Drug – bio-affecting and body treating compositions – Designated organic active ingredient containing – Having -c- – wherein x is chalcogen – bonded directly to...
Reexamination Certificate
1992-02-10
2001-08-07
Goldberg, Jerome D. (Department: 1614)
Drug, bio-affecting and body treating compositions
Designated organic active ingredient containing
Having -c-, wherein x is chalcogen, bonded directly to...
C514S211070
Reexamination Certificate
active
06271242
ABSTRACT:
BACKGROUND OF THE INVENTION
It is presently known that many human diseases are caused at least in part by proteins present in the cells of the afflicted individual. For example, certain proteins encoded by oncogenes are known to be responsible for the production of cancer in humans.
Included among these oncogenes is the oncogene designated as trk. The trk locus was originally identified by virtue of its activation as an oncogene in various human tumors (Martin-Zanca, D., et al. (1986).
Nature
, 319, 743-748). Subsequent studies revealed that the corresponding normal gene, the trk proto-oncogene, encodes a 790 amino acid-long cell surface receptor with intrinsic tyrosine protein kinase activity [(Martin-Zanca, D., et al. (1989).
Mol. Cell. Biol
., 9, 24-33)]. This protein, designated gp140
trk
, binds nerve growth factor (NGF) with high affinity, either by itself (Klein, R., et al. (1991).
Cell
, 65, 189-197) or in combination with a second NGF receptor, p75
LNGFR
(Hempstead, B. L., et al. (1991),
Nature
, 350, 678-683). Accumulative evidence indicates that gp
140
trk
mediates the functional activity of NGF. NGF induces the rapid autophosphorylation of gp140
trk
on tyrosine residues, a step necessary to activate the receptor and to initiate the flow of signal transduction (Kaplan, D. R., et al. (1991).
Nature
, 350, 158-160; Kaplan, D. R., et al. (1991).
Science
, 252, 554-558; Klein, R., et al. (1991).
Cell
, 65, 189-197). Moreover, addition of NGF to NIH3T3 cells ectopically expressing gp140
trk
receptors induces the transient expression of c-Fos protein, DNA synthesis and morphologic transformation (Cordon-Cardo, C., et al. (1991).
Cell
, 66, 173-183). Similarly, addition of NGF to Xenopus oocytes microinjected with trk proto-oncogene mRNA induces germinal vesicle breakdown (Nebreda, A. R., et al. (1991).
Science
, 252, 558-561). Finally, transfection of NGF-unresponsive PC12 cells with a trk cDNA clone restores the ability of these mutant cells to respond to NGF (Loeb, D. M., et al. (1991).
Cell
, 66, 961-966).
Neoplasia is a process by which the controlling mechanisms that regulate cell growth and differentiation are impaired, resulting in progressive growth. During neoplasia, there is a characteristic failure to control cell turnover and growth. This lack of control causes a tumor to grow progressively, enlarging and occupying space in vital areas of the body. If the tumor invades surrounding tissue and is transported to distant sites, death of the individual often results.
The preferential killing of cancer cells while minimizing deleterious effects on normal cells is the desired goal in cancer therapy. In the past this has been accomplished using a variety of procedures. These procedures include the administration of chemicals (chemotherapy), radiation (radiotherapy), and surgery.
Recently there has been a rapid expansion of cancer treatments. Even though new treatments are being developed, the need still exists for improved methods for the treatment of most types of cancers.
SUMMARY OF THE INVENTION
In accordance with the present invention, a novel method for preventing, stabilizing or causing the regression of cancer caused in whole or part by a tyrosine protein kinase is disclosed. The method comprises the administration of a therapeutically effective amount of a tyrosine protein kinase inhibitor to a mammalian species in need of such treatment.
As used in the present application, the term “cancer” is used in its broadest sense and includes tumors, neoplasms, carcinomas, sarcomas, leukemias, lymphomas and the like.
As used in the present application, the term “tyrosine protein kinase inhibitor” means a substance which is able to prevent or reduce the ability of a tyrosine protein kinase enzyme to catalyze a phosphorylation reaction.
