Cellular Models in Natural Toxins Investigations: Intestinal and Kidney Cell Lines

References

• Zucco F. Freshly isolated cells and cell lines from the intestine as an in vitro model for toxicological studies. Toxic. in Vitro 1993; 7: 397
   PubMed Web of Science ®Google Scholar
• Pinto M., Robin-Leon S., Appay M-D., Kedinger M., Triadou N., Dussaulx E., Lacroix B., Simon-Assman P., Haffen K., Fogh J., Zweibaum A. Enterocyte-like differentiation and polarization of the human colon carcinoma cell line Caco-2 in culture. Biol. Cell 1983; 47: 323
   Web of Science ®Google Scholar
• Ramond M-J., Martinot-Peignoux M., Erlinger S. Dome formation in the human colon carcinoma cell line Caco-2 in culture. Influence of ouabaun and permeable supports. Biol. Cell 1985; 54: 89
   PubMed Web of Science ®Google Scholar
• Vachon P. H., Beaulieu J-F. Transient mosaic patterns of morphological and functional differentiation in the Caco-2 cell line. Gastroenterology 1992; 103: 414
   PubMed Web of Science ®Google Scholar
• Chantret I., Barbat A., Dussaulx E., Brattain M. G., Zweibaum A. Epithelial polarity, villin expression, and enterocytic differentiation of cultured human colon carcinoma cells: a survey of twenty cell lines. Cancer Res. 1988; 48: 1936
   PubMed Web of Science ®Google Scholar
• Rousset M. The human colon carcinoma cell lines HT-29 and Caco-2: two in vitro models for the study of intestinal differentiation. Biochimie 1986; 68: 1035
   PubMed Web of Science ®Google Scholar
• Huet C., Sahuquillo-Merino C., Coudrier E., Louvard D. Absorptive and mucus-secreting subclones isolated from a multipotent intestinal cell line (HT-29) provide new models for cell polarity and terminal differentiation. J. Cell Biol. 1987; 105: 345
   PubMedGoogle Scholar
• Dharmsathaphorn K., McRoberts J. A., Mandel K. G., Tisdale L. D., Masui I. A human colonic tumor cell line that maintains vectorial electrolyte transport. Am. J. Physiol. 1984; 246: G204
   PubMed Web of Science ®Google Scholar
• Dharmsathaphorn K., Madara J. Established intestinal cell lines as model systems for electrolyte transport studies. Methods in Enzymology vol. 192, Biomembranes, S. Fleischer, B. Fleischer. Academic Press, San Diego 1990; 354
   Google Scholar
• Murakami H., Masui H. Hormonal control of human colon carcinoma cell growth in serumfree medium. Proc. Natl. A cad. Sci. 1980; 77: 3464
   Google Scholar
• Quaroni A., May R. J. Establishment and characterization of intestinal epithelial cell cultures. Methods Cell Biol. 1980; 21: 403
   Google Scholar
• Guarino A., Cohen M., Thompson M., Dharmasathaphorn K., Giannella R. T84 cell receptor binding and guanyl cyclase activation by Escherichia coli heat-stable toxin. Am. J. Physiol. 1987; 253: G775
   PubMedGoogle Scholar
• Huott P. A., Liu W., McRoberts J. A., Giannella R. A., Dharmasathaphorn K. Mechanism of action of Eschrichia coli heat-stable enterotoxin in a human colonic cell line. J. Clin. Invest. 1988; 82: 514
   PubMedGoogle Scholar
• Levine S. A., Donowitz M., Watson J. M., Sharp G. W.G., Crane J. K., Weikel C. S. Characterization of the synergistic interaction of Escherichia coli heat-stable toxin and carbachol. Am. J. Physiol. 1991; 261: G592
   Google Scholar
• Mezoff A. G., Giannella R. A., Eade M. N., Cohen M. B. Escherichia coli enterotoxin (STa) binds to receptors, stimulates Guanyl cyclase, and impairs absorption in rat colon. Gastroenterology 1992; 102: 816
   PubMedGoogle Scholar
• Cohen M. B., Jensen N. J., Hawkins J. A., Mann E. A., Thompson M. R., Lentze M. J., Giannella R. A. Receptors for Escherichia coli heat stable enterotoxin in human intestine and in a human intestinal cell line (Caco-2). J. Cell. Physiol. 1993; 156: 138
