Cooperation of protein disulfide isomerase and redox environment in the regulation of NF-κB and API binding to DNA

Cell Biochemistry and Function

Volumn 14, Issue 1, 1996, Pages 49-55

  Clive, Diana R ^a   Greene, James J ^a,b  

^a CATHOLIC UNIVERSITY OF AMERICA   (United States)

^b VIRGINIA COMMONWEALTH UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

API; Electromobility shift assay; NF B; Protein disulfide isomerase; Redox state

Indexed keywords

IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; OXIDOREDUCTASE; PROTEIN DISULFIDE ISOMERASE; TRANSCRIPTION FACTOR;

ARTICLE; BINDING SITE; CONTROLLED STUDY; ELECTROPHORETIC MOBILITY; ENZYME ACTIVITY; ENZYME PURIFICATION; GENE EXPRESSION; HUMAN; HUMAN CELL; OXIDATION REDUCTION POTENTIAL; OXIDATION REDUCTION STATE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DNA BINDING; SIGNAL TRANSDUCTION;

ADAPTOR PROTEIN COMPLEX 1; ADAPTOR PROTEIN COMPLEX ALPHA SUBUNITS; ADAPTOR PROTEINS, VESICULAR TRANSPORT; CELL EXTRACTS; CELL NUCLEUS; DNA, NEOPLASM; DNA-BINDING PROTEINS; ELECTROPHORESIS; FIBROSARCOMA; GLUTATHIONE; GLUTATHIONE DISULFIDE; HELA CELLS; HUMANS; ISOMERASES; MEMBRANE PROTEINS; NF-KAPPA B; OXIDATION-REDUCTION; PROTEIN DISULFIDE-ISOMERASE; SENSITIVITY AND SPECIFICITY; TRANSCRIPTION FACTORS; TUMOR CELLS, CULTURED;

EID: 0030020153     PISSN: 02636484     EISSN: None     Source Type: Journal    
DOI: 10.1002/cbf.638     Document Type: Article

References (21)

1. Kulesh, D. A. and Greene, J. J. (1986). Shape-dependent regulation of proliferation in normal and malignant human cells and its alteration by Interferon. Cancer Res., 46, 2793-2797.
2. Kulesh, D. A , Clive, D. R., Zarlenga, D. S. and Greene, J. J. (1987). Identification of interferon-modulated proliferation-related cDNA sequences. Proc. Natl. Acad. Sci. U.S.A., 84, 8453-8457.
3. Clive, D. R. and Greene, J. J. (1994). Association of protein disulfide isomerase activity and the induction of contact-inhibition. Exp. Cell Res.. 214, 139-144.
4. Staal, F. J. T., Roederer, M., Herzenberg, L. A. and Herzenberg, L. (1990). Intracellular thiols regulate activation of nuclear factor κB and transcription of human immunodeficiency virus. Proc. Natl. Acad. Sci. U.S.A., 87, 9943-9947.
5. Toledano, M. B. and Leonard, W. J. (1991). Modulation of transcript factor NF-κB binding activity by oxidation-reduction in vitro. Proc. Natl. Acad. Sci. U.S.A., 88, 4328-4332.
6. Abate, C., Patel, L., Rauscher III, F. J. and Curran, T. (1990). Redox regulation of fos and jun DNA-binding activity in vitro. Science, 249, 1157-1161.
7. Xanthoudakis, S., Miao, G., Pan, Y. C.E. and Curran, T. (1992). Redox activation of fos-jun DNA binding activity is mediated by a DNA repair enzyme. EMBO J., 11, 3323-3335.
8. McBride, A. A., Klausner, R. D. and Howley, P. M. (1992). Conserved crysteine residue in the DNA-binding domain of the bovine papillomavirus type 1 E2 protein confers redox regulation to the DNA-binding activity in vitro. Proc. Natl. Acad. Sci. U.S.A., 89, 7531-7535.
9. Fisher, R. J., Koizumi, S., Kondoh, A., Mariano, J. M., Mavrothalassitis G., Bhat, N. K. and Papas, T. S. (1992). Human ETS1 oncoprotein. J. Biol. Chem., 267, 17957-17965.
10. Hwang, C., Sinskey, A. J. and Lodish, H. F. (1992). Oxidized redox state of glutathione in the endoplasmic reticulum. Science, 257, 1496-1502.
11. Tsuchida, S. and Sato, K. (1992). Glutathione transferases and cancer. CRC Crit. Rev. Biochem. Molec. Biol., 27, 337-384.
12. Prestera, T., Zhang, Y., Spencer, S. R., Wilczak, C. A. and Talalay, P. (1993). The electrophile counterattack response: protection against neoplasia and toxicity. Adv. Enzyme Regul., 33, 281-296.
13. Atzori, L., Dypbukt, J. M., Sundqvist, K., Cotgreave, I., Edman, C. C., Moldeus, P., and Grafstrom, R. C. (1990). Growth-associated modifications of low-molecular-weight thus and protein sulfhydryls in human bronchial fibroblasts. J. Cell. Physiol., 143, 165-171.
14. Lyles, M. M. and Gilbert, H. F. (1991). Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: dependence of the rate on the composition of the redox buffer. Biochemistry, 30, 613-619.
15. Weissman, J. S. and Kim, P. S. (1993). Efficient catalysis of disulphide bond rearangements by protein disulphide isomerase. Nature, 365, 185-188.
16. Schreiber, E., Matthais, P., Muller, M. M. and Schaffner, W. (1991). Rapid detection of octomer binding proteins with 'mini-extracts', prepared from a small number of cells Nucl Acids Res., 17, 6419-6424.
17. Bradford, M. (1976). A rapid and sensitive method for the quantitation of protein utilizing the principle of protein-dye binding. Anal. Biochem., 72, 248-252.
18. Hayashi, T., Ueno, Y. and Okamoto, T. (1993). Oxidoreductive regulation of nuclear factor kappa B. Involvement of a cellular reducing catalyst thioredoxin. J. Biol. Chem., 268, 11380-11388.
19. Matthews, J. R., Wakasugi, N., Virelizier, J. L., Yodoi, J. and Hay, R. T. (1992). Thioredoxin regulates the DNA binding activity of NF-kappa B by reduction of a disulphide bond involving cysteine 62. Nucl Acids Res., 20, 3821-3830.
20. Schenk, H., Klein, M., Erdbrugger, W., Droge, W. and Schulze-Osthoff, K. (1994). Distinct effects of thioredoxin and antioxidants on the activation of transcription factors NF-κB and AP-1. Proc. Natl. Acad. Sci. U.S.A., 91, 1672-1676.
21. Lewin, B. (1991). Oncogenic conversation by regulatory changes in transcription factors. Cell, 64, 303-312.