Skip to main content

Effects of Metals on Gene Expression

  • Chapter

Part of the book series: Handbook of Experimental Pharmacology ((HEP,volume 115))

Abstract

Heavy metals are both ubiquitous and long-lived in the environment (reviewed by GOyer 1991) and have enormously varied effects on cells. They are an absolute requirement for the function of both prokaryotic and eukaryotic cells (17 out of the 30 elements essential for life are metals; COtton and WIlkinson 1980), but are toxic to cells and organs through different pathways and to different degrees (reviewed in several chapters of this volume). Some metals have no known function in cells, but have toxic effects:cadmium and arsenic are examples. Cells have developed mechanisms to keep toxic metal species away from critical targets, and some of those mechanisms will be covered in this review. Others are essential for normal cellular function, but are toxic under certain circumstances and at particular concentrations:metals that fall into this category include copper (an essential cofactor for many oxidative enzymes, including catalase, peroxidase, cytochrome oxides, and others — but also a dangerous cellular toxin; HOrn 1984), cobalt (an essential cofactor for vitamin B12), manganese (a cofactor in many enzymatic reactions involving phosphorylation, cholesterol, and fatty acid synthesis), iron (required for haemoglobin), selenium (essential for glutathione peroxidase; HOGBERG and ALexander 1986), and molybdenum (an essential cofactor for xanthine oxidase and aldehyde oxidase, and required in plants for fixing atmospheric nitrogen by bacteria).

This is a preview of subscription content, log in via an institution.

Buying options

Chapter
USD   29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD   84.99
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD   109.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Learn about institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  • Alam J, Smith A (1992) Heme-hemopexin-mediated induction of metallothionein gene expression. J Biol Chem 267:16379–16384

    PubMed  CAS  Google Scholar 

  • Alam J, Shibahara S, Smith A (1989) Transcriptional activation of the heme oxygenase gene by heme and cadmium in mouse hepatoma cells. J Biol Chem 264:6371–6375

    PubMed  CAS  Google Scholar 

  • Andrews GK (1990) Regulation of metallothionein gene expression. Prog Food Nutr Sci 14:193–258

    PubMed  CAS  Google Scholar 

  • Andrews GK, Gallant KR, Cherian MG (1987) Regulation of the ontogeny of rat liver metallothionein mRNA by zinc. Eur J Biochem 166:527–531

    PubMed  CAS  Google Scholar 

  • Angel P, Imagawa M, Chiu R, Stein B, Imbra RJ, Rahmsdorf HJ, Jonat C, Herrlich P, Karin M (1987) Phorbol ester-inducible genes contain a common cis element recognized by a TPA-modulated transacting factor. Cell 49:729–739

    PubMed  CAS  Google Scholar 

  • Becker PB, Gloss B, Schmid W, Strahle U, Schutz G (1986) In vivo protein-DNA interactions in a glucocorticoid response element require the presence of the hormone. Nature 324:686–688

    PubMed  CAS  Google Scholar 

  • Bianchi F, Rousseaux Prevost R, Sautiere P, Rousseaux J (1992) P2 protamines from human sperm are zinc-finger proteins with one CYS2/H1S2 motif. Biochem Biophys Res Commun 182:540–547

    PubMed  CAS  Google Scholar 

  • Biempica L, Rauch H, Quintana N, Sternlieb I (1988) Morphologic and chemical studies on a murine mutation (toxic milk mice) resulting in hepatic copper toxicosis. Lab Invest 59:500–508

    PubMed  CAS  Google Scholar 

  • Brouwer M, Schlenk D, Ringwood AH, Brouwer Hoexum T (1992) Metal-specific induction of metallothionein isoforms in the blue crab Callinectes sapidus in response to single- and mixed-metal exposure. Arch Biochem Biophys 294:461–468

    PubMed  CAS  Google Scholar 

  • Brown PH, Daniels McQueen S, Waiden WE, Patino MM, Gaffield L, Bielser D, Thach RE (1989) Requirements for the translational repression of ferritin transcripts in wheat germ extracts by a 90-kDa protein from rabbit liver. J Biol Chem 264:13383–13386

    PubMed  CAS  Google Scholar 

  • Carri MT, Galiazzo F, Ciriolo MR, Rotilio G (1991) Evidence for co-regulation of Cu,Zn superoxide dismutase and metallothionein gene expression in yeast through transcriptional control by copper via the ACE 1 factor. FEBS Lett 278:263–266

    PubMed  CAS  Google Scholar 

  • Castro CE (1987) Nutrient effects on DNA and chromatin structure. Annu Rev Nutr 7:407–421

    PubMed  CAS  Google Scholar 

  • Casswall TH, Bjorndahl L, Kvist U (1987) Cadmium interacts with the zinc-dependent stability of the human sperm chromatin. J Trace Elem Electrolytes Health Dis 1:85–87

    PubMed  CAS  Google Scholar 

  • Catelli MG, Binart N, Jung Testas I, Renoir JM, Baulieu EE, Feramisco JR, Welch WJ (1985) The common 90-kd protein component of non-transformed “8S” steroid receptors is a heat-shock protein. EMBO J 4:3131–3135

