Use of c-Src and c-Fos Knockout Mice for the Studies on the Role of c-Src Kinase Signaling in the Expression of Toxicity of TCDD

Journal of Biochemical and Molecular Toxicology

Volumn 12, Issue 5, 1998, Pages 263-274

  Enan, Essam ^a   Dunlap, Debra Y ^a   Matsumura, Fumio ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

2,3,7,8 TETRACHLORODIBENZO PARA DIOXIN; AROMATIC HYDROCARBON RECEPTOR; BENZOQUINONE DERIVATIVE; CYTOCHROME P450; ENZYME INHIBITOR; GELDANAMYCIN; GROWTH FACTOR RECEPTOR; MACROCYCLIC LACTAM; PROTEIN TYROSINE KINASE; PROTEIN TYROSINE KINASE C SRC; PROTEIN-TYROSINE KINASE C-SRC; QUINONE DERIVATIVE; THYROID HORMONE RECEPTOR;

ADIPOSE TISSUE; ANIMAL; ARTICLE; BIOSYNTHESIS; COMPARATIVE STUDY; DRUG ANTAGONISM; DRUG EFFECT; ENZYME INDUCTION; ENZYMOLOGY; GENETICS; LIVER; METABOLISM; MOUSE; MOUSE MUTANT; ONCOGENE; ONCOGENE SRC; PATHOLOGY; SIGNAL TRANSDUCTION; SRC HOMOLOGY DOMAIN; THYMUS;

ADIPOSE TISSUE; ANIMALS; BENZOQUINONES; CYTOCHROME P-450 ENZYME SYSTEM; ENZYME INDUCTION; ENZYME INHIBITORS; GENES, FOS; GENES, SRC; LACTAMS, MACROCYCLIC; LIVER; MICE; MICE, KNOCKOUT; PROTEIN-TYROSINE KINASES; QUINONES; RECEPTORS, ARYL HYDROCARBON; RECEPTORS, GROWTH FACTOR; RECEPTORS, THYROID HORMONE; SIGNAL TRANSDUCTION; SRC HOMOLOGY DOMAINS; TETRACHLORODIBENZODIOXIN; THYMUS GLAND;

EID: 0031626981     PISSN: 10956670     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1099-0461(1998)12:5<263::AID-JBT2>3.0.CO;2-J     Document Type: Article

References (41)

