Sterol Synthesis in Normal, Phytohemagglutinin-Stimulated, and Leukemic Mouse Lymphocytes

Chen, H.W.; Heiniger, H J; Kandutsch, Andrew A.

doi:10.1016/b978-0-12-651050-8.50025-9

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“…The normal S-phase burst of DNA synthesis is specifically prevented upon inhibition, during midto-late G1, of the rate controlling enzyme of cholesterogenesis, 3-hydroxy-3-methylglutaryl CoA reductase (HMGR) with either oxygenated sterols [5] or with competitive inhibitors of the enzyme, compactin and mevinolin [6- that are employed in cholesterol synthesis and the more common prenyl metabolites that arise from branches off the main cholesterogenie pathway. Thus, while mevalonate serves not only as direct precursor for the synthesis of sterol and other well-known isoprenoid metabolites (e.g., dolichol, the prenyl side chain of ubiquinone, etc.…”

Section: Introductionmentioning

confidence: 99%

Cellular distribution of cholesterogenesis‐linked, phosphoisoprenylated proteins in proliferating cells

1989

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A set of isoprenylated proteins has been detected in rapidly proliferating, suspension-grown murine lymphoma cells. Our evidence indicates that all of these isoprenylated proteins are phosphorylated. Subsequent to a 24 h incubation with mevinolin to deplete the intracellular mevalonate (MVA) level, cells were incubated with PHIMVA and/or 3ZPi and both total cell and subcellular fraction proteins were resolved via 1-and 2-D gel electrophoresis, then assessed via subsequent autoradiography. The phospho-isoprenylated proteins comprise a set spanning a molecular mass range of 21-69 kDa and all dispay acidic PI. MVA-derivatized proteins of 21-24 kDa, which consist of multiple isoforms, are present in both cytosolic and nuclear fractions. Larger phospho-isoprenylated protein species (4469 kDa) are specifically localized within the nucleus, where applicable extraction protocols indicate that they are part of or closely affiliated with the nuclear matrix-intermediate filament (NM-IF) components. The localization of the 69 kDa prenylated species within the NM-IF fraction, together with evidence of its phosphorylation, supports recent indications that this protein is the nuclear matrix component lamin B.

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Section: Introductionmentioning

confidence: 99%