    PubMed  CAS  Google Scholar 

  • Chambers I, Harrison PR (1987) A new puzzle in seleno-protein biosynthesis:selenocysteine seems to be encoded by a stop codon UGA. Trends Biochem Sci 12:255–256

    CAS  Google Scholar 

  • Chelly J, Turner Z, Tonnesen T, Petterson A, Ishikawa Brush Y, Tommerup N, Horn N, Monaco AP (1993) Isolation of a candidate gene for Menkes disease that encodes a potential heavy metal binding protein (see comments). Nat Genet 3:14–19

    PubMed  CAS  Google Scholar 

  • Chesters JK (1992) Trace element-gene interactions. Nutr Rev 50:217–223

    PubMed  CAS  Google Scholar 

  • Choudhuri S, McKim JM Jr, Klaassen CD (1992) Role of hepatic lysosomes in the degradation of metallothionein. Toxicol Appl Pharmacol 115:64–71

    PubMed  CAS  Google Scholar 

  • Chu E, Voeller D, Koeller DM, Drake JC, Takimoto CH, Maley GF, Maley F, Allegra CJ (1993) Identification of an RNA binding site for human thymidylate synthase. Proc Natl Acad Sci USA 90:517–521

    PubMed  CAS  Google Scholar 

  • Chubatsu LS, Meneghini R (1993) Metallothionein protects DNA from oxidative damage. Biochem J 291:193–198

    PubMed  CAS  Google Scholar 

  • Cotton FA, Wilkinson G (1980) Advanced inorganic chemistry. A comprehensive text. Wiley, New York

    Google Scholar 

  • Cousins RJ, Lee-Ambrose LM (1992) Nuclear zinc uptake and interactions and metallothionein gene expression are influenced by dietary zinc in rats. J Nutr 122:56–64

    PubMed  CAS  Google Scholar 

  • Croston GE, Kadonaga JT (1993) Role of chromatin structure in the regulation of transcription by RNA polymerase II. Curr Opin Cell Biol 5:417–423

    PubMed  CAS  Google Scholar 

  • Culotta VC, Hamer DH (1989) Fine mapping of a mouse metallothionein gene metal response element. Mol Cell Biol 9:1376–1380

    PubMed  CAS  Google Scholar 

  • Danks DM (1989) Disorders of copper transport. In:Scrives C, Beaudet A, Sly W, Valle D (eds) The metabolic basis of inherited disease. McGraw-Hill, New York, pp 1411–1432

    Google Scholar 

  • Danks DM, Mercer JFB (1988) Metallothionein and ceruloplasmin genes. In:Hurley LS, Keen CL, Lunnerdal B, Rucker RB (eds) Trace elements in man and animals, vol 6. Plenum, New York, pp 287–291

    Google Scholar 

  • Darwish HM, Hoke JE, Ettinger MJ (1983) Kinetics of Cu(II) transport and accumulation by hepatocytes from copper-deficient mice and the brindled mouse model of Menkes disease. J Biol Chem 258:13621–13626

    PubMed  CAS  Google Scholar 

  • Denis M, Gustafsson JA (1989) The Mr approximately 90000 heat shock protein:an important modulator of ligand and DNA-binding properties of the glucocorticoid receptor. Cancer Res 49:2275s–2281s

    PubMed  CAS  Google Scholar 

  • Devary Y, Gottlieb RA, Lau LF, Karin M (1991) Rapid and preferential activation of the c-jun gene during the mammalian UV response. Mol Cell Biol 11:2804–2811

    PubMed  CAS  Google Scholar 

  • Dix DJ, Lin PN, Kimata Y, Theil EC (1992) The iron regulatory region of ferritin mRNA is also a positive control element for iron-independent translation. Biochemistry 31:2818–2822

    PubMed  CAS  Google Scholar 

  • Epner DE, Herschman HR (1991) Heavy metals induce expression of the TPA-inducible sequence (TIS) genes. J Cell Physiol 148:68–74

    PubMed  CAS  Google Scholar 

  • Fantl WJ, Johnson DE, Williams LT (1993) Signalling by receptor tyrosine kinases. Annu Rev Biochem 62:453–481

    PubMed  CAS  Google Scholar 

  • Friberg L, Elinder CG, Kjellstrom T (1992) Cadmium. Environmental Health Criteria 134. World Health Organization, Geneva, p 199

    Google Scholar 

  • Frydman M, Bonne Tamir B, Farrer LA, Conneally PM, Magazanik A, Ashbel S, Goldwitch Z (1985) Assignment of the gene for Wilson’s disease to chromosome 13:linkage to the esterase D locus. Proc Natl Acad Sci USA 82:1819–1821

    PubMed  CAS  Google Scholar 

  • Gehring U (1993) The structure of glucocorticoid receptors. J Steroid Biochem Mol Biol 45:183–190

    PubMed  CAS  Google Scholar 

  • Gitlin JD, Schroeder JJ, Lee Ambrose LM, Cousins RJ (1992) Mechanisms of caeruloplasmin biosynthesis in normal and copper-deficient rats. Biochem J 282:835–839