   Google Scholar
• Mann E. A., Cohen M. B., Giannella R. A. Comparison of receptors for Escherichia coli heat-stable enterotoxin: novel receptor present in IEC-6 cells. Am. J. Physiol. 1993; 264: G172
   Google Scholar
• Lencer W. I., Delp C., Neutra M. R., Madara J. L. Mechanism of cholera toxin action on polarized human intestinal epithelial cell line: role of vescicular traffic. J. Cell Biol. 1992; 117: 1197
   PubMed Web of Science ®Google Scholar
• Apter F. M., Lencer W. I., Finkelstein R. A., Mekalanos J. J., Neutra M. R. Monoclonal immunoglobulin A antibodies directed against Cholera toxin prevent the toxin-induced chioride secretory response and block toxin binding to intestinal epithelial cells in vitro. Infect. Immun. 1993; 61: 5271
   PubMed Web of Science ®Google Scholar
• McGee D. W., Elson C. O., McGee J. R. Enhancing effect of Cholera toxin on interleukin-6 secretion by IEC-6 intestinal epithelial cells: mode of action and augmentating effect of inflammatory cytokines. Infect. Immun. 1993; 61: 4637
   PubMed Web of Science ®Google Scholar
• Bromander A. K., Kjerrulf M., Holmgren J., Lycke N. Cholera toxin enhanced alloantigens presentation by cultured intestinal epithelial cells, Scand. J. Immunol. 1993; 37: 452
   Google Scholar
• Chiossone D. C., Simon P. L., Smith P. L. Interleukin-1: effects on rabbit ileal mucosal ion transport in vitro. Eur. J. Pharmacol. 1990; 180: 217
   Google Scholar
• Czerucka D., Roux I., Rampal P. Saccharomyces boulardii inhibits secretagogue-mediated adenisine 3′,5′-cyclic monophosphate induction in intestinal cells. Gastroenterology 1994; 106: 65
   PubMed Web of Science ®Google Scholar
• Hecht G., Pothoulakis C., Thomas La Mont J., Madara L. Clostridium difficile Toxin A pertubs cytoskeletal structure and tight junction permeability of cultured human intestinal epithelial monolayers. J. Clin. Invest. 1988; 82: 1516
   PubMed Web of Science ®Google Scholar
• Fiorentini C., Donelli G., Nicotera P., Thelestam M. Clostridium difficile Toxin A elicits Ca++-independent cytotoxic effects in cultured normal rat intestinal crypt cells. Infect. Immun. 1993; 61: 3988
   PubMed Web of Science ®Google Scholar
• Torres J., Camorlinga-Ponce M., Munoz O. Sensitivity in culture of epithelial cells from rhesus monkey kidney and human colon carcinoma to Toxins A and B from Clostridium difficile. Toxicon 1992; 30: 419
   PubMed Web of Science ®Google Scholar
• Weikel C. S., Grieco F. D., Reuben J., Myers L. L., Sack R. B. Human colonic epithelial cells, HT29/C1, treated with crude Bacterioidis fragilis enterotoxin dramatically alter their morphology. Infect. Immun. 1992; 60: 321
   PubMedGoogle Scholar
• Canada A. T., Watkins W. D., Nguyen T. D. The toxicity of flavonols to guinea pig enterocytes. Toxicol. Appl. Pharmacol. 1989; 99: 357
   PubMed Web of Science ®Google Scholar
• Nguyen T. D., Canada A. T., Heintz G. G., Gettys T. W., Chon J. A. Stimulation of secretion by the T84 colonic epithelial cell line with dietary flavonols. Biochem. Pharmacol. 1991; 41: 1879
   PubMed Web of Science ®Google Scholar
• Nguyen T. D., Canada A. T. Citrus flavonoids stimulates secretion by human colonic T84 cells. J. Nutr. 1993; 123: 259
   PubMed Web of Science ®Google Scholar
• Draaijer M., Koninkx J., Hendriks H., Kik M., Van Dijk J., Mouwen J. Actin cytoskeletal lesion in differentiated human colon carcinoma Caco-2 cells after exposure to soybean agglutinin. Biol. Cell 1989; 65: 29
   PubMedGoogle Scholar
