Subcellular study of sphingoid base phosphorylation in rat tissues: evidence for multiple sphingosine kinases

被引：29

作者：

Gijsbers, S ^{[1
]}

Van der Hoeven, G ^{[1
]}

Van Veldhoven, PP ^{[1
]}

机构：

[1] Katholieke Univ Leuven, Dept Mol Celbiol, Afdeling Farmakol, B-3000 Louvain, Belgium

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS | 2001年 / 1532卷 / 1-2期

关键词：

sphingosine phosphate; signal transduction; calcium; sphinganine; lipid kinases;

D O I：

10.1016/S1388-1981(01)00111-1

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：

The enzymatic phosphorylation of sphingoid bases was analysed in rat tissues, using D-erythro-[4,5-H-3]sphinganine as substrate. After optimisation of the assay, taking care to block sphingosine-phosphate lyase and sphingosine phosphatase, highest ATP-dependent kinase activities were present in testis, followed by kidney, and intestinal mucosa. Approximately two thirds of the kidney activity were membrane bound, the remaining being cytosolic. Classical cell fractionation studies of kidney and liver did not allow to identify unequivocally the subcellular site of the membrane bound kinase. Separation of a particulate fraction from kidney homogenates by Percoll gradient and sucrose density gradient centrifugation revealed that kinase activities are associated with vesicles derived from the endoplasmic reticulum and the plasma membrane. Based on indirect data, such as the effect of detergents and divalent ions, the cytosolic and both membrane bound activities appear to reside in different proteins. N,N-Dimethylsphingenine was inhibitory to all three different kinases, which were mainly active towards the D-erythro isomers of sphingenine and sphinganine. (C) 2001 Elsevier Science B.V. All rights reserved.

引用

页码：37 / 50

页数：14

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