    PubMed  CAS  Google Scholar 

  • Godowski PJ, Rusconi S, Miesfeld R, Yamamoto KR (1987) Glucocorticoid receptor mutants that are constitutive activators of transcriptional enhancement (published erratum appears in Nature (1987) 326:105). Nature 325:365–368

    PubMed  CAS  Google Scholar 

  • Goyer RA (1991) Toxic effects of metals. In:Amdur MO, Doull J, Klaassen CD (eds) Casarett and Doull’s toxicology, 4th edn. Pergamon, New York, pp 652–661

    Google Scholar 

  • Gralla EB, Kosman DJ (1992) Molecular genetics of superoxide dismutases in yeasts and related fungi. Adv Genet 30:251–319

    PubMed  CAS  Google Scholar 

  • Gralla EB, Thiele DJ, Silar P, Valentine JS (1991) ACE1, a copper-dependent transcription factor, activates expression of the yeast copper, zinc superoxide dismutase gene. Proc Natl Acad Sci USA 88:8558–8562

    PubMed  CAS  Google Scholar 

  • Graupner G, Wills KN, Tzukerman M, Zhang XK, Pfahl M (1989) Dual regulatory role for thyroid-hormone receptors allows control of retinoic-acid receptor activity. Nature 340:653–656

    PubMed  CAS  Google Scholar 

  • Greco MA, Hrab DI, Magner W, Kosman DJ (1990) Cu,Zn superoxide dismutase and copper deprivation and toxicity in Saccharomyces cerevisiae. J Bacteriol 172:317–325

    PubMed  CAS  Google Scholar 

  • Gregory EM, Goscin SA, Fridovich I (1974) Superoxide dismutase and oxygen toxicity in a eukaryote. J Bacteriol 117:456–460

    PubMed  CAS  Google Scholar 

  • Guarente L, Mason T (1983) Heme regulates transcription of the CYC1 gene of S. cerevisiae via an upstream activation site. Cell 32:1279–1286

    PubMed  CAS  Google Scholar 

  • Halliwell B, Gutteridge JM (1984) Oxygen toxicity, oxygen radicals, transition metals and disease. Biochem J 219:1–14

    PubMed  CAS  Google Scholar 

  • Halliwell B, Gutteridge JM (1985) The importance of free radicals and catalytic metal ions in human diseases. Mol Aspects Med 8:89–193

    PubMed  CAS  Google Scholar 

  • Hamer DH (1986) Metallothionein. Annu Rev Biochem 55:913–951

    PubMed  CAS  Google Scholar 

  • Hamer DH (1993) “Kinky hair” disease sheds light on copper metabolism. Nat Genet 3:3–4

    PubMed  CAS  Google Scholar 

  • Hara K, Kominami E, Katunuma N (1988) Effects of proteinase inhibitors on intracellular processing of cathepsin B, H and L in rat macrophages. FEBS Lett 231:229–231

    PubMed  CAS  Google Scholar 

  • Harris ED, Stevens MD (1985) Receptors for ceruloplasmin in aortic cell membranes. In:Mills CF, Bremner I, Chester JK (eds) Trace elements in animals and man. Slough, UK, Commonwealth Agricultural Bureau, pp 320–323

    Google Scholar 

  • Hentze MW, Caughman SW, Rouault TA, Barriocanal JG, Dancis A, Harford JB, Klausner RD (1987) Identification of the iron-responsive element for the translational regulation of human ferritin mRNA. Science 238:1570–1573

    PubMed  CAS  Google Scholar 

  • Herd SM, Camakaris J, Christofferson R, Wookey P, Danks DM (1987) Uptake and efflux of copper-64 in Menkes’ disease and normal continuous lymphoid cell lines. Biochem J 247:341–347

    PubMed  CAS  Google Scholar 

  • Hill KL, Li HH, Singer J, Merchant S (1991) Isolation and structural characterization of the Chlamydomonas reinhardtii gene for cytochrome c6. Analysis of the kinetics and metal specificity of its copper-responsive expression. J Biol Chem 266:15060–15067

    PubMed  CAS  Google Scholar 

  • Hogberg J, Alexander J (1986) In:Friberg L, Nordberg GF, Vouk VB (eds) Specific metals, 2nd edn. Elsevier Scientific, Amsterdam, pp 482–512 (Handbook on the toxicology of metals, vol II)

    Google Scholar 

  • Hollenberg SM, Giguere V, Segui P, Evans RM (1987) Colocalization of DNA-binding and transcriptional activation functions in the human glucocorticoid receptor. Cell 49:39–46

    PubMed  CAS  Google Scholar 

  • Horn N (1984) Copper metabolism in Menkes’ disease. In:Rennert OM, Chan W-Y (eds) Metabolism of trace metals in man, vol II. CRC Press, Boca Raton, pp 26–52

    Google Scholar 

  • Hutchison KA, Scherrer LC, Czar MJ, Stancato LF, Chow YH, Jove R, Pratt WB (1993) Regulation of glucocorticoid receptor function through assembly of a receptor-heat shock protein complex. Ann N Y Acad Sci 684:35–48

