Alteration of kinase-mediated signalings in murine peritoneal macrophages by aflatoxin B1

Cancer Letters

Volumn 155, Issue 1, 2000, Pages 9-17

  Moon, Eun Yi ^a   Rhee, Dong Kwon ^b   Pyo, Suhkneung ^b  

^a DongWha Pharm Ind Co   (South Korea)

^b Sungkyunkwan University   (South Korea)

Author keywords

Aflatoxin B1; Lipopolysaccharide; Macrophages; Nitric oxide; Phosphorylation; Protein kinase C; Signaling

Indexed keywords

AFLATOXIN B1; CALCIUM ION; CHOLERA TOXIN; GUANINE NUCLEOTIDE BINDING PROTEIN; IONOMYCIN; LIPOPOLYSACCHARIDE; NITRIC OXIDE; PHORBOL 13 ACETATE 12 MYRISTATE; PROTEIN KINASE C;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; MALE; MOUSE; NONHUMAN; PERITONEUM MACROPHAGE; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; SIGNAL TRANSDUCTION;

AFLATOXIN B1; ANIMALS; BLOTTING, WESTERN; CALCIUM; CARCINOGENS; CHOLERA TOXIN; DOSE-RESPONSE RELATIONSHIP, DRUG; GTP-BINDING PROTEINS; IONOMYCIN; IONOPHORES; IONS; LIPOPOLYSACCHARIDES; MACROPHAGES, PERITONEAL; MALE; MICE; NITRIC OXIDE; PHOSPHORYLATION; PHOSPHOTRANSFERASES; PROTEIN KINASE C; SIGNAL TRANSDUCTION; TETRADECANOYLPHORBOL ACETATE;

ANIMALIA; MURINAE;

EID: 0034601097     PISSN: 03043835     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0304-3835(00)00363-3     Document Type: Article

References (44)

