ROLE OF KUPFFER CELLS IN PEROXISOME PROLIFERATOR-INDUCED HEPATOCYTE PROLIFERATION*

REFERENCES

• Hawkins J. M., Jones W. E., Bonner F. W., Gibson G. G. The effect of peroxisome proliferators on microsomal. peroxisoma, and mitochondrial enzyme activities in the liver and kidney. Drug Metab. Disp. 1987; 18: 441–515
   Web of Science ®Google Scholar
• Reddy J. K., Lalwani N. D. Carcinogenesis by hepatic peroxisome proliferators: Evaluation of the risk of hypolipidemic drugs and industrial plasticizers to humans. CRC Crit. Rev. Toxicol. 1983; 12: 1–58
   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., Rao M. S. 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 Veldhoven P., Van Broekhoven A., Vandebroek G., Debeer L. J. Evidence that peroxisomal acyl-CoA synthetase is located at the cytoplasmic side of the peroxisomal membrane. Biochem. J. 1982; 204: 17–23
   PubMed Web of Science ®Google Scholar
• Conway J. G., Tomaszewski K. E., Cattley R. C., Marsman D. S., Melnick R. L., Popp J. A. Relationship of oxidative damage to carcinogenicity with the peroxisome proliferators Di(2-ethylhexyl) phthalate (DEHP) and WY-14,643 (WY). Toxicologist 1988; 8: 167
   Google Scholar
• Kasai H., Okada Y., Nishimura S., Rao 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 adminstration of peroxisome proliferators. Peroxisomes: Biology and Importance in Toxicology and Medicine, G. Gibson, B. Lake. Taylor and Francis, London 1993
   Google Scholar
• Nicholls P., Schonbaum G. R. Catalases. The Enzymes, P. D. Boyer. Academic Press, New York 1963
   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; 176: 477–484
   PubMedGoogle 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
• Foerster E-C., Faehrenkemper 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
• Kornbrust D. J., Barfknecht T. R., Ingram P., Shelburne J. D. 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
• Price R. J., Evans J. G., Lake B. G. Comparison of the effects of nafenopin on hepatic peroxisome proliferation 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., Marsmann 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. 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
• Bojes H. K., Thurman R. G. Peroxisome proliferators activate Kupffer cells in vivo. Cancer Res. 1996; 56: 1–4
   PubMed Web of Science ®Google Scholar
• Bojes H. K., Germolec D. R., Simeonova P., Bruccoleri A., 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, WY-14,643. Carcinogenesis 1997; 18: 669–674
   PubMed Web of Science ®Google Scholar
• Rose M. L., Germolec D. R., Schoonhoven R., Thurman R. G. Kupffer cells are causally responsible for the mitogenic effect of peroxisome proliferators. Carcinogenesis 1997; 18: 1453–1456
   PubMed Web of Science ®Google Scholar
• Rose M. L., Germolec D. R., Arteel G. E., Schoonhoven R., Thurman R. G. Dietary glycine completely prevents the increase in hepatocyte proliferation caused by the peroxisome proliferator WY-14,643. Chem. Res. Toxicol. 1997; 10: 1198–1204
   PubMed Web of Science ®Google Scholar
• Rusyn I., Thurman R. G. WY-14,643 rapidly activates the nuclear factor κB in non-parenchymal cells. Hepatology 1997; 26: 460
   Google Scholar
• Nishizuka Y. 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. 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. 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. 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
• McPhail L. C., Clayton C. C., Snyderman R. A potential second messenger role for unsaturated fatty acids: Activation of Ca2+-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. Time and dose-response study of the effects on rats of the plasticizer di(2-ethylhexyl) phthalate. Toxicol. 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., Bridges J. W. Time and dose study on the response of 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. 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. Acyl-CoA synthetase in rat liver peroxisomes. J. Biol. Chem. 1980; 255: 9599–9607
   PubMed Web of Science ®Google Scholar
• Greenberg M. E., Greene L. A., Ziff E. B. Nerve growth factor and epidermal growth factor induce rapid transient changes in proto-oncogen transcription in PC12 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
• Issemann I., Green S. 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., Widmark E., Qiao L., Gustafsson J. 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