    PubMed  CAS  Google Scholar 

  • Imbert J, Zafarullah M, Culotta VC, Gedamu L, Hamer D (1989) Transcription factor MBF-1 interacts with metal regulatory elements of higher eucaryotic metallothionein genes. Mol Cell Biol 9:5315–5323

    PubMed  CAS  Google Scholar 

  • Isonishi S, Horn DK, Thiebaut FB, Mann SC, Andrews PA, Basu A, Lazo JS, Eastman A, Howell SB (1991) Expression of the c-Ha-ras oncogene in mouse NIH 3T3 cells induces resistance to cisplatin. Cancer Res 51:5903–5909

    PubMed  CAS  Google Scholar 

  • Ivarie RD, O’Farrell PH (1978) The glucocorticoid domain:steroid-mediated changes in the rate of synthesis of rat hepatoma proteins. Cell 13:41–55

    PubMed  CAS  Google Scholar 

  • Jensen EV, DeSombre ER (1972) Mechanism of action of the female sex hormones. Annu Rev Biochem 41:203–230

    PubMed  CAS  Google Scholar 

  • Jin P, Ringertz NR (1990) Cadmium induces transcription of proto-oncogenes c-jun and c-myc in rat L6 myoblasts. J Biol Chem 265:14061–14064

    PubMed  CAS  Google Scholar 

  • Jin P, Sejersen T, Ringertz NR (1991) Recombinant platelet-derived growth factor-BB stimulates growth and inhibits differentiation of rat L6 myoblasts. J Biol Chem 266:1245–1249

    PubMed  CAS  Google Scholar 

  • Kadonaga JT, Carner KR, Masiarz FR, Tjian R (1987) Isolation of cDNA encoding transcription factor Spl and functional analysis of the DNA binding domain. Cell 51:1079–1090

    PubMed  CAS  Google Scholar 

  • Kagi JH, Schaffer A (1988) Biochemistry of metallothionein. Biochemistry 27:8509–8515

    PubMed  CAS  Google Scholar 

  • Kapur S, Higgins JV, Delp K, Rogers B (1987) Menkes syndrome in a girl with X-autosome translocation. Am J Med Genet 26:503–510

    PubMed  CAS  Google Scholar 

  • Kargacin B, Klein CB, Costa M (1993) Mutagenic responses of nickel oxides and nickel sulfides in Chinese hamster V79 cell lines at the xanthine-guanine phosphoribosyl transferase locus. Mutat Res 300:63–72

    PubMed  CAS  Google Scholar 

  • Karin M (1992) Signal transduction from cell surface to nucleus in development and disease. FASEB J 6:2581–2590

    PubMed  CAS  Google Scholar 

  • Karin M, Slater EP, Herschman HR (1981) Regulation of metallothionein synthesis in HeLa cells by heavy metals and glucocorticoids. J Cell Physiol 106:63–74

    PubMed  CAS  Google Scholar 

  • Kelley SL, Basu A, Teicher BA, Hacker MP, Hamer DH, Lazo JS (1988) Overexpression of metallothionein confers resistance to anticancer drugs. Science 241:1813–1815

    PubMed  CAS  Google Scholar 

  • Kershaw WC, Klaassen CD (1992) Degradation and metal compositon of hepatic isometallothioneins in rats. Toxicol Appl Pharmacol 112:24–31

    PubMed  CAS  Google Scholar 

  • Kjellberg S, Bjorndahl L, Kvist U (1992) Sperm chromatin stability and zinc binding properties in semen from men in barren unions. Int J Androl 15:103–113

    PubMed  CAS  Google Scholar 

  • Klausner RD, Harford JB (1989) cis-trans models for post-transcriptional gene regulation. Science 246:870–872

    PubMed  CAS  Google Scholar 

  • Koizumi S, Suzuki K, Otsuka F (1992a) A nuclear factor that recognizes the metal-responsive elements of human metallothionein IIA gene. J Biol Chem 267:18659–18664

    PubMed  CAS  Google Scholar 

  • Koizumi S, Yamada H, Suzuki K, Otsuka F (1992b) Zinc-specific activation of a HeLa cell nuclear protein which interacts with a metal responsive element of the human metallothionein-IIA gene. Eur J Biochem 210:555–560

    PubMed  CAS  Google Scholar 

  • Kornberg RD, Lorch Y (1992) Chromatin structure and transcription. Annu Rev Cell Biol 8:563–587

    PubMed  CAS  Google Scholar 

  • Koropatnick J, Cherian MG (1993) A mutant mouse (tx) with increased hepatic metallothionein stability and accumulation. Biochem J 296:443–449

    PubMed  CAS  Google Scholar 

  • Koropatnick J, Pearson J (1990) Zinc treatment, metallothionein expression, and resistance to cisplatin in mouse melanoma cells. Somat Cell Mol Genet 16:529–537

