Lipopolysaccharide-Induced NF-κB Activation in Mouse 70Z/3 Pre-B Lymphocytes Is Inhibited by Mevinolin and 5′-Methylthioadenosine: Roles of Protein Isoprenylation and Carboxyl Methylation Reactions

References

• Bailey, J. L. 1967. Techniques in protein chemistry, p. 340. American Elsevier, New York.
   Google Scholar
• Bright, S. W., T.-Y. Chen, L. M. Flebbe, M.-G. Lei, and D. C. Morrison. 1990. Generation and characterization of hamstermouse hybridomas secreting monoclonal antibodies for lipopolysaccharide receptor. J. Immunol. 145:1–7.
   PubMed Web of Science ®Google Scholar
• Briskin, M., M. Kuwabara, D. Sigman, and R. Wall. 1988. Induction of κ transcription by interferon-γ without activation of NF-κB. Science 242:1036–1037.
   PubMed Web of Science ®Google Scholar
• Chelsky, D., C. Sobotka, and C. L. O'Neill. 1989. Lamin B methylation and assembly into the nuclear envelope. J. Biol. Chem. 264:7637–7643.
   PubMedGoogle Scholar
• Clarke, S., J. P. Vogel, R. J. Deschenes, and J. Stock. 1988. Posttranslational modification of the Ha-ras oncogene protein: evidence for a third class of protein carboxyl methyltransferases. Proc. Natl. Acad. Sci. USA 85:4643–4647.
   PubMed Web of Science ®Google Scholar
• Daniel-Issakani, S., A. M. Speigel, and B. Strulovici. 1989. Lipopolysaccharide response is linked to the GTP binding protein, Gi2, in the promonocytic cell line U937. J. Biol. Chem. 264:20240–20247.
   PubMedGoogle Scholar
• DeFranco, A. L., M. R. Gold, and J. P. Jakway. 1987. B-lym- phocyte signal transduction in response to anti-immunoglobulin and bacterial lipopolysaccharide. Immunol. Rev. 95:161–176.
   PubMed Web of Science ®Google Scholar
• Dignam, J. D., R. M. Lebovitz, and R. G. Roeder. 1983. Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei. Nucleic Acids Res. 11:1475–1489.
   PubMed Web of Science ®Google Scholar
• Ferro, A. J., A. A. Vandenbark, and K. Marchitto. 1979. The role of 5′-methylthioadenosine phosphorylase in 5′-methylthio- adenosine-mediated inhibition of lymphocyte transformation. Biochim. Biophys. Acta 588:294–301.
   PubMedGoogle Scholar
• Fredholm, B. B., M. Jondal, F. Lanefelt, and J. Ng. 1984. Effect of 5′-methylthioadenosine, 3-deazaadenosine, and related compounds on human natural killer cell activity. Scand. J. Immunol. 20:511–518.
   PubMedGoogle Scholar
• Galletti, P., A. Oliva, C. Manna, F. Della Ragione, and M. Carteni-Farina. 1981. Effect of 5′-methylthioadenosine on in vivo methyl esterification of human erythrocyte membrane proteins. FEBS Lett. 126:236–240.
   PubMedGoogle Scholar
• Giri, J. G., P. W. Kincade, and S. B. Mizel. 1984. Interleukin 1-mediated induction of κ light chain synthesis and surface immunoglobulin on pre-B cells. J. Immunol. 132:223–228.
   PubMedGoogle Scholar
• Goldstein, J. L., and M. S. Brown. 1990. Regulation of the mevalonate pathway. Nature (London) 343:425–430.
   PubMed Web of Science ®Google Scholar
• Greenberg, M. E., L. A. Greene, and E. B. Ziff. 1985. Nerve growth factor and epidermal growth factor induce rapid transient changes in proto-oncogene transcription in PC12 cells. J. Biol. Chem. 260:14101–14110.
   PubMed Web of Science ®Google Scholar
• Hagag, N., S. Halegoua, and M. Viola. 1986. Inhibition of growth factor-induced differentiation of PC12 cells by microinjection of antibody to ras p21. Nature (London) 319:680–682.
   PubMed Web of Science ®Google Scholar
• Hammerling, U., A. F. Chin, and J. Abbott. 1976. Ontogeny of murine B lymphocytes: sequence of B-cell differentiation from surface-immunoglobulin-negative precursors to plasma cells. Proc. Natl. Acad. Sci. USA 73:2008–2012.
   PubMedGoogle Scholar
• Hancock, J. F., K. Cadwallader, and C. J. Marshall. 1991. Methylation and proteolysis are essential for efficient membrane binding of prenylated p21K-ras(B). EMBO J. 10:641–646.
   PubMed Web of Science ®Google Scholar
• Hancock, J. F., A. I. Magee, J. E. Childs, and C. J. Marshall. 1989. All ras proteins are polyisoprenylated but only some are palmitoylated. Cell 57:1167–1177.
