DES2 protein is responsible for phytoceramide biosynthesis in the mouse small intestine

The C-4 hydroxylation of sphinganine and dihydroceramide is a rate-limiting reaction in the biosynthesis of phytosphingolipids. Mouse DES1 (MDES1) cDNA homologous to the Drosophila melanogaster degenerative spermatocyte gene-1 (des-1) cDNA leads to sphingosine Delta4-desaturase activity, and another...

Full description

Saved in:
Bibliographic Details
Published in:Biochemical journal 2004-05, Vol.379 (Pt 3), p.687-695
Main Authors: Omae, Fumio, Miyazaki, Masao, Enomoto, Ayako, Suzuki, Minoru, Suzuki, Yusuke, Suzuki, Akemi
Format: Article
Language:English
Subjects:
Animals
Cell Extracts
Ceramides - biosynthesis
Ceramides - chemistry
COS Cells
Fatty Acid Desaturases - genetics
Fatty Acid Desaturases - metabolism
Immunohistochemistry
In Situ Hybridization
Intestine, Small - enzymology
Intestine, Small - metabolism
Membrane Proteins - genetics
Membrane Proteins - metabolism
Mice
Mixed Function Oxygenases - genetics
Mixed Function Oxygenases - metabolism
Multienzyme Complexes - genetics
Multienzyme Complexes - metabolism
Organ Specificity
Oxidoreductases - genetics
Oxidoreductases - metabolism
RNA, Messenger - genetics
RNA, Messenger - metabolism
Sphingosine - analogs & derivatives
Sphingosine - metabolism
Transfection
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The C-4 hydroxylation of sphinganine and dihydroceramide is a rate-limiting reaction in the biosynthesis of phytosphingolipids. Mouse DES1 (MDES1) cDNA homologous to the Drosophila melanogaster degenerative spermatocyte gene-1 (des-1) cDNA leads to sphingosine Delta4-desaturase activity, and another mouse homologue, MDES2, has bifunctional activity, producing C-4 hydroxysphinganine and Delta4-sphingenine in yeast [Ternes, Franke, Zahringer, Sperling and Heinz (2002) J. Biol. Chem. 277, 25512-25518]. Here, we report the characterization of mouse DES2 (MDES2) using an in vitro assay with a homogenate of COS-7 cells transfected with MDES2 cDNA and N -octanoyl-sphinganine and sphinganine as substrates. MDES2 protein prefers dihydroceramide as a substrate to sphinganine, and exhibits dihydroceramide Delta4-desaturase and C-4 hydroxylase activities. MDES2 mRNA content was high in the small intestine and abundant in the kidney. In situ hybridization detected signals of MDES2 mRNA in the crypt cells. Immunohistochemistry using an anti-MDES2 peptide antibody stained the crypt cells and the adjacent epithelial cells. These results suggest that MDES2 is the dihydroceramide C-4 hydroxylase responsible for the biosynthesis of enriched phytosphingoglycolipids in the microvillous membranes of intestinal epithelial cells.
ISSN:0264-6021
1470-8728
DOI:10.1042/bj20031425