    PubMed  CAS  Google Scholar 

  • Koropatnick J, Pearson J (1993) Altered cisplatin and cadmium resistance and cell survival in Chinese hamster ovary cells expressing mouse metallothionein. Mol Pharmacol 44:44–50

    PubMed  CAS  Google Scholar 

  • Kortenkamp A, Curran B, O’Brien P (1992) Defining conditions for the efficient in vitro cross-linking of proteins to DNA by chromium(III) compounds. Carcinogenesis 13:307–308

    PubMed  CAS  Google Scholar 

  • Kuivaniemi H, Peltonen L, Palotie A, Kaitila I, Kivirikko K (1981) Abnormal copper metabolism and deficient lysyl oxidase activity in a heritable connective tissue disorder. J Clin Invest 69:730–733

    Google Scholar 

  • Labbe S, Prevost J, Remondelli P, Leone A, Seguin C (1991) A nuclear factor binds to the metal regulatory elements of the mouse gene encoding metallothionein-1. Nucleic Acids Res 19:4225–4231

    PubMed  CAS  Google Scholar 

  • Lad PM, Kaptein JS, Lin CK, Kalunta CI, Scott SJ, Gu DG (1992) G-proteins and the role of second messengers in the regulation of the human neutrophil. Immunol Ser 57:107–136

    PubMed  CAS  Google Scholar 

  • Lamb TD, Pugh ENJ (1992) G-protein cascades:gain and kinetics. Trends Neurosci 15:291–298

    PubMed  CAS  Google Scholar 

  • Larson JS, Schuetz TJ, Kingston RE (1988) Activation in vitro of sequence-specific DNA binding by a human regulatory factor. Nature 335:372–375

    PubMed  CAS  Google Scholar 

  • Lathrop JT, Timko MP (1993) Regulation by heme of mitochondrial protein transport through a conserved amino acid motif. Science 259:522–525

    PubMed  CAS  Google Scholar 

  • Laurin DE, Barnes DM, Klasing KC (1990) Rates of metallothionein synthesis, degradation and accretion in a chicken macrophage cell line. Proc Soc Exp Biol Med 194:157–164

    PubMed  CAS  Google Scholar 

  • Laybourn PJ, Kadonaga JT (1991) Role of nucleosomal cores and histone H1 in regulation of transcription by RNA polymerase II. Science 254:238–245

    PubMed  CAS  Google Scholar 

  • Leibbrandt MEI, Koropatnick J (1994) Activation of human monocytes with lipopolysaccharide induces metallothionein expression and is diminished by zinc. Toxicol Appl Pharmacol 124:72–81

    PubMed  CAS  Google Scholar 

  • Leibold EA, Laudano A, Yu Y (1990) Structural requirements of iron-responsive elements for binding of the protein involved in both transferrin receptor and ferritin mRNA post-transcriptional regulation. Nucleic Acids Res 18:1819–1824

    PubMed  CAS  Google Scholar 

  • Leibbrandt MEI,Khokha R, Koropatnick J (1994) Antisense down-regulation of metallothionein in a human monocytic cell line alters adherence, invasion and the respiratory burst. Cell Growth Diff 5:17–25

    PubMed  CAS  Google Scholar 

  • Lescure AM, Proudhon D, Pesey H, Ragland M, Theil EC, Briat JF (1991) Ferritin gene transcription is regulated by iron in soybean cell cultures. Proc Natl Acad Sci USA 88:8222–8226

    PubMed  CAS  Google Scholar 

  • Lewis CD, Laemmli UK (1982) Higher order metaphase chromosome structure:evidence for metalloprotein interactions. Cell 29:171–181

    PubMed  CAS  Google Scholar 

  • Li NQ, Reddy PS, Thyagaraju K, Reddy AP, Hsu BL, Scholz RW, Tu CP, Reddy CC (1990) Elevation of rat liver mRNA for selenium-dependent glutathione peroxidase by selenium deficiency. J Biol Chem 265:108–113

    PubMed  CAS  Google Scholar 

  • McArdle HJ, Mercer JF, Sargeson AM, Danks DM (1990) Effects of cellular copper content on copper uptake and metallothionein and ceruloplasmin mRNA levels in mouse hepatocytes. J Nutr 120:1370–1375

    PubMed  CAS  Google Scholar 

  • McKim JM Jr, Choudhuri S, Klaassen CD (1992) In vitro degradation of apo-, zinc-, and cadmium-metallothionein by cathepsins B, C, and D. Toxicol Appl Pharmacol 116:117–124

    PubMed  CAS  Google Scholar 

  • Mercer JF, Livingston J, Hall B, Paynter JA, Begy C, Chandrasekharappa S, Lockhart P, Grimes A, Bhave M, Siemieniak D et al (1993) Isolation of a partial candidate gene for Menkes disease by positional cloning (see comments). Nat Genet 3:20–25

    PubMed  CAS  Google Scholar 

  • Merchant S, Bogorad L (1987) The Cu(II)-repressible plastidic cytochrome c. Cloning and sequence of a complementary DNA for the pre-apoprotein. J Biol Chem 262:9062–9067

