UTILIZATION OF GERANYLGERANIOL FOR PROTEIN ISOPRENYLATION IN C6 GLIAL-CELLS

被引:48
作者
CRICK, DC [1 ]
WAECHTER, CJ [1 ]
ANDRES, DA [1 ]
机构
[1] UNIV KENTUCKY,COLL MED,DEPT BIOCHEM,LEXINGTON,KY 40536
关键词
D O I
10.1006/bbrc.1994.2758
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
When rat C6 glial cells were incubated with [H-3]geranylgeraniol (GGol), radioactivity was incorporated into a delipidated protein fraction. SDS-PAGE analysis of the protein fraction labeled by [H-3]GGol revealed a 46 kDa polypeptide and a group of labeled polypeptides (19-27 kDa) in the same size range as the small GTP-binding proteins. A similar pattern of labeled polypeptides was seen when C6 cells were metabolically labeled with [C-14]mevalonolactone. An isotopically labeled product, chromatographically identical to geranylgeranyl-cysteine (GG-Cys), was released by Pronase E digestion of the [H-3]GGol-labeled protein. When the protein fraction from cells metabolically labeled with [H-3]mevalonolactone was digested with Pronase E, two radiolabeled products were released with the chromatographic mobilities of farnesyl-cysteine (F-Cys) and GG-Cys. These studies suggest that C6 glial cells are capable of converting GGol to geranylgeranyl pyrophosphate (GG-P-P), or perhaps a novel ''activated'' form of the allylic isoprenol, that can be utilized for protein isoprenylation reactions. (C) 1994 Academic Press, Inc.
引用
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页码:955 / 961
页数:7
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