|
  K. L. Schnabl, M. Larcelet, A. B. R. Thomson, and M. T. Clandinin Uptake and fate of ganglioside GD3 in human intestinal Caco-2 cells Am J Physiol Gastrointest Liver Physiol, July 1, 2009; 297(1): G52 - G59. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 S. T. Pruett, A. Bushnev, K. Hagedorn, M. Adiga, C. A. Haynes, M. C. Sullards, D. C. Liotta, and A. H. Merrill Jr. Thematic Review Series: Sphingolipids. Biodiversity of sphingoid bases ("sphingosines") and related amino alcohols J. Lipid Res., August 1, 2008; 49(8): 1621 - 1639. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 E. H. Ahn, C.-C. Chang, and J. J. Schroeder Evaluation of sphinganine and sphingosine as human breast cancer chemotherapeutic and chemopreventive agents. Experimental Biology and Medicine, November 1, 2006; 231(10): 1664 - 1672. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 H. Symolon, E. M. Schmelz, D. L. Dillehay, and A. H. Merrill Jr. Dietary Soy Sphingolipids Suppress Tumorigenesis and Gene Expression in 1,2-Dimethylhydrazine-Treated CF1 Mice and ApcMin/+ Mice J. Nutr., May 1, 2004; 134(5): 1157 - 1161. [Abstract] [Full Text] [PDF]
|
|