1. Robens J.F., Richard J.L. Aflatoxins in animal and human health. Rev. Environ. Toxicol. 127:1992;69-94.
2. 1 on murine splenocyte culture. Environ. Mutagens Carcinogens. 13:1993;73-82.
3. 1. J. Appl. Pharmacol. 4:1996;190-195.
4. 1 and T-2 toxin on the granulocyte-macrophage progenitor cells in mouse bone marrow cultures. Immunopharmacology. 27:1994;57-65.
5. Adams D.O., Hamilton T.A. The cell biology of macrophage activation. Annu. Rev. Immunol. 2:1984;283-318.
6. Keller R., Keist R. Abilities of activated macrophages to manifest tumoricidal activity and to generate reactive nitrogen intermediates: a comparative study in vitro and ex vivo. Biochem. Biophys. Res. Commun. 164:1989;968-973.
7. Bredt D.S., Snyder S.H. Nitric oxide: a physiologic messenger molecule. Annu. Rev. Biochem. 63:1994;175-195.
8. 1-induced suppression of nitric oxide production in murine peritoneal macrophages. J. Toxicol. Environ. Health. 55:1998;517-530.
9. 1 on murine peritoneal macrophage functions. Toxicology. 133:1999;171-179.
10. 1 exposure in vivo. Int. J. Immunopharmacol. 21:1999;47-58.
11. Raetz C.R.H., Ulevitch R.J., Wright S.D., Sibley C.H., Ding A., Nathan C.F. Gram-negative endotoxin: an extraordinary lipid with profound effects on eukaryotic signal transduction. FASEB J. 5:1991;2652-2660.
12. Ulevitch R.J., Tobias P.S. Recognition of endotoxin by cells leading to transmembrane signaling. Curr. Opin. Immunol. 6:1994;125-130.
13. Jakway J.P., DeFranco A.L. Pertussis toxin inhibition of cell and macrophage responses to bacterial lipopolysaccharide. Science. 234:1986;743-746.
14. Prpic V., Weiel J.E., Somers S.D., DiGuiseppi J., Gonias S.L., Pizzo S.V., Hamilton T.A., Herman B., Adams D.O. Effects of bacterial lipopolysaccharide on the hydrolysis of phosphatidylinositol-4,5-biphosphate in murine peritoneal macrophages. J. Immunol. 147:1987;980-985.
15. Letari O., Nicosia S., Chiavaroli C., Vacher P., Schlege W. Activation by bacterial lipopolysaccharide causes changes in the cytolytic free calcium concentration in single peritoneal macrophages. J. Immunol. 147:1991;980-983.
16. Kovacs E.J., Radzioch D., Young H.A., Varesio L. Differential inhibition of IL-1 and TNF-α mRNA expression by agents which block second messenger pathway in murine macrophages. J. Immunol. 139:1988;526-530.
17. Arditi M., Zjou J., Torres M., Durden D.L., Stins M., Kim K.S. Lipopolysaccharide stimulates the tyrosine phosphorylation of mitogen-activated protein kinases p44, p42 and p41 in vascular endothelial cells in a soluble CD14-dependent manner. J. Immunol. 155:1995;3994-4003.
18. Weiel J.E., Hamilton T.A., Adams D.O. LPS induces altered phosphate labelling of proteins in murine peritoneal macrophages. J. Immunol. 136:1986;3012-3018.
19. Shinomiya H., Hirataand H., Nakano M. Purification and characterization of the 65-kDa proteins in murine peritoneal macrophages by stimulation with bacterial lipopolysaccharide. J. Immunol. 146:1991;3617-3625.
20. Weinstein S.L., Gold M.R., DeFranco A.L. Bacterial lipopolysaccharide stimulates protein tyrosine phosphorylation in macrophages. Proc. Natl. Acad. Sci. USA. 88:1991;4148-4152.
21. Weinstein S.L., Sanghera J.S., DeFranco A.L., Pelech S.L. LPS induces tyrosine phosphorylation and activation of MAP kinases in macrophages (Abstract). J. Cell Biochem. 16C:1992;169.
22. 1 exposure: phosphatidylinositol metabolism. Chem. Biol. Interact. 98:1995;145-152.
23. Pyo S., Gangemi J.D., Ghaffarand A., Mayer E.P. Poly I: C-induced anti-herpes simplex virus type I activity in inflammatory macrophages is mediated by induction of interferon-β J. Leukocyte Biol. 50:1991;479-487.
24. Klimetzek V., Remold H.G. The murine bone marrow macrophage, a sensitive indicator cell for murine migration inhibitory factor and a new method for their harvest. Cell. Immunol. 53:1980;257-266.
25. Ding A.H., Nathan C.F., Stuehr D.J. Release of reactive nitrogen intermediates and reactive oxygen intermediates from mouse peritoneal macrophages: comparison of activating cytokines and evidence for independent production. J. Immunol. 141:1988;2407-2412.
26. His E.D., Siegel J.N., Minami Y., Luong E.T., Klaunsner R.D., Samelson L.E. T cell activation induces rapid tyrosine phosphorylation of a limited number of cellular substrates. J. Biol. Chem. 264:1989;10836-10842.
27. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
28. Shinji H., Akagawa K.S., Yoshida T. LPS induces selective translocation of protein kinase C-β in LPS-responsive mouse macrophages, but not in LPS-non-responsive mouse macrophages. J. Immunol. 153:1994;5760-5771.
29. Yasuda I., Kishimoto A., Tanaka S., Tominaga M., Sakurai A., Nishizuka Y. A synthetic peptide substrate for selective assay of protein kinase C. Biochem. Biophys. Res. Commun. 166:1990;1220-1227.
30. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
31. Stossel T.P. Evaluation of opsonic and leukocyte function with a spectrophotometric test in patients with infection and with phagocytic disorder. Blood. 42:1973;121-130.
32. 1-induced hepatocellular carcinoma and adenoma in the rat: detection by denaturing gradient gel electrophoresis. Proc. Natl. Acad. Sci. USA. 90:1993;2045-2049.
33. Carmichael J., DeGraff W.G., Gazdar A.F., Minna J.D., Mitchell J.B. Evaluation of a tetrazolium-based semiautomated colorimetric assay: assessment of chemosensitivity testing. Cancer Res. 47:1987;936-942.
34. Cohen P. The role of protein phosphorylation in neural and hormonal control of cellular activity. Nature. 296:1982;613-616.
35. Krebs E.G., Beavo J.A. Phosphorylation-dephosphorylation of enzymes. Annu. Rev. Biochem. 48:1979;923-928.
36. Swantek J.L., Cobb M.H., Geppert T.D. Jun N-terminal kinase/stress-activated protein kinase (JNK/SAPK) is required for lipopolysaccharide stimulation of tumor necrosis factor-alpha (TNF-alpha) translation: glucocorticoids inhibit TNF-alpha translation by blocking JNK/SAPK. Mol. Cell. Biol. 17:1997;6274-6282.
37. Nathan C.F. Nitric oxide as a secretory product of mammalian cells. FASEB J. 6:1992;3051-3064.
38. Xie Q., Kashiwabara Y., Nathan C. Role of transcription factor NF-kB/Rel in induction of nitric oxide synthase. J. Biol. Chem. 269:1994;4705-4708.
39. Zhang X., Laubach V.E., Alley E.W., Edwards K.A., Sherman P.A., Russell S.W., Murphy W.J. Transcriptional basis for hyporesponsiveness of the human inducible nitric oxide synthase gene to lipopolysaccharide. J. Leukocyte Biol. 59:1996;575-585.
40. 1 on interleukin-1 production in bovine macrophages. Drug Dev. Res. 24:1991;157-166.
41. 1. Cancer Res. 35:1975;3811-3823.
42. Nose H., Imazeki F., Ohto M., Omata M. p53 Gene mutation and 17p allelic deletion in hepatocellular carcinoma from Japan. Cancer. 72:1993;355-360.
43. Tobias P.S., Soldau K., Kline L., Lee J.D., Kato K., Martin T.P., Ulevitch R.J. Cross-linking of lipopolysaccharide (LPS) to CD14 on THP-1 cells mediated by LPS-binding protein. J. Immunol. 150:1993;3011-3021.
44. Landmann R., Scherer F., Schumann R., Link S., Sansano S., Zimmerli W. LPS directly induces oxygen radical production in human monocytes via LPS binding protein and CD14. J. Leukocyte Biol. 57:1995;440-449.