    PubMed  CAS  Google Scholar 

  • Merchant S, Hill K, Howe G (1991) Dynamic interplay between two copper-titrating components in the transcriptional regulation of cyt c6 (published erratum appears in EMBO J (1991) 10:23201). EMBO J 10:1383–1389

    PubMed  CAS  Google Scholar 

  • Miller J, McLachlan AD, Klug A (1985) Repetitive zinc-binding domains in the protein transcription factor IIIA from Xenopus oocytes. EMBO J 4:1609–1614

    PubMed  CAS  Google Scholar 

  • Min KS, Nakatsubo T, Fujita Y, Onosaka S, Tanaka K (1992) Degradation of cadmium metallothionein in vitro by lysosomal proteases. Toxicol Appl Pharmacol 113:299–305

    PubMed  CAS  Google Scholar 

  • Muller M, Renkawitz R (1991) The glucocorticoid receptor. Biochim Biophys Acta 1088:171–182

    PubMed  CAS  Google Scholar 

  • Nartey NO, Banerjee D, Cherian MG (1987) Immunohistochemical localization of metallothionein in cell nucleus and cytoplasm of fetal human liver and kidney and its changes during development. Pathology 19:233–238

    PubMed  CAS  Google Scholar 

  • O’Halloran TV (1989) In:Sigel H (ed) Metal ions in biological systems, vol 25. Dekker, New York, p 105

    Google Scholar 

  • O’Halloran TV (1993) Transition metals in control of gene expression (see comments). Science 261:715–725

    PubMed  Google Scholar 

  • Oppenheimer JH, Koerner D, Schwartz HL, Surks MI (1972) Specific nuclear triiodothyronine binding sites in rat liver and kidney. J Clin Endocrinol Metab 35:330–333

    PubMed  CAS  Google Scholar 

  • Pabo CO, Sauer RT (1992) Transcription factors:structural families and principles of DNA recognition. Annu Rev Biochem 61:1053–1095

    PubMed  CAS  Google Scholar 

  • Packman S, O’Toole T (1984) Trace metal metabolism in cultured skin fibroblasts of the mottled mouse:response to metallothionein inducers. Pediatr Res 18:1282–1286

    PubMed  CAS  Google Scholar 

  • Packman S, O’Toole C, Price DC, Thaler MM (1983) Cadmium, zinc, and copper metabolism in the mottled mouse, an animal model for Menkes’ kinky hair syndrome. J Inorg Biochem 19:203–211

    PubMed  CAS  Google Scholar 

  • Packman S, Sample S, Whitney W (1987) Defective intracellular copper translocation in Menkes’ kinky hair syndrome. Pediatr Res [Suppl]21:293s

    Google Scholar 

  • Panemangalore M, Banerjee D, Onosaka S, Cherian MG (1983) Changes in the intracellular accumulation and distribution of metallothionein in rat liver and kidney during postnatal development. Dev Biol 97:95–102

    PubMed  CAS  Google Scholar 

  • Pfeifer K, Arcangioli B, Guarente L (1987a) Yeast HAP1 activator competes with the factor RC2 for binding to the upstream activator site UAS1 of the CYC1 gene. Cell 49:9–18

    CAS  Google Scholar 

  • Pfeifer K, Prezant T, Guarente L (1987b) Yeast HAP1 activator binds to two upstream activation sites of different sequence. Cell 49:19–27

    CAS  Google Scholar 

  • Pfeifer K, Kim KS, Kogan S, Guarente L (1989) Functional dissection and sequence of yeast HAP1 activator. Cell 56:291–301

    PubMed  CAS  Google Scholar 

  • Pfister C, Bennett N, Bruckert F, Catty P, Clerc A, Pages F, Deterre P (1993) Interactions of a G-protein with its effector:transducin and cGMP phosphodiesterase in retinal rods. Cell Signal 5:235–241

    PubMed  CAS  Google Scholar 

  • Pick E, Keisari Y (1980) A simple colorimetric method for the measurement of hydrogen peroxide produced by cells in culture. J Immunol Methods 38:161–170

    PubMed  CAS  Google Scholar 

  • Ralston DM, O’Halloran TV (1990) Metalloregulatory proteins and molecular mechanisms of heavy metal signal transduction. Adv Inorg Biochem 8:1–31

    PubMed  CAS  Google Scholar 

  • Rauch H (1983) Toxic milk, a new mutation affecting copper metabolism in the mouse. J Hered 74:141–144

    PubMed  CAS  Google Scholar 

  • Rauch H, Dupuy D, Stockert RJ, Sternlieb (1986) Hepatic copper and superoxide dismutase activity in toxic milk mutant mice. In:Rotilio G (ed) Superoxide and superoxide dismutase in chemistry, biology and medicine. Elsevier, New York, pp 304–306

    Google Scholar 

  • Rouault TA, Hentze MW, Caughman SW, Harford JB, Klausner RD (1988) Binding of a cytosolic protein to the iron-responsive element of human ferritin messenger RNA. Science 241:1207–1210

