Abstract
Three new types of regulatory somatic cell mutants defective in expression of the enzyme 3-hydroxy-3-methylglutaryl coenzyme A reductase are described. They include a recessive mutant with abnormally high enzyme activity, apparently defective in degradation of the enzyme, and one, phenotypically a mevalonate auxotroph, that maintains permanently repressed levels of enzyme activity and are recessive, constitutive mutants. These mutants offer means for analyses of the mechanism of regulation of expression of 3-hydroxy-3-methylglutaryl coenzyme A reductase in cultured fibroblasts.
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- Beg Z. H., Stonik J. A., Brewer H. B., Jr Characterization and regulation of reductase kinase, a protein kinase that modulates the enzymic activity of 3-hydroxy-3-methylglutaryl-coenzyme A reductase. Proc Natl Acad Sci U S A. 1979 Sep;76(9):4375–4379. doi: 10.1073/pnas.76.9.4375. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Beirne O. R., Heller R., Watson J. A. Regulation of 3-hydroxy-3-methylglutaryl coenzyme a reductase in minimal deviation hepatoma 7288C. Immunological measurements in hepatoma tissue culture cells. J Biol Chem. 1977 Feb 10;252(3):950–954. [PubMed] [Google Scholar]
- Cham B. E., Knowles B. R. A solvent system for delipidation of plasma or serum without protein precipitation. J Lipid Res. 1976 Mar;17(2):176–181. [PubMed] [Google Scholar]
- Goldstein J. L., Brown M. S. The low-density lipoprotein pathway and its relation to atherosclerosis. Annu Rev Biochem. 1977;46:897–930. doi: 10.1146/annurev.bi.46.070177.004341. [DOI] [PubMed] [Google Scholar]
- HAM R. G. CLONAL GROWTH OF MAMMALIAN CELLS IN A CHEMICALLY DEFINED, SYNTHETIC MEDIUM. Proc Natl Acad Sci U S A. 1965 Feb;53:288–293. doi: 10.1073/pnas.53.2.288. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kandutsch A. A., Chen H. W., Heiniger H. J. Biological activity of some oxygenated sterols. Science. 1978 Aug 11;201(4355):498–501. doi: 10.1126/science.663671. [DOI] [PubMed] [Google Scholar]
- Kandutsch A. A., Chen H. W. Inhibition of sterol synthesis in cultured mouse cells by cholesterol derivatives oxygenated in the side chain. J Biol Chem. 1974 Oct 10;249(19):6057–6061. [PubMed] [Google Scholar]
- Kao F. T., Johnson R. T., Puck T. T. Complementation analysis on virus-fused Chinese hamster cells with nutritional markers. Science. 1969 Apr 18;164(3877):312–314. doi: 10.1126/science.164.3877.312. [DOI] [PubMed] [Google Scholar]
- Kao F. T., Puck T. T. Genetics of somatic mammalian cells, VII. Induction and isolation of nutritional mutants in Chinese hamster cells. Proc Natl Acad Sci U S A. 1968 Aug;60(4):1275–1281. doi: 10.1073/pnas.60.4.1275. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kao F. T., Puck T. T. Genetics of somatic mammalian cells. IX. Quantitation of mutagenesis by physical and chemical agents. J Cell Physiol. 1969 Dec;74(3):245–258. doi: 10.1002/jcp.1040740305. [DOI] [PubMed] [Google Scholar]
- Sinensky M. A nutritional test for the low density lipoprotein receptor in Chinese hamster fibroblasts. FEBS Lett. 1979 Oct 1;106(1):129–131. doi: 10.1016/0014-5793(79)80709-7. [DOI] [PubMed] [Google Scholar]
- Sinensky M., Duwe G., Pinkerton F. Defective regulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase in a somatic cell mutant. J Biol Chem. 1979 Jun 10;254(11):4482–4486. [PubMed] [Google Scholar]
- Sinensky M. Isolation of a mammalian cell mutant resistant to 25-hydroxy cholesterol. Biochem Biophys Res Commun. 1977 Oct 10;78(3):863–867. doi: 10.1016/0006-291x(77)90502-2. [DOI] [PubMed] [Google Scholar]