   PubMed Web of Science ®Google Scholar
• Hrycyna, C. A., and S. Clarke. 1990. Farnesyl cysteine C-terminal methyltransferase activity is dependent upon the STE14 gene product in Saccharomyces cerevisiae. Mol. Cell. Biol. 10:5071–5076.
   PubMedGoogle Scholar
• Jakway, J. P., and A. L. DeFranco. 1986. Pertussis toxin inhibition of B cell and macrophage responses to bacterial lipopolysaccharide. Science 234:743–746.
   PubMedGoogle Scholar
• Kurland, J. L., and R. Bockman. 1978. Activation of macrophage by bacterial lipopolysaccharide. J. Exp. Med. 147:952–957.
   PubMed Web of Science ®Google Scholar
• Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227:680–685.
   PubMed Web of Science ®Google Scholar
• Law, R. E., R. M. Sinibaldi, M. R. Cummings, and A. J. Ferro. 1976. Inhibition of RNA synthesis in salivary glands of Drosophila melanogaster by 5′-methylthioadenosine. Biochem. Biophys. Res. Commun. 73:600–606.
   PubMedGoogle Scholar
• Law, R. E., R. M. Sinibaldi, A. J. Ferro, and M. R. Cummings. 1979. Effect of 5′-methylthioadenosine on gene action during heat shock in Drosophila melanogaster. FEBS Lett. 99:247–250.
   PubMedGoogle Scholar
• Lenardo, M. J., and D. Baltimore. 1989. NF-κB: a pleiotropic mediator of inducible and tissue-specific gene control. Cell 58:227–229.
   PubMed Web of Science ®Google Scholar
• Lenardo, M. J., J. W. Pierce, and D. Baltimore. 1987. Protein binding sites in Ig gene enhancers determine transcriptional activity and inducibility. Science 236:1573–1577.
   PubMed Web of Science ®Google Scholar
• Maher, P. A. 1988. Nerve growth factor induces proteintyrosine phosphorylation. Proc. Natl. Acad. Sci. USA 85:6788–6791.
   PubMed Web of Science ®Google Scholar
• Maltese, W. A. 1990. Posttranslational modifications of proteins by isoprenoids in mammalian cells. FASEB J. 4:3319–3328.
   PubMed Web of Science ®Google Scholar
• Maltese, W. A., and K. M. Sheridan. 1987. Isoprenylated proteins in cultured cells: subcellular distribution and changes related to altered morphology and growth arrest induced by mevalonate deprivation. J. Cell Physiol. 133:471–481.
   PubMedGoogle Scholar
• Max, E. E., J. G. Seidman, and P. Leder. 1979. Sequences of five potential recombination sites encoded close to an immunoglobulin κ constant region gene. Proc. Natl. Acad. Sci. USA 76:3450–3454.
   PubMed Web of Science ®Google Scholar
• Mumby, S. M., P. J. Casey, A. G. Gilman, S. Gutowski, and P. C. Sternweis. 1990. G protein γ subunits contain a 20-carbon isoprenoid. Proc. Natl. Acad. Sci. USA 87:5872–5877.
   Google Scholar
• Paige, C. J., P. W. Kincade, and P. Ralph. 1978. Murine B cell leukemia line with inducible surface immunoglobulin expression. J. Immunol. 121:641–647.
   PubMed Web of Science ®Google Scholar
• Perez-Sala, D., E. W. Tan, F. J. Canada, and R. R. Rando. 1991. Methylation and demethylation reactions of guanine nucleotide- binding proteins of retinal rod outer segments. Proc. Natl. Acad. Sci. USA 88:3043–3046.
   PubMedGoogle Scholar
• Pierce, J. W., M. Lenardo, and D. Baltimore. 1988. Oligonucleotide that binds nuclear factor NF-κB acts as a lymphoidspecific and inducible enhancer element. Proc. Natl. Acad. Sci. USA 85:1482–1486.
   PubMed Web of Science ®Google Scholar
• Prywes, R., and R. G. Roeder. 1986. Inducible binding of a factor to the c-fos enhancer. Cell 47:777–784.
   PubMed Web of Science ®Google Scholar
• Repko, E. M., and W. A. Maltese. 1989. Post-translational isoprenylation of cellular proteins is altered in response to mevalonate availability. J. Biol. Chem. 264:9945–9952.
   PubMedGoogle Scholar
• Rosoff, P. M., L. F. Stein, and L. C. Cantley. 1984. Phorbol esters induce differentiation in a pre-B-lymphocyte cell line by enhancing Na+/H+ exchange. J. Biol. Chem. 259:7059–7060.
   Google Scholar
• Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Molecular cloning: a laboratory manual, 2nd. ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
   Google Scholar
• Schreck, R., P. Rieber, and P. A. Baeuerle. 1991. Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-κB transcription factor and HIV-1. EMBO J. 10:2247–2258.
   PubMed Web of Science ®Google Scholar
• Seeley, P. J., A. Rukenstein, J. L. Connolly, and L. A. Greene. 1984. Differential inhibition of nerve growth factor and epidermal growth factor effects on the PC12 pheochromocytoma line. J. Cell Biol. 98:417–426.
