AN ISOFORM OF THE PHOSPHATIDYLINOSITOL-TRANSFER PROTEIN TRANSFERS SPHINGOMYELIN AND IS ASSOCIATED WITH THE GOLGI SYSTEM

被引：89
作者：
DEVRIES, KJ
HEINRICHS, AAJ
CUNNINGHAM, E
BRUNINK, F
WESTERMAN, J
SOMERHARJU, PJ
COCKCROFT, S
WIRTZ, KWA
SNOEK, GT
机构：
[1] UCL, DEPT PHYSIOL, LONDON, ENGLAND
[2] UNIV HELSINKI, DEPT BASIC CHEM, HELSINKI, FINLAND
来源：
BIOCHEMICAL JOURNAL | 1995年 / 310卷
关键词：
D O I：
10.1042/bj3100643
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：
An isoform of the phosphatidylinositol-transfer protein (PI-TP) was identified in the cytosol fraction of bovine brain. This protein, designated PI-TP beta, has an apparent molecular mass of 36 kDa and an isoelectric point of 5.4. The N-terminal amino acid sequence (21 residues) is 90% similar to that of bovine brain PI-TP, henceforth designated PI-TP alpha. (molecular mass 35 kDa and pI 5.5). As observed for PI-TP alpha, PI-TP beta has a distinct preference for phosphatidylinositol over phosphatidylcholine. addition, it expresses a high transfer activity towards sphingomyelin. PI-TP alpha lacks this activity completely. By indirect immunofluorescence we demonstrated that, in Swiss mouse 3T3 fibroblasts, PI-TP beta is preferentially associated with the Golgi system whereas PI-TP alpha is predominantly present in the cytoplasm and the nucleus. In cytosol-depleted HL60 cells, both PI-TP alpha and PI-TP beta were equally effective at reconstituting guanosine 5'-[gamma-thio]triphosphate-mediated phospholipase C beta activity.
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页码：643 / 649
页数：7
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