• Sher T., Yi H. F., McBride O. W., Gonzalez F. J. cDNA Cloning, chromosomal mapping, and functional characterization of the human peroxisome proliferator activated receptor. Biochemistry 1993; 32: 5598–5604
   PubMed Web of Science ®Google Scholar
• Aldridge T. C., Tugwood J. D., Green S. Identification and characterization of DNA elements implicated in the regulation of CYP4A1 transcription. Biochem. J. 1995; 306: 473–479
   PubMed 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., Westphal H., Gonzalez F. J. Targeted disruption of the alpha isoform of the peroxisome proliferator-activated receptor gene in mice results in abolishment of the pleiotropic effects of peroxisome proliferators. 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 clofibiric acid, Toxicol. Appl. Pharmacol. 1993; 122: 1–6
   PubMed Web of Science ®Google Scholar
• Nagel R. A., Dirix L. Y., Hayllar K. M., Preisig R., Tredger J. M., Williams R. Use of quantitative liver function tests—Caffeine clearance and galactose elimination capacity after orthotopic liver transplantation. Hepatology 1990; 10: 149–157
   Web of Science ®Google Scholar
• Birmelin M., Decker K. Ca2+ 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
• Rose M. L., Thurman R. G. Rapid phagocytosis of particles of the peroxisome proliferator LY171883 activates Kupffer cells. Fund. Appl. Toxicol. 1995; 30(1)1060
   Google Scholar
• Pieters M. N., Esbach S., Schouten D., Brower A., Knook D. L., van Berkel T. J. 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; 6: 1459–1467
   Google Scholar
• Baldwin J. R., Witiak D. T., Feller D. R. Disposition of clofibrate in the rat. Acute and chronic administration. Biochem. Pharmacol. 1980; 29: 3143–3154
   PubMed Web of Science ®Google Scholar
• Rose M. L., Rivera C. A., Schoonhoven R., Swenberg J. A., Thurman R. G. Peroxisome proliferators activate Kupffer cells directly. Toxicol. Sci. 1998; 42: 11
   Google Scholar
• Beutler B., Cerami A. Cachectin (tumor necrosis factor): A macrophage hormone governing cellular metabolism and inflammatory response. Endocr. Rev. 1988; 9: 57–66
   PubMed Web of Science ®Google Scholar
• Akerman P., Cote P., Yang S. Q., McClain 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
• Beyer H. S., Theologides A. Tumor necrosis factor-α is a direct hepatocyte mitogen in the rat. Biochem. Mol. Biol. Int. 1993; 29: 1–4
   PubMedGoogle Scholar
• Feingold K. R., Soued M., Grunfeld C. Tumor necrosis factor stimulates DNA synthesis in the liver of intact rats. Biochem. Biophys. Res. Commun. 1988; 153: 576–582
   PubMed Web of Science ®Google Scholar
• Rolfe M., James R., Roberts R. A. Tumour necrosis factor α suppresses apoptosis and induces DNA synthesis in rodent hepatocytes: A mediator of the hepatocarcinogenicity of peroxisome proliferators. Carcinogenesis 1997; 18: 2277–2280
   PubMed Web of Science ®Google Scholar
• Cornell R. P., Liljequist B. L., Bartizal K. F. Depressed liver regeneration after partial hepatectomy of germ-free, athymic and lipopolysaccharide-resistant mice. Hepatology 1990; 11: 916–922
   PubMed Web of Science ®Google Scholar
• Shinagawa T., Yoshioka K., Kakumu S., Wakita T., Ishikawa T., Itoh Y., Takayanagi M. 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. Tumor necrosis factor alpha modulates mitogenic responses of human cultured airway smooth muscle. Am. J. Respir. Cell Mol. Biol. 1995; 12: 110–119
   PubMed Web of Science ®Google Scholar
• Cowper K. B., Currin R. T., Dawson T. L., Lindert K. A., Lemasters J. J., Thurman R. G. A new method to monitor Kupffer cell function continuously in the perfused rat liver: Dissociation of glycogenolysis from particle phagocytosis. Biochem. J. 1990; 266: 141–147
   PubMed Web of Science ®Google Scholar
• Gunawardhana L., Mobley S. A., Sipes I. G. Modulation of 1,2-dichlorobenzene hepatotoxicity in the Fischer-344 rat by a scavenger of superoxide anions and an inhibitor of Kupffer cells. Toxicol. Appl. Pharmacol. 1993; 119: 205–213
   PubMed Web of Science ®Google Scholar
• Marzi I., Cowper K. B., Takei Y., Lindert K. A., Lemasters J. J., Thurman R. G. Methyl palmitate prevents Kupffer cell activation and improves survival after orthotopic liver transplantation in the rat. Transplant. Int. 1991; 4: 215–220
   PubMed Web of Science ®Google Scholar
• Kato K., Onodera K., Kato J., Kasai S., Mito M. The immuno-stimulant OK-432 enhances liver regeneration after 70% hepatectomy. J. Hepatol. 1995; 23: 87–94
   PubMed Web of Science ®Google Scholar