   PubMed Web of Science ®Google Scholar
• Sen, R., and D. Baltimore. 1986. Multiple nuclear factors interact with the immunoglobulin enhancer sequences. Cell 46:705–716.
   PubMed Web of Science ®Google Scholar
• Sen, R., and D. Baltimore. 1986. Inducibility of κ immunoglobulin enhancer-binding protein NF-κB by a posttranslational mechanism. Cell 47:921–928.
   PubMed Web of Science ®Google Scholar
• Sepp-Lorenzino, L., N. Azrolan, and P. S. Coleman. 1989. Cellular distribution of cholesterogenesis-linked, phospho-iso- prenylated proteins in proliferating cells. FEBS Lett. 245:110–116.
   PubMedGoogle Scholar
• Shirakawa, F., M. Chedid, J. Suttles, B. A. Pollok, and S. B. Mizel. 1989. Interleukin-1 and cyclic AMP induce κ immunoglobulin light-chain expression via activation of an NF-κB-like DNA-binding protein. Mol. Cell. Biol. 9:959–964.
   PubMed Web of Science ®Google Scholar
• Sinensky, M., L. A. Beck, S. Leonard, and R. Evans. 1990. Differential inhibitory effects of lovastatin on protein isoprenylation and sterol synthesis. J. Biol. Chem. 265:19937–19941.
   PubMed Web of Science ®Google Scholar
• Sinensky, M., and J. Logel. 1985. Defective macromolecule biosynthesis and cell-cycle progression in a mammalian cell starved for mevalonate. Proc. Natl. Acad. Sci. USA 82:3257–3261.
   PubMed Web of Science ®Google Scholar
• Singh, H., R. Sen, D. Baltimore, and P. A. Sharp. 1986. A nuclear factor that binds to a conserved sequence motif in transcriptional control elements of immunoglobulin genes. Nature (London) 319:154–158.
   PubMed Web of Science ®Google Scholar
• Smith, D. S., C. S. King, E. Pearson, C. K. Gittinger, and G. E. Landreth. 1989. Selective inhibition of nerve growth factor- stimulated protein kinases by K-252a and 5′-S-methyladonosine in PC12 cells. J. Neurochem. 53:800–806.
   PubMedGoogle Scholar
• Staal, F. J. T., M. Roederer, L. A. Herzenberg, and L. A. Herzenberg. 1990. Intracellular thiols regulate activation of nuclear factor κB and transcription of human immunodeficiency virus. Proc. Natl. Acad. Sci. USA 87:9943–9947.
   PubMed Web of Science ®Google Scholar
• Stephenson, R. C., and S. Clarke. 1990. Identification of a C-terminal protein carboxyl methyltransferase in rat liver membranes utilizing a synthetic famesyl cysteine-containing peptide substrate. J. Biol. Chem. 265:16248–16254.
   PubMedGoogle Scholar
• Stimmel, J. B., R. J. Deschenes, C. Volker, J. Stock, and S. Clarke. 1990. Evidence for an S-famesylcysteine methyl ester at the carboxyl terminus of Saccharomyces cerevisiae RAS2 protein. Biochemistry 29:9651–9659.
   PubMedGoogle Scholar
• Stock, J. B., S. Clarke, and D. E. Koshland, Jr. 1984. The protein carboxylmethyltransferase involved in Escherichia coli and Salmonella typhimurium chemotaxis. Methods Enzymol. 106:310–321.
   PubMedGoogle Scholar
• Vandenbark, A. A., A. J. Ferro, and C. L. Barney. 1980. Inhibition of lymphocyte transformation by a naturally occurring metabolite: 5′-methylthioadenosine. Cell. Immunol. 49:26–33.
   PubMedGoogle Scholar
• Wall, R., M. Briskin, C. Carter, H. Govan, A. Taylor, and P. Kincade. 1986. A labile inhibitor blocks immunoglobulin κ-light- chain-gene transcription in a pre-B leukemic cell line. Proc. Natl. Acad. Sci. USA 83:295–298.
   PubMed Web of Science ®Google Scholar
• Williams-Ashman, H. G., J. Seidenfeld, and P. Galletti. 1982. Trends in the biochemical pharmacology of 5′-deoxy-5-meth- ylthioadenosine. Biochem. Pharmacol. 31:277–288.
   PubMed Web of Science ®Google Scholar
• Wolberg, G., T. P. Zimmerman, C. J. Schmitges, G. S. Duncan, and R. D. Deeprose. 1982. Inhibition of lymphocyte cyclic AMP phosphodiesterase and lymphocyte function by 5′-methylthioadenosine. Biochem. Pharmacol. 31:2201–2203.
   PubMedGoogle Scholar
• Yamane, H. K., C. C. Farnsworth, H. Xie, W. Howald, B. K.-K. Fung, S. Clarke, M. H. Gelb, and J. A. Glomset. 1990. Brain G protein γ subunits contain an all-trans-geranylgeranylcysteine methyl ester at their carboxyl termini. Proc. Natl. Acad. Sci. USA 87:5868–5872.
   PubMed Web of Science ®Google Scholar