• Koninkx J., Hendriks H., Van Rossum J., Van den Ingh T., Mouwen J. Interaction of legume lectins with the cellular metabolism of differentiated Caco-2 cells. Gastroenterology 1992; 102: 1516
   PubMedGoogle Scholar
• Leher C-M., Lee V. H. Binding and transport of some bioadhesive plant lectins across Caco-2 cell monolayer. Pharmac. Res. 1993; 10: 1796
   Google Scholar
• Wilson G., Davis S. S., Illum L., Zweibaum A. Pharmaceutical application of cell and tissue culture to drug transport. Plenum Press, New York 1991
   Google Scholar
• Rousset M., Laburthe M., Pinto M., Chevalier G., Ruyer-Fessard C., Dussaulx E., Trugnan G., Boige N., Brun J-L., Zweibaum A. Enterocytic differentiation and glucose utilization in the human colon tumor cell line Caco-2: modulation by forskolin. J. Cell. Physiol. 1985; 123: 377
   PubMed Web of Science ®Google Scholar
• Darmoul D., Baricault L., Sapin C., Chantret I., Trugnan G., Rousset M. Decrease of mRNA levels and biosynthesis of sucrase-isomaltase but not dipeptidylpeptidase IV in forskolin or monesin-treated Caco-2 cells. Experientia 1991; 47: 1211
   Google Scholar
• Baricault L., Garcia M., Cibert C., Sapin C., Geraud G., Codogno P., Trugnan G. Forskolin blocks the apical expression of dipeptidyl peptidase IV in Caco-2 cells and induces its retention in lamp-1-containing vescicles. Exp. Cell Res. 1993; 209: 277
   Google Scholar
• Kreisberg J. I., Wilson P. D. Renal cell culture. J. Electr. Micr. Tech. 1988; 9: 235
   Google Scholar
• Leighton H., Brada Z., Estes L. W., Justh G. Secretory activity and oncogenicity of a cell line (MDCK) derived from canine kidney. Science 1969; 163: 472
   PubMedGoogle Scholar
• Rindler M. J., Chuman L. M., Shaffer L., Saier M. H. Retention of differentiated properties in an established dog kidney epithelial cell line (MDCK). J. Cell Biol. 1979; 81: 635
   PubMed Web of Science ®Google Scholar
• Meza I., Ibarra G., Sabanero M., Martinez-Palomo A., Cereijido M. Occluding junctions and cytoskeletal components in a cultured transporting epithelium. J. Cell Biol. 1980; 87: 746
   PubMed Web of Science ®Google Scholar
• Cereijido M., Meza I., Martinez-Palomo A. Occluding junctions in cultured epithelial monolayers. Am. J. Physiol. 1981; 240: C96
   Google Scholar
• Thomas S. R., Shultz S. G., Lever J. E. Stimulation of dome formation in MDCK kidney epithelial cultures by inducers of differentiation: dissociation from effects on transepithelial resistance and cyclic AMP levels. J. Cell. Physiol. 1982; 113: 427
   Google Scholar
• Leighton J., Estes L. W., Mansukhani S., Brada Z. A cell line derived from normal dog kidney (MDCK) exhibiting qualities of papillary adenocarcinoma and of renal tubular epithelium. Cancer 1970; 26: 1022
   Google Scholar
• Valentich J. D., Tchao R., Leighton J. Hemicyst formation stimulated by cyclic AMP in dog kidney cell line MDCK. J. Cell Physiol. 1979; 100: 291
   PubMed Web of Science ®Google Scholar
• Lever J. E. Inducers of mammalian cell differentiation stimulate dome formation in a differentiated kidney epithelial cell line (MDCK). Proc. Natl. Acad. Sci. USA 1979; 76: 1323
   PubMedGoogle Scholar
• Rindler M. J., Chuman L. M., Shaffer L., Saier M. H., Jr. Retention of differentiated properties in an established dog kidney epithelial cell line (MDCK). J. Cell Biol. 1979; 81: 635
   PubMed Web of Science ®Google Scholar
• Abaza N. A., Leighton J., Shultz S. Effects of ouabain on the function and structure of a cell line (MDCK) derived from canine kidney. In Vitro 1974; 10: 172
   Google Scholar
