Organic compounds -- part of the class 532-570 series – Organic compounds – Carbohydrates or derivatives
Reexamination Certificate
2000-10-18
2003-05-20
McGarry, Sean (Department: 1635)
Organic compounds -- part of the class 532-570 series
Organic compounds
Carbohydrates or derivatives
C536S024300, C536S024310, C536S024330, C435S006120, C435S091100, C435S325000, C435S375000
Reexamination Certificate
active
06566514
ABSTRACT:
BACKGROUND OF THE INVENTION
1. Field of the Invention
This invention relates to oligonucleotides that are complementary to the thioredoxin and thioredoxin reductase genes which modulate tumor cell growth in mammals. This invention is also related to methods of using such compounds in inhibiting the growth of tumor cells in mammals. This invention also relates to pharmaceutical compositions comprising a pharmaceutically acceptable excipient and an effective amount of a compound of this invention.
References
The following publications, patent applications and patents are cited in this application as superscript numbers:
1. Holmgren, “Enzymatic reduction-oxidation of protein disulfide by thioredoxin”
Methods Enzymol
107:295-300 (1984)
2. Wright and Anazodo, “Antisense Molecues and their potential for the treatment of cancer and AIDS”
The Cancer Journal
4:185-189 (1995)
3. Matthew et al., “Thioredoxin regulates the DNA binding activity of NF-Kappa B by reduction of a disulphide bond involving cysteine 62
Nucleic Acids Res
. 20:3821-3830 (1992)
4. Bannister et al., “In vitro DNA binding activity of Fos/Jun and BZLF1 but not C/EBP is affected by redox changes”
Oncogene
6:1243-50 (1991)
5. Cromlish and Roeder “Human transcription factor IIIC (TFIIIC)”
J. Biol. Chem
. 264:18100-9 (1989)
6. Abate et al., “Redox regulation of fos and jun DNA-binding activity in vitro”
Science
249:1157-1161 (1990)
7. Tagaya et al., “ATL-derived factor (ADF), an IL-2 receptor/Tac inducer homologous to thioredoxin: possible involvement of dithiol-reduction in the Il-2 receptor induction
EMBO J
. 8:757-64 (1989)
8. Powis et al., “The thioredoxin/thioredoxin reductase redox system and control of cell growth”
Oncol. Res
. 6:53944 (1994)
9. Oblong et al., “Site directed mutagenesis of active site cysteines in human thioredoxin produces competitive inhibitors of human thioredoxin reductase and elimination of mitogenic properties of thioredoxin
J. Biol. Chem
. 269:11714-20 (1994)
10. Gasdaska et al. “Cell growth stimulation by the redox protein thioredoxin occurs by a novel helper mechanism”
Cell Growth Differ
6:1643-1650 (1995)
11. Gasdaska et al., “The predicted amino acid sequence of human thioredoxin is identical to that of the autocrine growth factor human adult T-cell derived factor (ADF); thioredoxin mRNA is elevated in some human tumors”
Biochem Biophys. Acta
1218:292-296 (1994)
12. Berggren et al., “Thioredoxin and thioredoxin reductase gene expression in human tumors and cell lines and the effects of serum stimulation and hypoxia”
Anticancer Res
. 16:3459-3466 (1996)
13. Fujii et al., “Coexpression of adult T-cell leukemia-derived factor, a human thioredoxin homologue and human papillomavirus DNA in neoplastic cervical squamous epithelium”
Cancer
68:1583-91 (1991)
14. Kawahara et al., “Enhanced coexpression of thioredoxin and high mobility group protein 1 genes in human hepatocellular carcinoma and the possible association with decreased sensitivity to cisplatin”
Cancer Res
. 56:5330-3 (1996)
15. Gallegos et al., “Transfection with human thioredoxin increases cell proliferation and a dominant-negative mutant thioredoxin reverses the transformed phenotype of human breast cancer cells”,
Cancer Res
. 56:5765-70 (1996)
16. Baker et al., “Thioredoxin, a gene found overexpressed in human cancer, inhibits apoptosis in vitro and in vivo”
Cancer Res
. 57:5162-7 (1997)
17. Mau and Powis, “Inhibition of cellular thioredoxin reductase by diaziquinone and doxorubicin. Relationship to the inhibition of cell proliferation and decreased ribonucleotide reductase activity”
Biochem Pharmacol
43: 1621-7 (1992)
18. Mau and Powis, “Mechanism-based inhibition of thioredoxin reductase by antitumor quinoid compounds”
Biochem Pharmacol
43: 1613-20 (1992)
19. Schallreuter and Wood, “New aspects in the pathophysiology of cutaneous melanoma: a review of the role of thioproteins and the effect to nitrosoureas”
Melanoma Res
. 1:159-167 (1991)
20. Schallreuter and Wood, “The stereospecific suicide inhibition of human melanoma thioredoxin reductase by 13-cis-retinoic acid”
Biochem Biophys. Res. Commun
. 160:573-9 (1989)
21. Curcio et al., “Oligonucleotides as modulators of cancer gene expression”
Pharmacol Ther
. 74:317-32 (1997)
22. Narayanan and Akhtar, “Antisense therapy”
Curr Opin. Oncol
. 8:509-15 (1996)
23. Remington's Pharmaceutical Sciences, Mace Publishing Company, Philadelphia, Pa. 17
th
ed. (1985)
24. Sambrook et al.,
Molecular Cloning: A Laboratory Manual
, Cold Spring Harbor Laboratory, New York (1989, 1992)
25. Ausubel et al.,
Current Protocols in Molecular Biology
, John Wiley and Sons, Baltimore, Md. (1989)
26. Perbal,
A Practical Guide to Molecular Cloning
, John Wiley & Sons, New York (1988)
27. Hurta and Wright, “Malignant transformation by H-ras results in aberrant regulation of ribonucleotide reductase gene expression by transforming growth factor-beta”
J. Cell Biochem
57:543-556 (1995)
28. Tagaya et al., “ATL-derived factor (ADF) an IL-2-receptor/Tac inducer homologous to thioredoxin: possible involvement of dithiol-reduction in the IL-2 receptor induction”
EMBO J
. 13:2244 (1994)
29 Choy et al., “Molecular mechanisms of drug resistance involving ribonucleotide reductase: hydroxyurea resistance in a series of clonally related mouse cell lines selected in the presence of increasing drug concentrations”
Cancer Res
. 48:2029-2035 (1988)
30. Fan et al., “Ribonucleotide reductase R2 component is a novel malignancy determinant that cooperates with activated oncogenes to determine transformation and malignant potential”
Proc. Natl. Acad. Sci USA
93:14036-40 (1996)
31. Huang and Wright, “Fibroblast growth factor mediated alterations in drug resistance and evidence of gene amplification”
Oncogene
9:491499 (1994)
32. Gasdaska et al., “Cloning and sequencing of a human thioredoxin reductase”
FEBS Letters
373:5-9 (1995)
29. Nielsen et al.;
Science
(1991) 354:1497
30. Good and Nielsen; “Inhibition of translation and bacterial growth by peptide nucleic acid targeted to ribosomal RNA”,
PNAS USA
(1998) 95:2073-2076
31. Buchardt, deceased, et al., U.S. Pat. No. 5,766,855
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33
34. Altschul, et al. “Basic local alignment search tool”,
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35. Devereux J. et al., “A comprehensive set of sequence analysis programs for the VAX”,
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36. Chang et al.
36
; Somatic Gene Therapy, CRC Press, Ann Arbor, Mich. (1995);
37. Vega et al.
37
; Gene Targeting
, CRC Press, Ann Arbor, Mich. (1995)
38
. Vectors: A Survey of Molecular Cloning Vectors and Their Uses
, Butterworths, Boston, Mass. (1988)
39. Sullivan 1994, U.S. Pat. No. 5,225,347
40. U.S. Pat. No. 5,023,252 issued Jun. 11, 1991
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All of the above publications, patent applications and patents are herein incorporated by reference in their entirety to the same extent as if each individual publication, patent application or patent was specifically and individually indicated to be incorporated by reference in its entirety.
2. State of the Art
Thioredoxin is a small ubiquitous redox protein originally identified as a reducing cofactor for ribonucleotide reductase which is essential for DNA synthesis
1
. Thioredoxin and thioredoxin reductase comprise the thioredoxin system. Thioredoxin reductase is a selenocysteine containing flavoenzyme which uses NADPH as a proton donor to reduce thioredoxin which in turn reduces other proteins and therefore influences their functions.
In recent years, mammalian thioredoxin has been implicated in a variety of other biochemical pathways. For example, it modulates redox properties of transcription factors by dithiol disulfide exchanges, which alter their DNA binding characteristics. Transcription factors such as NF-&kgr;B
3
, BZLFI
4
and TFIIIC
5
are directly regulated, while AP-1 activation is mediated indirectly through the nuclear redox
Lee Yoon S.
Wright Jim A.
Young Aiping H.
GeneSense Technologies Inc.
Goldberg Joshua B.
Juneau Todd L.
Lacourciere Karen A
McGarry Sean
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