Method for inactivating gonadotrophs

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

C514S014800, C530S313000, C530S328000, C530S402000

Reexamination Certificate

active

06924268

ABSTRACT:
Certain toxic compounds (T) such as, for example, compounds based upon diphtheria toxin, ricin toxin, pseudomonas exotoxin, α-amanitin, pokeweed antiviral protein (PAP), ribosome inhibiting proteins, especially the ribosome inhibiting proteins of barley, wheat, corn, rye, gelonin and abrin, as well as certain cytotoxic chemicals such as, for example, melphalan and daunomycin can be conjugated to certain analogs of gonadotropin-releasing hormone to form a class of compounds which, when injected into an animal, destroy the gonadotrophs of the animal's anterior pituitary gland. Hence such compounds may be used to sterilize such animals and/or to treat certain sex hormone related diseases.

REFERENCES:
patent: 4081533 (1978-03-01), Cheesman
patent: 4201770 (1980-05-01), Stevens
patent: 4302386 (1981-11-01), Stevens
patent: 4400376 (1983-08-01), Sanderson
patent: 4444759 (1984-04-01), Rivier et al.
patent: 4526716 (1985-07-01), Stevens
patent: 4652550 (1987-03-01), Rivier et al.
patent: 4691006 (1987-09-01), Stevens
patent: 4713366 (1987-12-01), Stevens
patent: 4767842 (1988-08-01), Stevens
patent: 4863857 (1989-09-01), Blalock et al.
patent: 5169933 (1992-12-01), Anderson et al.
patent: 5378688 (1995-01-01), Nett et al.
patent: 5488036 (1996-01-01), Nett et al.
patent: 5492893 (1996-02-01), Nett et al.
patent: 5631229 (1997-05-01), Nett et al.
patent: 5786457 (1998-07-01), Nett et al.
patent: 6103881 (2000-08-01), Nett et al.
patent: 6214969 (2001-04-01), Janaky et al.
patent: 6326467 (2001-12-01), Nett et al.
patent: 91 10 4730 (1991-03-01), None
patent: 2185486 (1987-07-01), None
patent: WO 90/09799 (1990-09-01), None
Bacha et al., “Organ-Specific Binding of a Thyrotropin-Releasing Hormone-Diphtheria Toxin Complex after Intravenous Administration to Rats”, pp. 1072-1076, 1983,Endocrinology, vol. 113.
Bacha et al., Systemic Toxicity of Diphtheria Toxin-Related Fragments (CRM26, CRM45), a Hormone-Toxin Hybrid Protein (TRH-CRM45), and Ricin A1(42234), pp. 131-138, 1986,Proc. Soc. Exp. Biol. Med., vol. 181.
Bacha et al., “Thryotropin-Releasing Hormone-Diphtheria Toxin-Related Polypeptide Conjugates; Potential Role of the Hydrophobic Domain in Toxin Entry”. pp. 1565-1570,J. Biol Chem., vol. 258, Feb.
Bajusz et al., Proc. Nat'l, Acad. Sci, vol. 86, pp. 6318-6322 (Aug., 1989).
Bourdon et al., “The Potential of Monoclonal Antibodies as Carriers of Radiation and Drugs for Immunodetection and Therapy of Brain Tumors”, pp. 79-101, 1984,Prog. Exp. Tumor Res.,vol. 28.
Cawley et al., “Epidermal Growth Factor-Toxin A Chain Conjugates: EGF-Ricin A is a Potent Toxin While EGF-Diphtheria Fragment A is Nontoxic”, pp. 563-570, 1980,Cell, vol. 22, Nov.
Chang et al., “Artificial Hybrid Protein Containing a Toxin Protein Fragment and a Cell Membrane Receptor-Binding Moiety in a Disulfide Conjugate”, pp. 1515-1522, 1977,J. Biol. Chem., vol. 252, Feb.
Chaudhary et al., “Activity of a Recombinant Fusion Protein Between Transforming Growth Factor Type α andPseudomonasToxin”, pp. 4538-4542, 1987,Proc. Natl. Acad. Sci. USA, vol. 84, Jul.
Colombatti et al.,“Cloned Fragment of Diphtheria Toxin Linked to T Cell-specific Antibody Indentifies Regions of B Chain Active in Cell Entry”, pp. 3030-3035, 1986J. Biol. Chem., vol. 261, Mar.
Greenfield et al., “Mutations in Diphtheria Toxin Separate Binding from Entry and Amplify Immunotoxin Selectivity”, pp. 536-539, 1987,Science, vol. 238, Oct.
E. Gross and J. Heienhofer (eds), Peptides, Proceedings of the Sixth American Pept. Symposium, pp. 803-806.
Meyers et al., “Specific Chemical Cleavage of Diphtheria Toxin With Hydroxylamine”, pp. 17122-17127, 1988,J. Biol. Chem., vol. 263, No. 32, Nov.
Murphy et al., “Genetic Construction, Expression, and Melanoma-Selective Cytotoxicity of a Diphtheria Toxin-Related α-Melanocyte-Stimulating Hormone Fusion Protein”, pp. 8258-8262, 1986Proc. Natl. Acad. Sci. USA, vol. 83, Nov.
Myers, “Hybrid Toxins: An Approach to Cell Specific Toxicity”, 1987, Dissertation submitted to the Division of Animal Science and the Graduate School of the University of Wyoming, Laramie, Wyoming.
Myers D.A., et al., “Protein-Peptide Conjugation by a Two-Phase Reaction”, p. 343, 1985,Biochem J., 227:1.
Oeltmann et al., “A Hybrid Protein Containing the Toxic Subunit of Ricin and the Cell-Specific Subunit of Human Chorionic Gonadotrophin”, pp. 1028-1032, 1979,J. Biol. Chem., vol. 4, Feb.
Oeltmann, “Synthesis andIn VitroActivity of a Hormone-Diphtheria Toxin Fragment of a Hybrid”, pp. 430-435, 1985,Biochem Biophys. Res. Commun., vol. 133, Dec.
Pastan et al., “Immunotoxins”, pp. 641-648, 1986,Cell, vol. 47, Dec.
Pineda M.H. et al., “Atrophy of Rabbit Testes Associated with Production of Antiserum to Bovine Luteinizing Hormone”, pp. 665-668, 1967,Proc. Soc. Exp. Bio. Med., vol. 125, No. 3, Jul.
Quadri S.K. et al., “Inhibition of Spermatogenesis and Ovulation in Rabbits with Antiovine LH Rabbit Serum”, pp. 809-814, 1966,Proc. Soc. Exp. Biol. Med., vol. 123.
Schwartz et al., “A New Cytotoxin Specific for the Target Cells of Corticotrophin-Releasing Factor”, pp. 1454-1460, 1987,Endocrinology, vol. 121.
Singh et al., “Controlled Release of LHRH-DT From Bioerodible Hydrogel Microsphers”, pp. R5-R8, 1976International Journal of Pharmacology.
Szepeshazi et al., Anti-Cancer Drugs, 3 109-116 (1992).
Tallgat M. et al., “Impairment of Spermatogenesis and Libido Through Antibodies to Luteinizing Hormone”, pp. 113-118, 1971,Fertility and Sterility, vol. 22, No. 2, Feb.
Vitetta et al., “Redesigning Nature's Poisons to Create Anti-Tumor Reagents”, pp. 1098-1104, 1987,Science, vol. 238, Nov.
Youle, et al., “Immunotoxins Show Rapid Entry of Diphtheria Toxin but not Ricin via the T3 Antigen”, pp. 93-98, 1986,J. Immunol., vol. 136, Jan.
CRC of Chemistry of Protein Conjugation and Cross-Linking, pp. 58, 152-160, 189, 267-285, 288-293.
Youle, et al., “Cytotoxic Ribonucleases and Chimeras in Cancer Therapy”,Crit. Rev. in Therapeutic Drug Carrier Systems, 10(1), pp. 1-28 (1993).
Conn et al., “Gonadotrophin-Releasing Hormone and its Analogues”,The New England J. of Med., pp. 93-103, Jan., 1991.

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

Method for inactivating gonadotrophs does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Method for inactivating gonadotrophs, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Method for inactivating gonadotrophs will most certainly appreciate the feedback.

Rate now

     

Profile ID: LFUS-PAI-O-3471915

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