Isoprenylated proteins in myelin Journal Article
| Authors: | Sepp-Lorenzino, L.; Coleman, P. S.; Larocca, J. N. |
| Article Title: | Isoprenylated proteins in myelin |
| Abstract: | Abstract: Incubation of rat brainstem slices with [3H]‐ mevalonate ([3H]MVA) in the presence of lovastatin resulted in the incorporation of label into three groups of myelin‐associated proteins with molecular masses of 47, 21–27, and 8 kDa, as revealed on sodium dodecyl sulfate‐ polyacrylamide rod gel electrophoresis. Although the gel patterns of [3H]MVA‐derived prenylated proteins were similar, the relative level of 3H incorporated into each protein species differed between myelin and the brainstem homogenate. Immunoprecipitation studies identified the 47‐kDa prenylated protein as a 2′‐3′‐cyclic nucleotide phospho‐ diesterase, whereas the 8‐kDa protein proved to be the γ subunit of membrane‐associated guanine nucleotide regulatory protein. The 3H‐labeled 21–27‐kDa group in myelin corresponds to the molecular mass of the extensive Ras‐ like family of monomeric GTP‐binding proteins known to be prenylated in other tissues. Increase in lovastatin concentration resulted in reduced levels of [3H]MVA‐labeled species in myelin and concomitantly increased levels in the cytosol. A cold MVA chase restored to normality the appearance of [3H]MVA‐labeled proteins in myelin. Furthermore, a high lovastatin concentration in the brainstem slice incubation mixture altered the appearance of newly synthesized nonprenylated myelin proteins, including proteolipid protein and the 17‐kDa subspecies of myelin basic protein. Because other myelin proteins were unaffected by the high lovastatin concentration, restricting the availability of MVA in myelin‐forming cells may selectively alter processes required for myelinogenesis. Although the molecular basis for the” different MVA requirements in myelin‐ forming cells remains undefined, it may involve an alteration in the biological activity of certain proteins that require prenylation to be functionally active, and that are responsible for promoting insertion of specific proteins into the myelin membrane. Copyright © 1994, Wiley Blackwell. All rights reserved |
| Keywords: | nonhuman; animals; animal tissue; gtp-binding proteins; animalia; protein processing; protein synthesis; rat; rats; rats, sprague-dawley; protein structure; guanine nucleotide binding protein; brain stem; oncogene ras; cytosol; myelin; myelination; polyacrylamide gel electrophoresis; tritium; hydroxymethylglutaryl-coa reductase inhibitors; mevinolin; myelin sheath; protein isoprenylation; lovastatin; immunosorbent techniques; mevalonic acid; priority journal; article; myelin proteins; hydroxymethylglutaryl coa reductases; myelin protein; gtp‐binding protein; isopren‐ ylation |
| Journal Title: | Journal of Neurochemistry |
| Volume: | 62 |
| Issue: | 4 |
| ISSN: | 0022-3042 |
| Publisher: | Wiley Blackwell |
| Date Published: | 1994-04-01 |
| Start Page: | 1539 |
| End Page: | 1545 |
| Language: | English |
| DOI: | 10.1046/j.1471-4159.1994.62041539.x |
| PROVIDER: | scopus |
| PUBMED: | 8133281 |
| DOI/URL: | |
| Notes: | Export Date: 14 January 2019 -- Article -- Source: Scopus |
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