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Isoprenylated proteins in myelin
L Sepp-Lorenzino1, P S Coleman, J N Larocca
1SKI Program in Cell Biology, Memorial Sloan-Kettering Cancer Center, New York, New York.
Journal of Neurochemistry
|April 1, 1994
Summary
Lovastatin treatment of rat brainstem slices reveals prenylated proteins in myelin. Inhibiting mevalonate (MVA) synthesis selectively impacts myelin protein production and assembly.
Area of Science:
- Neuroscience
- Biochemistry
- Cell Biology
Background:
- Myelin is a crucial lipid-rich sheath insulating nerve fibers.
- Prenylation, a post-translational modification, is essential for the function of many proteins.
- The role of prenylation in myelin protein synthesis and assembly is not fully understood.
Purpose of the Study:
- To investigate the incorporation of mevalonate into myelin-associated proteins.
- To identify prenylated proteins within rat brainstem myelin.
- To determine the effect of lovastatin on myelin protein synthesis and prenylation.
Main Methods:
- Incubation of rat brainstem slices with [3H]-mevalonate and lovastatin.
- Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) for protein separation.
- Immunoprecipitation to identify specific prenylated proteins.
Main Results:
- [3H]-mevalonate was incorporated into 47, 21-27, and 8 kDa myelin-associated proteins.
- The 47-kDa protein identified as 2'-3'-cyclic nucleotide phosphodiesterase; 8-kDa protein as gamma subunit of G protein.
- Lovastatin reduced myelin prenylated proteins, increased cytosolic levels, and altered nonprenylated myelin protein synthesis.
Conclusions:
- Prenylation is a significant post-translational modification for specific myelin proteins.
- Mevalonate availability is critical for the proper synthesis and assembly of myelin proteins.
- Lovastatin's impact suggests a selective vulnerability in myelinogenesis to disruptions in the mevalonate pathway.