• Misfeldt D. S., Hamamoto S. T., Pitelka D. R. Transepithelial transport in cell culture. Proc. Natl. Acad. Sci. USA 1976; 73: 1212
   PubMed Web of Science ®Google Scholar
• Taub M., Chuman L., Saier M. H., Sato G. Growth of Madin-Darby canine kidney epithelial cell (MDCK) line in hormone-supplemented, serum-free medium. Proc. Natl. Acad. Sci. USA 1979; 76: 3338
   PubMedGoogle Scholar
• Boerner P., Saier M. H. Nutrient transport and growth regulation in kidney epithelial cells (MDCK) cultured in a defined medium. Growth of cells in hormonally defined media, G. H. Sato, A. B. Pardee, D. A. Sirbasku. Vol. 9: 555–565, Book A
   Google Scholar
• Hull Cherry R. H.W.R., Weaver G. W. The origin and characteristics of a pig kidney cell strain LLC-PK1. In Vitro 1976; 12: 670
   Google Scholar
• Lever J. E., Sari C. E. Effect of tunicamycin on polarized membrane functions of an established kidney epithelial cell line. Biochim. Biophys. Acta 1983; 762: 265
   Google Scholar
• Melby E., Prydz Olsnes K. S., Sandvig K. Effect of monensin on ricin and fluid phase transport in polarized MDCK cells. J. Cell. Biochem. 1991; 47: 251
   PubMed Web of Science ®Google Scholar
• Riley R. T., Hinton D. M., Showker J. L., Rigsby W, Norred W. P. Chronology of patulin-induced alterations in membrane function of cultured renal cells, LLC-PK1. Toxicol. Appl. Pharmacol. 1990; 102: 128
   Google Scholar
• Riley R. T., Showker J. L. The mechanism of patulin's cytotoxicity and the antioxidant activity of indole tetramic acid. Toxicol. Appl. Pharmacol. 1991; 109: 108
   PubMed Web of Science ®Google Scholar
• Burghardt R. C., Barhoumi R., Lewis E. H., Hartford Bailey R., Pyle K. A., Clement B. A., Phillips T. D. Patulin-induced cellular toxicity: a vital fluorescence study. Toxicol. Appl. Pharmacol. 1992; 112: 235
   PubMed Web of Science ®Google Scholar
• Richard J.-M., Creppy E. E., Benoit-Guyod J.-L., Dirheimer G. Orellanine inhibits protein synthesis in Madin-Darby canine kidney cells, in rat liver mitochondria, and in vitro: indication for its activation prior to in vitro inhibition. Toxicology 1991; 67: 53
   PubMed Web of Science ®Google Scholar
• Ruedl C., Gstraunthaler G., Moser M. Differential inhibitory action of the fungal toxin orellanine on alkaline phosphatase isoenzymes. Biochim. Biophys. Acta 1989; 991: 280
   Google Scholar
• Kretz O., Creppy E. E., Boulanger Y., Dirheimer G. Purification and some properties of bolesatine, a protein inhibiting in vitro protein synthesis, from the mushroom Boletus satanas Lenz (Boletaceae). Arch. Toxicol., suppl. 1989; 13: 422
   PubMedGoogle Scholar
• Kretz O., Creppy E. E., Dirheimer G. Characterization of bolesatine, a toxic protein from the mushroom Boletus satanas Lenz and it's effects on kidney cells. Toxicology 1991; 66: 213
   PubMedGoogle Scholar
• Lindenfelser L. A., Lillehoj E. B., Milburn M. S. Ochratoxin and penicillic acid in tumorigenic and acute toxicity tests with white mice. Dev. Ind. Microbiol. 1973; 14: 331
   Google Scholar
• Purchase I. F.H., Theron J. J. The acute toxicity of ochratoxin A to rats. J. Fd. Cosmet. Toxicol. 1968; 6: 479
   PubMedGoogle Scholar
• Kitabatake N., Doi E., Trivedi A. B. Toxicity evaluation of the mycotoxins, citrinin and ochratoxin A, using several animal cell lines. Comp. Biochem. Physiol. 1993; 105C: 429
   Google Scholar
• Vesonder R. F., Gasdorf H., Peterson E. Comparison of the cytotoxicities of Fusarium metabolites and Alternaria metabolite AAL-toxin to cultured mammalian cell lines. Arch. Environ. Contam. Toxicol. 1993; 24: 473
   PubMed Web of Science ®Google Scholar
