Utilization of geranylgeraniol for protein isoprenylation in C6 glial cells

Dean C. Crick, Charies J. Waechter, Douglas A. Andres

Research output: Contribution to journalArticlepeer-review

44 Scopus citations

Abstract

When rat C6 glial celles were incubated with [3H]geranylgeraniol (GGol), radioactivity was incorporated into a delipidated protein fraction. SDS-PAGE analysis of the protein fraction labeled by [3H]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 [14C]mevalonolactone. An isotopically labeled product, chromatographically identical to geranylgeranyl-cysteine (GG-Cys), was released by Pronase E digestion of the [3H]GGol-labeled protein. When the protein fraction from cells metabolically labeled with [3H]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.

Original languageEnglish
Pages (from-to)955-961
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume205
Issue number1
DOIs
StatePublished - Nov 30 1994

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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