Molecular cloning and expression of mouse ceramide glucosyltransferase

被引：0

作者：

Ichikawa, S ^{[1
]}

Ozawa, K ^{[1
]}

Hirabayashi, Y ^{[1
]}

机构：

[1] RIKEN, Inst Phys & Chem Res, Lab Cellular Glycobiol, Frontier Res Program, Wako, Saitama 35101, Japan

来源：

BIOCHEMISTRY AND MOLECULAR BIOLOGY INTERNATIONAL | 1998年 / 44卷 / 06期

关键词：

ceramide; glucosylceramide; glucosyltransferase; cDNA; mouse;

D O I：

暂无

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Ceramide glucosyltransferase (EC 2.4.1.80) catalyzes the first glycosylation step of glycosphingolipid (GSL) synthesis, the transfer of glucose from UDP-Glucose to hydrophobic ceramide and generate glucosylceramide (GlcCer). We have cloned mouse ceramide glucosyltransferase cDNA from a brain cDNA library by PCR based homology cloning. The nucleotide sequence determination revealed that mouse ceramide glucosyltransferase cDNA encodes 394 amino acids with a calculated molecular mass of 45 kDa. The amino acid sequence of mouse ceramide glucosyltransferase showed 98% identity with the human sequence. Homology searches against currently available databases identified three homologous proteins in Caenorhabditis elegans and one homologous protein in Cyanobacteria. Highly conserved sequences of ceramide glucosyltransferases and the homologs among a wide variety of, organisms suggest biological significance of the lipid glucosylation system.

引用

页码：1193 / 1202

页数：10

共 19 条

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