• Shier W. T., Abbas H. K., Mirocha C. J. Toxicity of mycotoxins fumonisins B1 and B2 and Alternaria alternata f. sp. lycopersici toxin (AAL) in cultured mammalian cells. Mycopathologia 1991; 116: 97
   PubMed Web of Science ®Google Scholar
• Yoo H.-S., Norred W. P., Wang E., Merrill A. H., Jr, Riley R. T. Fumonisin inhibition of de novo sphingolipid biosynthesis and cytotoxicity are correlated in LLC-PK1 cells. Toxicol. Appl. Pharmacol. 1992; 114: 9
   PubMed Web of Science ®Google Scholar
• Wang E., Norred W. P., Bacon C. W., Riley R. T., Merrill A. H. Inhibition of sphingolipid biosynthesis by fumonisins: implications for diseases associated with Fusarium moniliforme. J. Biol. Chem., 266: 14, 486
   Google Scholar
• Merrill A. H., Jr. Cell regulation by sphingosine and more complex sphingolipids. J. Bioenerg. Biomembr. 1991; 23: 83
   PubMed Web of Science ®Google Scholar
• Voss K. A., Norred W. P., Plattner R. D., Bacon C. W. Hepatotoxicity and renal toxicity in rats of corn samples associated with field cases of equine leukoencephalomalacia. Fd. Chem. Toxicol. 1989; 27: 89
   PubMed Web of Science ®Google Scholar
• Norred W. P., Wang E., Yoo H., Riley R. T., Merrill A. H. In vitro toxicology of fumonisins and the mechanistic implications. Mycopathologia 1992; 117: 73
   PubMedGoogle Scholar
• Nassberger L., Bergstrand A., De Pierre J. W. An electron and fluorescence microscopic study of LLC-PK1, cells, a kidney epithelial cell line: normal morphology and cyclosporin A-and cremophor-induced alterations. Int. J. Exp. Pathol. 1991; 72: 365
   PubMed Web of Science ®Google Scholar
• Steyn P. S., Vleggaar R., Du Preez N. P., Blyth A. A., Seegers J. C. The in vitro toxicity of analogs of ochratoxin A in monkey kidney epithelial cells. Toxicol. Appl. Pharmacol. 1975; 32: 198
   PubMed Web of Science ®Google Scholar
• Garvican L., Rees K. R. The effect of aflatoxin B1, on the maturation of ribosomal and transfer RNA in monkey kidney (CV-1) cells in culture. Chem.-Biol. Interact. 1974; 9: 429
   PubMedGoogle Scholar
• Olsnes S., Sandvig K. How protein toxins enter and kill the cells. Immunotoxins, A. E. Frankel. Kluwer, Boston 1988; 39–73
   Google Scholar
• Olsnes S., Pihl A. Cytotoxicoproteins with intracellular site of action: mechanism of action and anti-cancer properties. Cancer Surv. 1982; 1: 467
   Google Scholar
• Olsnes S., Sandvig K., Petersen O. W., van Deurs B. Immunotoxins-entry into cells and mechanism of action. Immunol. Today 1989; 10: 291
   PubMedGoogle Scholar
• Sandvig K., van Deurs B. Toxin-induced cell lysis: protection by 3-methyladenine and cycloheximide. Exp. Cell res. 1992; 200: 253
   Google Scholar
• Yoshida T., Chen C., Zhang M., Wu H. C. Disruption of the Golgi apparatus by brefeldin A inhibits the cytotoxicity of ricin, modeccin and Pseudomonas toxin. Exp. Cell Res. 1991; 190: 11
   Google Scholar
• Yoshida T., Chen C., Zhang M., Wu H. C. Increased cytotoxicity of ricin in a putative Golgi-defective mutant of Chinese hamster ovary cell. Exp. Cell Res. 1991; 192: 389
   PubMedGoogle Scholar
• Oda T., Wu H. C. Cerulinin inhibits the cytotoxicity of ricin, modeccin, Pseudomonas toxin and diphteria toxin in Brefeldin A-resistant cell lines. J. Biol. Chem. 1993; 268: 12596
   Google Scholar
• van Deurs B., Hansen S. H., Petersen O., Melby E., Sandvig K. Endocytosis, intracellular transport and transcytosis of the toxic protein ricin by a polarized epithelium. Eur. J. Cell Biol. 1990; 51: 96
   Google Scholar
• Melby E. L., Jacobsen J., Olsnes S., Sandvig K. Entry of protein toxins in polarized epithelial cells. Cancer Res. 1993; 53: 1755
   PubMed Web of Science ®Google Scholar