Compositions and methods for inhibiting abnormal cell growth

Drug – bio-affecting and body treating compositions – Designated organic active ingredient containing – Peptide containing doai

Reexamination Certificate

Rate now

  [ 0.00 ] – not rated yet Voters 0   Comments 0

Details

C530S300000, C530S388300, C435S213000, C524S094000, C514S934000

Reexamination Certificate

active

11076680

ABSTRACT:
In the US about ⅓ of college women show evidence of HPV infection. The clinical problem may be even larger in developing countries. There are currently no effective therapies for HPV infections, aside from therapeutic cone biopsies, which often are followed by recurrent, progressive lesions. Thus, pharmaceutical compositions and processes for treatment of an HPV infection are detailed. In particular, a pharmaceutical composition for inhibiting growth of a human papilloma virus-infected cell is provided which includes a peptide halomethyl ketone inhibitor of a chymotrypsin or chymotrypsin-like protease and a pharmaceutically acceptable carrier. A preferred inhibitor is AAPFcmk.

REFERENCES:
patent: 4518528 (1985-05-01), Rasnick
patent: 4636492 (1987-01-01), Kettner et al.
patent: 6358928 (2002-03-01), Rasnick
Stoppler, et al., Oncogene, 1996, 13, 1545-1548.
Voet, et al., Biochemistry, 1995, John Wiley & sons, Inc., p. 841.
Rapp, et al., Biochimica et Biophysica Acta 1998, 1378, F1-F19.
Oda, et al., Experimental Cell Research, 1996, 226, 164-169.
“Nuclear Scaffold-Associated Protease: In Situ Nuclear Localization and Effects of a Protease Inhibitor on Growth and Morphology of a ras-Transformed Hepatocyte Cell Line,” Gary A. Clawson, Ling Ren, and Harriet C. Isom, Hepatology, vol. 22, No. 4, 1995.
“The Mr 46,000 Nuclear Scaffold ATP-binding Protein: Identification of the Putative Nucleoside Triphosphatase by Proteolysis and Monoclonal Antibodies Directed Against Lamins A/C,” Gary A. Clawson, Yan-Fei Wang, Arnold M. Schwartz, and Christine L. Hatem, Cell Growth and Differentiation, vol. 1, 559-568, Nov. 1990.
“Ca2+=regulated Serine Protease Associated with the Nuclear Scaffold,” Gary A. Clawson, Lauri L. Norbeck, Christine L. Hatem, Cheryl Rhodes, Payman Amiri, James H. McKerrow, Steven R. Patierno, and Gary Fiskum, Cell Growth & Differentiation, vol. 3, 827-838, Nov. 1992.
“An Inhibitor of Nuclear Scaffold Protease Blocks Chemical Transformation of Fibroblasts,” Gary A. Clawson, Lauri L. Norbeck, John P. Wise, and Steven R. Patierno, Cell Growth & Differentiation, vol. 4, 589-594, Jul. 1993.
“Proteolytic Activity Associated with the Nuclear Scaffold—The Effect of Self-Digestion on Lamins,” Zoltan A. Tokes and Gary A. Clawson, J. Biol. Chem., vol. 264, No. 25, Sep. 5, 1989, pp. 15059-15065.
The serine protease inhibitors TLCK and TPCK inhibit the invitro immortalization of primary human keratinocytes by HPV-18 DNA, Hubert Stoppler, Debra Koval and Richard Schlegel, Oncogene (1996) 13, 1545-1548.
“The Serine Protease Inhibitors TLCK and TPCK React with the RB-Binding Core of HPV-18 E7 Protein and Abolish its RB-Binding Capability,” Hubert Stoppler, Melissa Conrad Stoppler, Alexander Adduci, Debra Koval, and Richard Schlegel, Virology 217, 542-553 (1996).
“Proline-Valine Pseudo Peptide Enol Lactones-Effective and Selective Inhibitors of Chymotrypsin and Human Leukocyte Elastase,” Peter E. Reed and John A. Katzenellenbogen, J. Biol. Chem., vol. 266, No. 1, Issue of Jan. 5, 1991, pp. 13-21.
Itoh, Hiroshi, Hiroaki Kataoka, Masamichi Yamauchi, Seiji Naganuma, Yutaka Akiyama, Yoshitsugu Nuki, Takeshi Shimomura, Keiji Miyazawa, Naomi Kitamura, Masashi Koono, “Identification of Hepatocyte Growth Factor Activator Inhibitor Type 2 (HAI-2)-Related Small Peptide (H2RSP): Its Nuclear Localization and Generation of Chimeric mRNA Transcribed from both HAI-2 and H2RSP Genes,” Biochemical and Biophysical Research Communications 288, 390-399 (2001).
Bury, M., Mlynarczuk, I., Pieban, E., Hoser, G., Kawiak, J., and Wojcik, C.; Effects of an inhibitor of tripeptidyl peptidase II (Ala-Ala-Phe-chloromethylketone) and its combination with an inhibitor of the chymotrypsin-like activity of the proteasome (PSI) on apoptosis, cell cycle and proteasome activity in U937 cells. 2001. Folia Histochemica et Cytobiologica 39:131-132.
Geier, E., Preifer, G., et al. A giant protease with potential to substitute for some functions of the proteasome. 1999. Science 283:978-981.
Osmulski, P., Gaczynska, M. A new large proteolytic complex distinct from the proteasome is present in the cytosol of fission yeast. 1998. Curr. Biol. 8:1023-1026.
Hori, H., Nembai, T., Miyata, Y., Hayashi, T., Ueno K., and Koide, T.; Isolation and characterization of two 20S proteasomes from the endoplasmic reticulum of rat liver microsomes. 1999. J. biochem (Tokyo) 126:722-730.
J. Powers, “Haloketone Inhibitors of Proteolytic Enzymes,” in Chemistry and Biochemistry of Amino Acids, Peptides, and Proteins, B. Weinstein (ed.), vol. 4, Marcel-Dekker, NY, 1977, pp. 65-178.

LandOfFree

Say what you really think

Search LandOfFree.com for the USA inventors and patents. Rate them and share your experience with other people.

Rating

Compositions and methods for inhibiting abnormal cell growth does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Compositions and methods for inhibiting abnormal cell growth, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Compositions and methods for inhibiting abnormal cell growth will most certainly appreciate the feedback.

Rate now

     

Profile ID: LFUS-PAI-O-3923347

  Search
All data on this website is collected from public sources. Our data reflects the most accurate information available at the time of publication.