1. F. Matsumura, E. Enan, D. Y. Dunlap, K. E. Pinkerton, and J. Peake (1997). Altered in vivo toxic expression of 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) in src-deficient mice. Biochem. Pharmacol., 53, 1599-1612.
2. E. Enan and F. Matsumura (1996). Identification of c-src as the integral component of the cytosolic Ah receptor complex, transducing the signal of 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) through the protein phosphorylation pathway. Biochem. Pharmacol., 52, 1599-1612.
3. R. E. Tucker, A. L. Young, and A. P. Gray (eds.) (1982). Human and Environmental Risks of Chlorinated Dioxins and Related Compounds, pp. 1-823, Plenum Press, New York.
4. A. Poland and R. D. Kimbrough (eds.) (1984). Biological Mechanisms of Dioxin Action. Banbury Report 18, p. 500, Cold Spring Harbor Laboratory, Cold Spring Harbor, New York.
5. H. I. Swanson and C. A. Bradfield (1993). The Ah-receptor: genetics, structure and function. Pharmacogenetics, 3, 213-230.
6. C. J. Elferink and J. P. Whitlock Jr. (1989). 2,3,7,8-Tetrachlorodibenzo-p-dioxin inducible Ah receptor-mediated binding of enhancer DNA. J. Biol. Chem., 265, 5718-5721.
7. F. Matsumura, D. W. Brewster, B. V. Madhukar, and D. W. Bombick (1984). Alteration of rat hepatic plasma membrane functions by 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD). Arch. Environ. Contam. Toxicol., 13, 509-515.
8. F. Matsumura (1994). How important is the protein phosphorylation pathway in the toxic expression of dioxin-type chemicals? Biochem. Pharmacol., 48, 215-224.
9. src. J. Biochem. Toxicol., 2, 141-154.
10. E. Enan and F. Matsumura (1995). Evidence for a second pathway in the action mechanism of TCDD: significance of Ah-receptor mediated activation of protein kinase under cell-free conditions. Biochem. Pharmacol., 49, 249-261.
11. J. A. Cooper (1990). The src family of protein tyrosine kinases. In Peptides and Protein Phosphorylation, B. E. Kemp, ed., pp. 85-113, CRC Press, Boca Raton, FL.
12. H. R. Herschman (1991). Primary response genes induced by growth factors and tumor promotors. Annu. Rev. Biochem., 60, 281-319.
13. B. F. Boyce, H. Chen, P. Soriano, and G. R. Mundy (1993). Histomorphomethric and immunocytochemical studies of src-related osteopetrosis. Bone, 14, 335-340.
14. J. A. Bruege and S. D. Aust (1978). Microsomal lipid peroxidation. Methods in Enzymology S. Fleischer and L. Packer, eds., vol. 52, pp. 302-310, Academic Press, New York.
15. H. Ashida, E. Enan, and F. Matsumura (1996). Protective action of dehydrascorbic acid on the Ah receptor dependent and independent induction or lipid peroxidation in adipose tissue of male guinea pig caused by TCDD administration. J. Biochem. Toxicol., 11, 269-279.
16. S. W. Cushman and L. J. Wardzala (1980). Potential mechanism of insulin action on glucose transport in the isolated rate adipose cell: apparent translocation of intracellular transport systems to the plasma membrane. J. Biol. Chem., 255, 4758-4762.
17. I. D. Dignam, R. M. Lebovitz, and R. A. Roeder (1983). Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei. Nucleic. Acid Res., 11, 1475-1489.
18. M. Marselos and V. Vasiliou (1991). Effect of various chemicals on the aldehyde dehydrogenase activity of the rat liver cytosol. Chem. Biol. Interactions, 79, 79-89.
19. L. Ernster (1967). DT diaphorase. Meth. Enzymol., 10, 309-317.
20. A. R. Temple, A. K. Dane, and M. S. Clement (1971). Studies of glucuronidation III. The measurement of p-nitrophenyl. J. Lab. Clin. Med., 77, 1015-1019.
21. S. W. Kennedy, S. P. Jones, and L. J. Bastien (1995). Efficient analysis of cytochrome P4501A catalytic activity. Porphorins and total proteins in chick embryo hepatocyte cultures with a fluorescence plate reader. Analyt. Biochem., 266, 362-370.
22. R. A. Aiyer and B. B. Aggrawal (1990). Characterization of receptors for recombinant human tumor necrosis factor λ from human placental membranes. Lymphokine Res., 9, 333-344.
23. M. J. Duclos and C. Goddard (1990). Insulin-like growth factor's receptors in chicken liver membranes: binding properties, specificity, developmental pattern and evidence for a single receptor type. J. Endocrinol., 125, 199-206.
24. M. Romkes and S. Safe (1988). Comparative activities of 2,3,7,8-tetrachlorodibenzo-p-dioxin and progesterone as antiestrogens in the female rat uterus. Toxicol. Appl. Pharmacol., 92, 368-380.
25. B. Charpentier, J. M. Bernardon, J. Eustache, C. Millais, B. Martin, S. Michel, and B. Shroot (1995). Synthesis, structure-affinity relationships, and biological activities of ligands binding to retinoic acid receptor subtype. J. Med. Chem., 38, 4993-5006.
26. A. H. Cavanaugh and S. Simons Jr. (1994). Factor-assisted DNA binding as a possible general mechanism for steroid receptors. Functional heterogeneity among activated receptor-steroid complex. J. Steroid Biochem. Molec. Biol., 48, 433-466.
27. P. M. Yen, J. H. Brubaker, J. W. Apriletti, J. D. Baxter, and W. W. Chin (1994). Role of 3,5,3′-triiodothyronine and deoxyribonucleic acid binding on thyroid hormone receptor complex formation. Endocrinology, 134, 1075-1081.
28. H. Gjille, M. Kortenjann, O. Thomas, C. Moomaw, C. Slaughter, M. Cobb, and P. E. Shaw (1995). ERK phosphorylation potentiates EIK1-mediated ternary complex formation and transactivation. EMBO J., 14, 951-962.
29. B. Derijard, M. Hibi, I. H. Wu, T. Barrett, B. Su, T. Deng, M. Karin, and R. T. Davis (1994). JNK1: a protein kinase stimulated by UV light and Ha-ras that binds and phosphorylates the c-Jun activation domain. Cell, 76, 1025-1037.
30. P. L. Stein, H. Vogel, and P. Soriano (1994). Combined deficiencies of src, fyn and yes tyrosine kinases in mutant mice. Genes Developm., 8, 1999-2007.
31. H. Yamaki (1995). Inhibition of the association with nuclear matrix of PRB, p70 and p40 proteins along with the specific suppression of c-Myc expression by geldanamycin, an inhibitor of Src kinase. J. Antibiotics, 48, 1021-1026.
32. K. Bonham and D. J. Fujita (1993). Organization and analysis of the promoter region and 5′-non-coding exons of the human c-src proto-oncogene. Oncogene, 8, 1973-1981.
33. T. Dorai, L. B. Levy, L. Kang, J. S. Brugge, and L. H. Wang (1983). Analysis of cDNA of the proto-oncogene c-Src: Heterogeniety in 5′exons and possible mechanism for the genesis of the 3′-end of v-src. Molec. Cell Biol., 11, 4165-4176.
34. T. Takeya and H. Hanafusa (1983). Structure and sequence of the cellular gene homologous to the RSV src gene and the mechanism for generating the transforming virus. Cell, 32, 881-890.
35. W. F. Greenlee, T. R. Sutter, and C. Marcus (1994). Molecular basis of dioxin actions on rodent and human target tissues. Progr. Clinic. Biol. Res., 387, 47-57.
36. D. C. Lee, K. D. Barlow, and K. W. Gaido (1996). The Actions of 2,3,7,8-tetrachlorodibenzo-p-dioxin on transforming growth factor beta 2 promoter activity are localized to the TATA box binding region and controlled through a tyrosine kinase dependent pathway. Toxicol. Appl. Pharmacol., 137, 90-99.
37. D. R. Stover, M. Becker, J. Liebetanz, and N. B. Lydon (1995). Src phosphorylation of the epidermal growth factor receptor at novel sites mediates receptor interaction with Src and p85 alpha. J. Biol. Chem., 270, 15591-15597.
38. T. Parson (1995). Protein modules and signalling network. Nature, 373, 573-580.
39. src Mediated phosphorylation of connexin 43, a gap junction protein. J. Biol. Chem., 270, 12751-12761.
40. T. R. Polte and S. K. Hanks (1997). Complexes of focal adhesion kinase (FAK) and CrK-associated substrate (p 130cas) are elevated in cytoskeltone-associated fractions following adhesion and src transformation. J. Biol. Chem., 272, 5501-5509.
41. T. David-Pfeuty, S. Bagrodia, and D. Shalloway (1993). Differential localization patterns of myristoylated and nonmyristoylated c-src proteins in interphase and mitotic c-src overexpressed cells. J. Cell Sci., 105, 613-628.