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Results for “Mevalonic Acid”

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PubMed1988

Incorporation of a product of mevalonic acid metabolism into proteins of Chinese hamster ovary cell nuclei.

We have examined the nuclear localization of isoprenylated proteins in CHO-K1 cells labeled with [14C]mevalonate. Nuclear proteins of 68, 70, and 74 kD, posttranslationally modified by an isoprenoid, are also components of a nuclear matrix-intermediate filament preparation from CHO cells. Furthermore, the 68-, 70-, and 74-kD isoprenylated polypeptides are immunoprecipitated from cell extracts with two different anti-lamin antisera. Based on exact two-dimensional comigration with lamin B, both from rat liver lamin and CHO nuclear matrix-intermediate filament preparations, and its immunoprecipitation with anti-lamin antisera, we conclude that the 68-kD isoprenylated protein found in nuclei from [14C]mevalonate-labeled CHO cells is lamin B. The more basic 74-kD isoprenylated nuclear protein is similar in molecular mass and isoelectric pH variants to the lamin A precursor polypeptide reported by others. Starving cells for mevalonate results in a dramatic accumulation of a polypeptide that comigrates on two-dimensional, non-equilibrium pH gradient electrophoresis (NEPHGE) gels with the 74-kD isoprenylated protein. The 70-kD isoprenylated protein, which is resolved on NEPHGE gels as being higher in molecular mass and slightly more basic than lamin B, has not yet been identified.

Animals↗
PubMed1992

Isopentenoid synthesis in isolated embryonic Drosophila cells: absolute mevalonic acid utilization and 3-hydroxy-3-methylglutaryl-coenzyme A reductase modulation.

The relationship between absolute isopentenoidogenesis (total and specific) and 3-hydroxy-3-methylglutaryl-coenzyme A suppression in response to increased mevalonate availability is unknown. We determined absolute isopentenoidogenesis values for the nonsterologenic Drosophila Kc cell incubated (2 h) with increasing [3H]mevalonate concentrations. At least 80% of the maximum suppression of 3-hydroxy-3-methyl glutaryl-co-enzyme A activity was achieved when total isopentenoidogenesis was increased only 2-fold. However, a 12-fold increase in total isopentenoidogenesis was achieved at higher exogenous [3H]mevalonate concentrations. Thus, modulation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase activity was coupled to physiological changes in mevalonate/nonsterol isopentenoid availability. In contrast, isopentenoid accumulation, oxidation, and secretion were enhanced with pharmacological increases in mevalonate availability. Furthermore, an apparent constancy of total isopentenoidogenesis values plus increased metabolism of exogenous mevalonate and a significant (35-45%) suppression of 3-hydroxy-3-methylglutaryl-coenzyme A reductase activity, in response to exogenous substrate concentrations (less than 150 microM), supported a partial or complete compensatory dimunition in endogenous substrate synthesis. Since these responses occurred within the 2-h study, earlier time periods must be assessed to (i) define the initial nonsterol-mediated regulatory response and (ii) to trap the nonsterol isopentenoid regulatory signal molecule(s).

Animals↗