    PubMed  CAS  Google Scholar 

  • Rowley DA, Halliwell B (1983) Superoxide-dependent and ascorbate-dependent formation of hydroxyl radicals in the presence of copper salts:a physiologically significant reaction? Arch Biochem Biophys 225:279–284

    PubMed  CAS  Google Scholar 

  • Saedi MS, Smith CG, Frampton J, Chambers I, Harrison PR, Sunde RA (1988) Effect of selenium status on mRNA levels for glutathione peroxidase in rat liver. Biochem Biophys Res Commun 153:855–861

    PubMed  CAS  Google Scholar 

  • Salnikow K, Zhitkovich A, Costa M (1992) Analysis of the binding sites of chromium to DNA and protein in vitro and in intact cells. Carcinogenesis 13:2341–2346

    PubMed  CAS  Google Scholar 

  • Sanchez ER, Toft DO, Schlesinger MJ, Pratt WB (1985) Evidence that the 90-kDa phosphoprotein associated with the untransformed L-cell glucocorticoid receptor is a murine heat shock protein. J Biol Chem 260:12398–12401

    PubMed  CAS  Google Scholar 

  • Sato M, Bremner I (1993) Oxygen free radicals and metallothionein. Free Radie Biol Med 14:325–337

    CAS  Google Scholar 

  • Sauk JJ, Norris K, Kerr JM, Somerman MJ, Young MF (1991) Diverse forms of stress result in changes in cellular levels of osteonectin/SPARC without altering mRNA levels in osteoligament cells. Calcif Tissue Int 49:58–62

    PubMed  CAS  Google Scholar 

  • Schauer M, Chalepakis G, Willmann T, Beato M (1989) Binding of hormone accelerates the kinetics of glucocorticoid and progesterone receptor binding to DNA. Proc Natl Acad Sci USA 86:1123–1127

    PubMed  CAS  Google Scholar 

  • Schilder RJ, Hall L, Monks A, Handel LM, Fornace AJ Jr, Ozols RF, Fojo AT, Hamilton TC (1990) Metallothionein gene expression and resistance to cisplatin in human ovarian cancer. Int J Cancer 45:416–422

    PubMed  CAS  Google Scholar 

  • Searle PF (1990) Zinc dependent binding of a liver nuclear factor to metal response element MRE-a of the mouse metallothionein-1 gene and variant sequences. Nucleic Acids Res 18:4683–4690

    PubMed  CAS  Google Scholar 

  • Searle PF, Stuart GW, Palmiter RD (1987) Metal regulatory elements of the mouse metallothionein-1 gene. In:Metallothionein II. Birkhauser, Basel, pp 407–414 (Experientia supplementum 52)

    Google Scholar 

  • Seguin C (1991) A nuclear factor requires Zn2+ to bind a regulatory MRE element of the mouse gene encoding metallothionein-1. Gene 97:295–300

    PubMed  CAS  Google Scholar 

  • Séguin C, Felber BK, Carter AD, Hamer DH (1984) Competition for cellular factors that activate metallothionein gene transcription. Nature 312:781–785

    PubMed  Google Scholar 

  • Sloane BF, Moin K, Krepela E, Rozhin J (1990) Cathepsin B and its endogenous inhibitors:the role in tumor malignancy. Cancer Metastasis Rev 9:333–352

    PubMed  CAS  Google Scholar 

  • Snow ET (1992) Metal carcinogenesis:mechanistic implications. Pharmacol Ther 53:31–65

    PubMed  CAS  Google Scholar 

  • Srivastava G, Borthwick IA, Maguire DJ, Elferink CJ, Bawden MJ, Mercer JF, May BK (1988) Regulation of 5-aminolevulinate synthase mRNA in different rat tissues. J Biol Chem 263:5202–5209

    PubMed  CAS  Google Scholar 

  • Sunde RA (1990) Molecular biology of selenoproteins. Annu Rev Nutr 10:451–474

    PubMed  CAS  Google Scholar 

  • Suttle NF (1986) Copper deficiency in ruminants; recent developments. Vet Rec 119:519–522

    PubMed  CAS  Google Scholar 

  • Suzuki CA, Ohta H, Albores A, Koropatnick J, Cherian MG (1990) Induction of metallothionein synthesis by zinc in cadmium pretreated rats. Toxicology 63:273–284

    PubMed  CAS  Google Scholar 

  • Tamai KT, Gralla EB, Ellerby LM, Valentine JS, Thiele DJ (1993) Yeast and mammalian metallothioneins functionally substitute for yeast copper-zinc superoxide dismutase. Proc Natl Acad Sci USA 90:8013–8017

    PubMed  CAS  Google Scholar 

  • Thiele DJ (1992) Metal-regulated transcription in eukaryotes. Nucleic Acids Res 20:1183–1191

    PubMed  CAS  Google Scholar 

  • Toyoda H, Himeno S, Imura N (1989) The regulation of glutathione peroxidase gene expression; implications for species differences and the effect of dietary selenium manipulation. In:Wendel A (ed) Selenium in biology and medicine. Springer, Berlin Heidelberg New York, pp 3–7

