Mitogenic Actions of Peroxisome Proliferators: Involvement of Protein Kinase C and Tumor Necrosis Factor α

References

• Hawkins J. M., Jones W. E., Bonner F. W., Gibson G. G. The effect of peroxisome proliferators on microsomal, peroxisomal, and mitochondrial enzyme activities in the liver and kidney. Drug Metab. Dispos. 1987; 18: 441–515
   Web of Science ®Google Scholar
• Reddy J. K., Lalwani N. D. ldquo;Carcinogenesis by hepatic peroxisome proliferators: Evaluation of the risk of hypolipidemic drugs and industrial plastciizers to humans”. Crit. Rev. Toxicol. 1983; 12: 1–58
   PubMed Web of Science ®Google Scholar
• Eacho P. I., Lanier T. L., Brodhecker C. A. Hepatocellular DNA synthesis in rats given peroxisome proliferating agents: Comparison of WY-14,643 to clofibric acid, nafenopin and LY171883. Carcinogenesis 1991; 12: 1557–1561
   PubMed Web of Science ®Google Scholar
• Marsman D. S., Cattley R. C., Conway J. G., Popp J. A. Relationship of hepatic peroxisome proliferation and replicative DNA synthesis to the hepatocarcinogenicity of the peroxisome proliferators di(2-ethylhexyl)phthalate and [4-chloro-6-(2,3-xylidino)-2-pyrimidinylthio]acetic acid (WY-14,643) in rats. Cancer Res. 1988; 48: 6739–6744
   PubMed Web of Science ®Google Scholar
• Reddy J. K., Roa M. S. ldquo;Oxidative DNA damage caused by persistent peroxisome proliferation: Its role in hepatocarcinogenesis”. Mutat. Res. 1989; 214: 63–68
   PubMed Web of Science ®Google Scholar
• Mannaerts G. P., Van Velhoven P., Van Broekhoven A., Vandebroek G., Debeer L. J. ldquo;Evidence that peroxisomal acyl-CoA synthetase is located at the cytoplasmic side of the peroxisomal membrane”. Biochem. J. 1982; 20: 17–23
   Google Scholar
• Conway J. G., Tomaszewski K. E., Olsen M. J., Cattely R. C., Marsman D. S., Popp J. A. Relationship of oxidative damage to the hepatocarcinogenicity of the peroxisome proliferators di(2-ethylhexyl)phthalate and [4-chloro-6-(2,3-xylidino)-2-pyrimidinylthio]acetic acid (WY-14,643). Carcinogenesis 1989; 10: 513–519
   PubMed Web of Science ®Google Scholar
• Kasai H., Okada Y., Nishimura S., Roa M. S., Reddy J. K. Formation of 8-hydroxydeoxyguanosine in liver DNA of rats following long-term exposure to a peroxisome proliferator. Cancer Res. 1989; 49: 2603–2605
   PubMed Web of Science ®Google Scholar
• Takagi A., Sai K., Umemura T., Hasegawa R., Kurokawa Y. Production of 8-hydroxydeoxyguanosine in rodent liver by the administration of peroxisome proliferators. Peroxisomes: Biology and Importance in Toxicology and Medicine, G. Gordon, B. Lake. Taylor and Francis, London 1983
   Google Scholar
• Lake B. G. ldquo;Mechanisms of hepatocarcinogenicity of peroxisome-proliferating drugs and cheimcals”. Annu. Rev. Pharmacol. Toxicol. 1995; 35: 483–507
   PubMed Web of Science ®Google Scholar
• Nicholls P., Schonbaum G. R. Catalases, P. D. Boyer. Academic Press, New York 1963; 147–225
   Google Scholar
• Handler J. A., Seed C. B., Bradford B. U., Thurman R. G. Induction of peroxisomes by treatment with perfluorooctanoate does not increase rates of H2O2 production in intact liver. Toxicol. Lett. 1992; 60: 61–68
   PubMed Web of Science ®Google Scholar
• Handler J. A., Thurman R. G. Catalase-dependent ethanol oxidation in perfused rat liver. Requirement for fatty-acid-stimulated H2O2 production by peroxisomes. Eur. J. Biochem. 1988; 172: 477–481
   PubMedGoogle Scholar
• Foerster F.-C., Fahrenkemper T., Rabe U., Graf P., Sies H. Peroxisomal fatty acid oxidation as detected by H2O2 production in intact perfused rat liver. Biochem. J. 1981; 196: 705–712
   PubMed Web of Science ®Google Scholar
• Kornburst D. J., Barfknecht T. R., Ingram P., Shelburne J. D. ldquo;Effect of di(2-ethylhexyl)phthalate on DNA repair and lipid peroxidation in rat hepatocytes and on metabolic cooperation in Chinese hamster V-79 cells”. J. Toxicol. Environ. Health 1984; 13: 99–116
   PubMed Web of Science ®Google Scholar
• Barrass N. C., Price R. J., Lake B. G., Orton T. C. ldquo;Comparison of the acute and chronic mitogenic effects of the peroxisome proliferators methylclofenapate and clofibric acid in rat liver”. Carcinogenesis 1993; 14: 1451–1456
   PubMed Web of Science ®Google Scholar
• Price R. J., Evans J. G., Lake B. G. ldquo;Comparison of the effects of nafenopin on hepatic peroxisome proliferation and replicative DNA synthesis in the rat and Syrian hamster”. Food Chem. Toxicol. 1992; 30: 937–944
   PubMed Web of Science ®Google Scholar
• Cattley R. C., Marsman D. S., Popp J. A. Age-related susceptibility to the carcinogenic effect of the peroxisome proliferator WY-14,643 in rat liver. Carcinogenesis 1991; 12: 469–473
   PubMed Web of Science ®Google Scholar
• Kraupp-Grasl B., Huber W., Taper H., Schulte-Hermann R. ldquo;Increased susceptibility of aged rats to hepatocarcinogenesis by the peroxisome proliferator nafenopin and the possible involvement of altered liver foci occurring spontaneously”. Cancer Res. 1991; 51: 666–671
   PubMed Web of Science ®Google Scholar
• Marsman D. S., Popp J. A. Biological potential of basophilic hepatocellular foci and hepatic adenoma induced by the peroxisome proliferator, WY-14,643. Carcinogenesis 1994; 15: 111–117
   PubMed Web of Science ®Google Scholar
• Keller B. J., Yamanaka H., Liang D., Kauffman F. C., Thurman R. G. ldquo;Oxygen-dependent hepatotoxicity to ethylhexanol in the perfused rat liver: Mitochondria as a site of action”. J. Pharmacol. Exp. Ther 1990; 252: 1355–1360
   PubMed Web of Science ®Google Scholar
• Keller B. J., Marsman D. S., Popp J. A., Thurman R. G. ldquo;Several nongenotoxic carcinogens uncouple mitochondrial oxidative phosphorylation”. Biochim. Biophys. Acta 1992; 1102: 237–244
   PubMed Web of Science ®Google Scholar
• Keller B. J., Bradford B. U., Marsman D. S., Cattley R. C., Popp J. A., Bojes H. K., Thurman R. G. The nongenotoxic hepatocarcinogen WY-14,643 is an uncoupler of oxidative phosphorylation in vivo. Toxicol. Appl. Pharmacol. 1993; 119: 52–58
   PubMed Web of Science ®Google Scholar
• Jewell S. A., Bellomo G., Hjordis T., Orrenius S., Smith M. T. ldquo;Bleb formation in hepatocytes during drug metabolism caused by disturbance in thiol and calcium ion homeostasis”. Science 1982; 217: 1257–1259
   PubMed Web of Science ®Google Scholar
• Bojes H. K., Sausen P. J., Cattley R. C., Keller B. J., Thurman R. G. Paradoxical increase in peroxisomal cyanide-insensitive respiration following dietary exposure to WY-14,634 in the perfused liver. Toxicol. Appl. Pharmacol. 1996; 137: 202–209
   PubMed Web of Science ®Google Scholar
• Thurman R. G., Scholz R. ldquo;Mixed function oxidation in perfused rat liver. The effect of aminopyrine on oxygen uptake”. Eur. J. Biochem. 1969; 10: 459–467
   PubMedGoogle Scholar
• Nishizuka Y. ldquo;The role of protein kinase C in cell surface signal transduction and tumor promotion”. Nature 1984; 308: 693–698
   PubMed Web of Science ®Google Scholar
• Nishizuka Y. ldquo;The molecular heterogeneity of protein kinase C and its implications for cellular regulation”. Nature 1988; 334: 661–665
   PubMed Web of Science ®Google Scholar
• Bojes H. K., Thurman R. G. ldquo;Peroxisomal proliferators inhibit acyl CoA synthetase and stimulate protein kinase C in vivo”. Toxicol. Appl. Pharmacol. 1994; 126: 233–239
   PubMed Web of Science ®Google Scholar
• Bronfman M., Orellana A., Morales M. N., Bieri F., Waechter F., Staubli W., Bentley P. ldquo;Potentiation of diacylglycerol-activated protein kinase C by acyl-coenzyme A thioesters of hypolipidaemic drugs”. Biochem. Biophys. Res. Commun. 1989; 159: 1026–1031
   PubMed Web of Science ®Google Scholar
• Mc Phail L. C., Clayton C. C., Snyderman R. A potential second messenger role for unsaturated fatty acids: Activation of Ca+2-dependent protein kinase. Science 1984; 224: 622–624
   PubMed Web of Science ®Google Scholar
• Mitchell F. E., Price S. C., Hinton R. C., Grasso P., Bridges J. W. ldquo;Time and dose-response study of the effects on the rates of the plasticizer di(2-ethylhexyl)phthalate”. Toxol. Appl. Pharmacol. 1985; 81: 371–392
   PubMed Web of Science ®Google Scholar
• Price S. C., Hinton R. H., Mitchell F. E., Hall D. E., Grasso P., Blane G. F., Brigdes J. W. ldquo;Time and dose study on the response on rats to the hypolipidaemic drug fenofibrate”. Toxicology 1986; 41: 169–191
   PubMed Web of Science ®Google Scholar
• Foxworthy P. S., Perry D. N., Hoover D. M., Eacho P. I. ldquo;Changes in hepatic lipid metabolism associated with lipid accumulation and its reversal in rats given peroxisome proliferator LY171883”. Toxicol. Appl, Pharmacol. 1990; 106: 375–383
   PubMed Web of Science ®Google Scholar
• George M. E., Andersen M. E. Toxic effects of nonadecafluoro-n-decanoic acid in rats. Toxicol. Appl. Pharmacol. 1986; 85: 169–180
   PubMed Web of Science ®Google Scholar
• Krisans S. K., Mortensen R. M., Lazarow P. B. ldquo;Acyl-CoA synthetase in rat liver peroxisomes”. J. Biol. Chem. 1980; 255: 9599–9607
   PubMed Web of Science ®Google Scholar
• Bojes H. K., Thurman R. G. Potent peroxisome proliferators inhibit β-oxidation in the isolated perfused rat liver. Toxicol. Appl. Pharmacol 1996, in press
   Web of Science ®Google Scholar
• Baldwin J. R., Witiak D. T., Feller D. R. ldquo;Disposition of clofibrate in rat. Acute and chronic adminstration”. Biochem. Pharmacol. 1980; 29: 3143–3154
   PubMed Web of Science ®Google Scholar
• Okerholm R. A., Keeley F. J., Peterson F. E., Glazko A. J. ldquo;The metabolism of gemfibrozil”. Proc. Roy. Soc. Lond. 1976; 69: 11–14
   Google Scholar
• Issemann I., Green S. ldquo;Activation of a member of the steroid hormone receptor superfamily by peroxisome proliferators”. Nature 1990; 347: 645–650
   PubMed Web of Science ®Google Scholar
• Gottlicher M., Wildmark E., Qiao L., Gustafsson J. ldquo;Fatty acids activate a chimera of the clofibric acid-activated receptor and the glucocorticoid receptor”. Proc. Natl. Acad. Sci. USA 1992; 89: 4653–4657
   PubMed Web of Science ®Google Scholar
• Greenberg M. E., Greene L. A., Zeff E. B. ldquo;Never growth factor and epidermal growth factor induce rapid transient changes in proto-oncogene transcription in PC 12 cells”. J. Biol. Chem. 1985; 260: 14101–14110
   PubMed Web of Science ®Google Scholar
• Greenberg M. E., Ziff E. B. Stimulation of 3T3 cells induces transcription of the c-fos proto-oncogene. Nature 1984; 311: 433–438
   PubMed Web of Science ®Google Scholar
• Hansen L. A., Monteiro-Riviere N. A., Smart R. C. Differential down-regulation of epidermal protein kinase C by 12-O-tetra-decanoylphorbol-13-acetate and diacylglycerol: Association with epidermal hyperplasia and tumor promotion. Cancer Res. 1990; 50: 5740–5745
   PubMed Web of Science ®Google Scholar
• Sher T., Yi H. F., Mc Bride O. W., Gonzalez F. J. cDNA cloning, chromosomal mapping, and functional characterization of the human peroxisome proliferator activated receptor. Biochemistry 1993; 32: 98–5604
   Google Scholar
• Aldridge T. C., Tugwood J. D., Green S. ldquo;Identification and chacracterization of DNA elements implicated in the regulation of CYP4A 1 transcription”. Biochem. J. 1995; 306: 473–479
   PubMed Web of Science ®Google Scholar
• Wan Y.-J. Y., Morimoto M., Thurman R. G., Bojes H. K., French S. ldquo;Expression of the peroxisome proliferator-activated receptor gene is decreased in experimental alcoholic liver disease”. Life Sci. 1994; 56: 307–317
   Web of Science ®Google Scholar
• Lee S. S., Pineau T., Drago J., Lee E. J., Owens J W, Kroetz D. L., Fernandez-Salguero P. M. Targeted disruption of the alpha isoform of the peroxisome proliferator-activated receptor gene in mice results in abolishment of the pleiotropic effects of peroxisome prolifeators. Mol. Cell Biol. 1995; 15: 3012–3022
   PubMed Web of Science ®Google Scholar
• Marsman D. S., Swanson-Pfeiffer C. L., Popp J. A. Lack of comitogenicity by the peroxisome proliferator hepatocarcinogens, WY-14,643 and clofibric acid. Toxicol. Appl. Pharmacol. 1993; 122: 1–6
   PubMed Web of Science ®Google Scholar
• Beyer H. S., Theologides A. ldquo;Tumor necrosis factor-α is a direct hepatocyte mitogen in the rat”. Bichem. Mol. Biol. Int. 1993; 29: 1–4
   PubMedGoogle Scholar
• Birmelin M., Decker K. Ca+2 flux as an initial event in phagocytosis by rat Kupffer cells. Eur. J. Biochem. 1983; 131: 539–543
   PubMedGoogle Scholar
• Buckley A. R., Crowe P. D., Russell D. H. Rapid activation of protein kinase C in isolated rat liver nuclei by prolactin, a known hepatic mitogen. Proc. Natl. Acad. Sci. USA 1988; 85: 8649–8653
   PubMed Web of Science ®Google Scholar
• Michalopoulos G. K. ldquo;Liver regeneration: Molecular mechanisms of growth control”. FASEB J. 1990; 4: 176–187
   PubMed Web of Science ®Google Scholar
• Bojes H. K., Thurman R. G. ldquo;Peroxisome proliferators activate Kupffer cells in vivo”. Cancer Res. 1996; 56: 1–4
   PubMed Web of Science ®Google Scholar
• Rose M. L., Thurman R. G. Rapid phagocytosis of particles of the peroxisome proliferator LY171883 activates Kupffer cells. Fundam. Appl. Toxicol. 1996; 30: 1060
   Google Scholar
• Decker K. ldquo;Biologically active products of stimulated liver macrophages (Kupffer cells)”. Eur. J. Biochem. 1990; 192: 245–261
   PubMedGoogle Scholar
• Sakagami Y., Mizoguchi Y., Seki S., Kobayashi K., Morisawa S., Yamamoto S. Release of leukotriene B4 from rat Kupffer cells. Prostanglandins Leuko. Essent. Fatty Acids 1989; 36: 125–128
   PubMed Web of Science ®Google Scholar
• Pieters M. N., Esbach S., Schouten D., Brower A., Knook D. L., von Berkel T. J. ldquo;Cholesteryl esters from oxidized low-density lipoproteins are in vivo rapidly hydrolyzed in rat Kupffer cells and transported to liver parenchymal cells and bile”. Hepatology 1994; 19: 1459–1467
   PubMed Web of Science ®Google Scholar
• Bayly A. C., Roberts R. A., Dive C. ldquo;Suppression of liver cell apoptosis in vitro by the nongenotoxic hepatocarcinogen and peroxisome proliferator nafenopin”. J. Cell Biol. 1994; 125: 197–203
   PubMed Web of Science ®Google Scholar
• Daniel L. W., Lands W. E. M. Phopholipases. Biochemistry of Arachidonic Acid Metabolism. Matinus Nijhoff, Boston 1985; 175–193
   Google Scholar
• Nakagawa Y., Matsumura T., Goto M., Qu W., Kauffman F. C., Thurman R. G. Increase in oxygen uptake due to arachidonic acid is oxygen dependent in the perfused liver. Am. J. Physiol. 1994; 266: G953–G959
   PubMed Web of Science ®Google Scholar
• Qu W., Zhong Z., Goto M., Thurman R. G. Kupffer cell prostaglandin E2 stimulates paranchymal cell O2 consumption: Effect of alcohol treatment on cell–cell communication. Am. J. Physiol. 1996; 270: G575–G580
   Google Scholar
• Beutler B., Cerami A. ldquo;Cahectin (tumor necrosis factor): A macrophage hormone governing cellular metabolism and inflammatory response”. Endocrine Rev. 1988; 9: 57–66
   PubMed Web of Science ®Google Scholar
• Akerman P., Cote P., Yang S. Q., Mc Clain C., Nelson S., Bagby G. J., Diehl A. M. Antibodies to tumor necrosis factor-α inhibit liver regeneration after partial hepatectomy. Am. J. Physiol. 1992; 263: G579–G585
   PubMed Web of Science ®Google Scholar
• Bojes H. K., Gemolec D. R., Simeonova P., Bruccoleri A., Schoonhoven R., Luster M. I., Thurman R. G. Antibodies to tumor necrosis factor α prevent increases in cell replication in liver due to the potent peroxisome proliferator. Carcinogenesis 1997; WY-14: 643, in press
   Google Scholar
• Cornell R. P., Lijequist B. L., Bartizal K. F. Depresses liver regeneration after partial hepatectomy of germ-free, athymic and lipopolysaccharide-resistant mice. Hepatology 1990; 11: 916–922
   PubMed Web of Science ®Google Scholar
• Endo Y., Suzuki R., Kumagi K. ldquo;Induction of ornithine decarboxylase in liver and spleen of mice by interleuken l-like factors produced from a macrophage line”. Biochem. Biophys. Acta 1985; 838: 343–350
   PubMed Web of Science ®Google Scholar
• Shinagawa T., Yoshioka K., Kakumu S., Wakita T., Ishikawa T., Itoh Y., Takayanagi M. ldquo;Apoptosis in cultured rat hepatocytes: The effects of tumor necrosis factor α and interferon γ”. J. Pathol. 1991; 165: 247–253
   PubMed Web of Science ®Google Scholar
• Stewart A. G., Tomlinson P. R., Fernandes D. J., Wilson J. W., Harris T. ldquo;Tumor necrosis factor alpha modulates mitogenic responses of human cultured airway smooth muscle”. Am. J. Respiratory Cell Mol Biol. 1995; 12: 110–119
   PubMed Web of Science ®Google Scholar
• Hannun Y. A. ldquo;The spingomyelin cycle and the second messenger function of ceramide”. J. Biol. Chem. 1994; 269: 3125–3128
   PubMed Web of Science ®Google Scholar
• Heller R. A., Kronke M. ldquo;Tumor necrosis facator receptor-mediated signaling pathways”. J. Cell. Biol. 1994; 126: 5–9
   PubMed Web of Science ®Google Scholar