The phrase “stabilizing” cancer as used in the present application refers to slowing down the development of and/or inhibiting the formation of new cancerous lesions.
The phrase “causing the regression of” cancer as used in the present application refers to reducing and/or eliminating cancerous lesions.
REFERENCES:
patent: 62/155284 (1987-07-01), None
T. Toaka et al., Biochemical and Biophysical Research Communication, vol. 170, No. 3, pp. 1151-1156, 1990.
M. M. Berg et al., The Journal of Biological Chemistry, vol. 267, No. 1, pp. 13-16, 1992.
G. Powis et al., Clinical Biochemistry, vol. 24, pp. 385-397, 1991.
S. Akinaga et al., Cancer Chemotherapy and Pharmacology, vol. 29, No. 4, pp. 266-272, 1992.
Patent Abstracts of Japan, vol. 13, No. 442 (C-641) (3790), Oct. 4, 1989.
Elliot, L.H. et al., Biochem. Biophys. Res. Commun. 171, 148-154 (1990). “K252a is a Potent and SElective Inhibitor of Phosphorylase Kinase.”
Hashimoto, S., J. Cell. Biol., 107, 1531-1539 (1988). “K-252a, a Potent Protein Kinase Inhibitor, Blocks Nerve Growth Factor-induced Neurite Outgrowth and Changes in the Phosphorylation of Proteins in PC12h Cells.”
Koizumi, S. et al., J. Neurosci., 8, 715-721 (1988). “K-252a: A specific Inhibitor of the Action of Nerve Growth Factor on PC12 Cells.”
Nakanishi, S. et al., J. Antibiot., 39, 1066-1071 (1986). “K-252b, .c and D, Potent Inhibitors of Protein Kinase C From Microbial Origin.”
Nakanishi, S. et al., J. Biol. Chem., 263, 6215-6219 (1988). “K-252a, a Novel Microbial Product, Inhibits Smooth Muscle Myosin Light Chain Kinase.”
Ruegg, U.T. and Burgess, G.M., Trends Pharmacol. Sci., 10, 218-220 (1989). “Staurosporine, K-252 and UCN-01: potent but nonspecific inhibitors of protein kinases.”
Lazarovici, B. et al., J. Neurosci. Res., 23, 1-8 (1989). “K-252a Inhibits the Increase in c-fos Transcription and the Increase in Intracellular Calcium Produced by Nerve Growth Factor in PC12 Cells.”
Geissler, J.F. et al., J. Biol. Chem. 265, 22255-22261, (1990). “Thiazolidine-Diones.”
Meyer, T. et al., INt. J. Cnacer 43, 851-856 (1989). “A derivative of Staurosporine (CGP 41 251) Shows Selectivity For Protein Kinase C Inhibition and In Vitro Anti-Proliferative as Well as In Vivo Anti-Tumor Activity.”
Kase, H. et al., Biochem. and Biophys. Res. Comm. 142, 436-440 (1987). “K-252 Compounds, Novel and Potent Inhibitors of Protein Kinase C and Cyclic Nucleotide-Dependent Protein Kinases.”
Fujita-Yamaguchi, Y. and Satish, K., Biochem. and Biophys. Res. Comm., 157, 955-962 (1988). “Characterization of Recepotr Tyrosine-Specific Protein Kinases By The Use of Inhibitors. Staurosporine Is A 100-Times More Potent Inhibitor of Insulin Receptor Than IGF-1 Receptor.”
Nakano, H. et al., J. of Antibiotics 5, 706-708 (1987). “Staurosporine Inhibits Tyrosine-Specific Protein Kinase Activity of Rous Sarcoma Virus Transforming Protein p60.”
Kase, H. et al., J. of Antibiotics 8, 1059-1065 (1986). “K-252a, A Potent Inhibitor of Protein Kinase C From Microbial Origin.”
Tomaoki, T. et al., Biochem. and Biophys. Res. Comm. 135, 397-402 (1986). “Staurosporine, A Potent Inhibitor of Phospholipid/CA++Dependent Protein Kianse.”
Bristol-Myers Squibb Co.
Gaul Timothy J.
Goldberg Jerome D.
Klein Christopher A.
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