• Decker K. Biologically active products of stimulated liver macrophages (Kupffer cells). Eur. J. Biochem. 1990; 192: 245–261
   PubMedGoogle Scholar
• Inestrosa N. C., Bronfman M., Leighton F. Detection of peroxisomal fatty acyl-coenzyme A oxidase activity. Biochem. J. 1979; 182: 779–788
   PubMed Web of Science ®Google Scholar
• Kayama F., Yoshida T., Elwell M. R., Luster M. I. Role of tumor necrosis factor-α in cadmium-induced hepatotoxicity. Toxicol. Appl. Pharmacol. 1995; 131: 224–234
   PubMed Web of Science ®Google Scholar
• Ikejima K., Iimuro Y., Forman D. T., Thurman R. G. A diet containing glycine improves survival in endotoxin shock in the rat. Am. J. Physiol. 1996; 271: G97–G103
   PubMed Web of Science ®Google Scholar
• Ikejima K., Qu W., Stachlewitz R. F., Thurman R. G. Kupffer cells contain a glycine-gated chloride channel. Am. J. Physiol. 1997; 272: G1581–G1586
   PubMed Web of Science ®Google Scholar
• Dieter P., Schulze-Specking A., Decker K. Ca2+ requirement of prostanoid but not of superoxide production by rat Kupffer cells. Eur. J. Biochem. 1988; 177: 61–67
   PubMedGoogle Scholar
• Kawada N., Mizoguchi Y., Kobayashi K., Monna T., Morisawa S. Calcium-dependent prostaglandin biosynthesis by lipopolysaccharide-stimulated rat Kupffer cells. Prostaglandins Leukot. Essent. Fatty Acids 1992; 47: 209–214
   PubMed Web of Science ®Google Scholar
• Currin R. T., Lichtman S. N., Thurman R. G., Lemasters J. J. Pentoxifylline, adenosine, prostaglandin E1 and nisoldipine inhibit tumor necrosis factor release from LPS-stimulated rat Kupffer cells. Hepatology 1991; 14: 470
   Google Scholar
• Watanabe N., Suzuki J., Kobayashi Y. Role of calcium in tumor necrosis factor-α produced by activated macrophages. J. Biochem. 1996; 120: 1190–1195
   PubMed Web of Science ®Google Scholar
• Baldwin A. S. The NF-κB and IκB proteins: New discoveries and insights. Annu. Rev. Immunol. 1996; 14: 649–681
   PubMed Web of Science ®Google Scholar
• Li Y., Leung L. K., Glauert H. P., Spear B. T. Treatment of rats with the peroxisome proliferator ciprofibrate results in increased liver NF-κB activity. Carcinogenesis 1996; 17: 2305–2309
   PubMed Web of Science ®Google Scholar
• Menegazzi M., Carcereri-De Prati A., Suzuki H., Shinozuka H., Pibiri M., Piga R., Columbano A., Ledda-Columbano G. M. Liver cell proliferation induced by nafenopin and cyproterone acetate is not associated with increases in activation of transcription factors NF-κB and AP-1 or with expression of TNF alpha. Hepatology 1997; 25: 585–592
   PubMed Web of Science ®Google Scholar
• Ohmura T., Ledda-Columbano G. M., Piga R., Columbano A., Glemba J., Katyal S. L., Locker J., Shinozuka H. Hepatocyte proliferation induced by a single dose of a peroxisome proliferator. Am. J. Pathol. 1996; 148: 815–824
   PubMed Web of Science ®Google Scholar
• Rusyn I., Tsukamoto H., Thurman R. G. WY-14,643 rapidly activates nuclear factor κB in Kupffer cells before hepatocytes. Carcinogenesis 1998; 7: 1217–1222
   Google Scholar
• Diaz-Meco M. T., Dominguez I., Sanz L., Dent P., Lozano J., Municio M. M., Berra E., Hay R. T., Sturgill T. W., Moscat J. Zeta PKC induces phosphorylation and inactivation of I kappa B-alpha in vitro. EMBO J. 1994; 13: 2842–2848
   PubMed Web of Science ®Google Scholar
• Flohe L., Brigelius-Flohe R., Saliou C., Traber M. G., Packer L. Redox regulation of NF-kappa B activation. Free Rad. Biol. Med. 1997; 22: 1115–1126
   PubMed Web of Science ®Google Scholar
• Wiezorek J. S., Brown D. H., Kupperman D. E., Brass C. A. Rapid conversion to high xanthine oxidase activity in viable Kupffer cells during hypoxia. J. Clin. Invest. 1994; 94: 2224–2230
   PubMed Web of Science ®Google Scholar
• Grilli M., Chiou J. S., Lenardo M. J. NF-κB and Rel: Participants in a multiform transcriptional regulatory system. Int. Rev. Cytol. 1993; 143: 1–62
   PubMed Web of Science ®Google Scholar
• Columbano A., Shinozuka H. Liver regeneration versus direct hyperplasia. FASEB J 1996; 10: 1118–1128
   PubMed Web of Science ®Google Scholar
• Peters J. M., Cattley R. C., Gonzalez F. J. Role of PPARα in the mechanism of action of the nongenotoxic carcinogen and peroxisome proliferator WY-14,643. Carcinogenesis 1997; 18: 2029–2033
   PubMed Web of Science ®Google Scholar
• Nanji A. A., Dannenberg A. J., Thomas P., Bass N. M. Ethanol selectively induces expression of peroxisome proliferator-activated receptor α (PPARα) in hepatocytes: Evidence for a role for oxidized products of arachidonic acid. Hepatology 1996; 24(4)1256
   PubMed Web of Science ®Google Scholar