    Google Scholar 

  • Trueblood CE, Wright RM, Poyton RO (1988) Differential regulation of the two genes encoding Saccharomyces cerevisiae cytochrome c oxidase subunit V by heme and the HAP2 and REOl genes. Mol Cell Biol 8:4537–4540

    PubMed  CAS  Google Scholar 

  • Vallee BL, Falchuk FH (1993) The biochemical basis of zinc physiology. Physiol Rev 73:79–118

    PubMed  CAS  Google Scholar 

  • Vulpe C, Levinson B, Whitney S, Packman S, Gitschier J (1993) Isolation of a candidate gene for Menkes disease and evidence that it encodes a copper-transporting ATPase. Nat Genet 3:7–13

    PubMed  CAS  Google Scholar 

  • Walden WE, Daniels McQueen S, Brown PH, Gaffield L, Russell DA, Bielser D, Bailey LD, Thach RE (1988) Translational repression in eukaryotes:partial purification and characterization of a repressor of ferritin mRNA translation. Proc Natl Acad Sci USA 85:9503–9507

    PubMed  CAS  Google Scholar 

  • Wan M, Hunziker PE, Kagi JH (1993) Induction of metallothionein synthesis by cadmium and zinc in cultured rabbit kidney cells (RK-13). Biochem J 292:609–615

    PubMed  CAS  Google Scholar 

  • Westin G, Schaffner W (1988) Heavy metal ions in transcription factors from HeLa cells:Sp1, but not octamer transcription factor requires zinc for DNA binding and for activator function. Nucleic Acids Res 16:5771–5781

    PubMed  CAS  Google Scholar 

  • White K, Munro HN (1988) Induction of ferritin subunit synthesis by iron is regulated at both the transcriptional and translational levels. J Biol Chem 263:8938–8942

    PubMed  CAS  Google Scholar 

  • Williams GT, Morimoto RI (1990) Maximal stress-induced transcription from the human HSP70 promoter requires interactions with the basal promoter elements independent of rotational alignment. Mol Cell Biol 10:3125–3136

    PubMed  CAS  Google Scholar 

  • Willmann T, Beato M (1986) Steroid-free glucocorticoid receptor binds specifically to mouse mammary tumour virus DNA. Nature 324:688–691

    PubMed  CAS  Google Scholar 

  • Winkler H, Adam G, Mattes E, Schanz M, Hartig A, Ruis H (1988) Co-ordinate control of synthesis of mitochondrial and non-mitochondrial hemoproteins:a binding site for the HAP-1 (CYP1) protein in the UAS region of the yeast catalase T gene. EMBO J 7:1799–1804

    PubMed  CAS  Google Scholar 

  • Yiangou M, Ge X, Carter KD, Papaconstantinou J (1991) Induction of several acute-phase protein genes by heavy metals:a new class of metal-responsive genes. Biochemistry 30:3798–3806

    PubMed  CAS  Google Scholar 

  • Yoshida T, Biro P, Cohen T, Muller RM, Shibahara S (1988) Human heme oxygenase cDNA and induction of its mRNA by hemin. Eur J Biochem 171:457–461

    PubMed  CAS  Google Scholar 

  • Zeng J, Heuchel R, Schaffner W, Kagi JH (1991a) Thionein (apometallothionein) can modulate DNA binding and transcription activation by zinc finger containing factor Sp1. FEBS Lett 279:310–312

    PubMed  CAS  Google Scholar 

  • Zeng J, Vallee BL, Kagi JH (1991b) Zinc transfer from transcription factor IIIA fingers to thionein clusters. Proc Natl Acad Sci USA 88:9984–9988

    PubMed  CAS  Google Scholar 

  • Zhou P, Thiele DJ (1993) Copper and gene regulation in yeast. Biofactors 4:105–115

    PubMed  CAS  Google Scholar 

  • Zhou P, Szczypka MS, Sosinowski T, Thiele DJ (1992) Expression of a yeast metallothionein gene family is activated by a single metalloregulatory transcription factor. Mol Cell Biol 12:3766–3775

    PubMed  CAS  Google Scholar 

  • Zimarino V, Wilson S, Wu C (1990) Antibody-mediated activation of Drosophila heat shock factor in vitro. Science 249:546–549

    PubMed  CAS  Google Scholar 

  • Zitomer RS, Seller JW, McCarter DW, Hastings GA, Wick P, Lowry CV (1987) Elements involved in oxygen regulation of the Saccharomyces cerevisiae CYC7 gene. Mol Cell Biol 7:2212–2220

    PubMed  CAS  Google Scholar 

Download references

Authors

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 1995 Springer-Verlag Berlin Heidelberg

About this chapter

Cite this chapter

Koropatnick, J., Leibbrandt, M.E.I. (1995). Effects of Metals on Gene Expression. In: Goyer, R.A., Cherian, M.G. (eds) Toxicology of Metals. Handbook of Experimental Pharmacology, vol 115. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-79162-8_5

Download citation

  • DOI: https://doi.org/10.1007/978-3-642-79162-8_5

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-79164-2

  • Online ISBN: 978-3-642-79162-8

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics