CD10-activated prodrug compounds

Chemistry: molecular biology and microbiology – Measuring or testing process involving enzymes or... – Involving hydrolase

Reexamination Certificate

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C530S345000

Reexamination Certificate

active

06897034

ABSTRACT:
The compounds of the invention are modified forms of therapeutic agents. A typical prodrug compound of the invention comprises a therapeutic agent, an oligopeptide, a stabilizing group and, optionally, a linker group. The prodrug is cleavable by the CD10 enzyme. Methods of treatment using the prodrug and methods of designing a prodrug are also disclosed.

REFERENCES:
patent: 5599686 (1997-02-01), DeFeo-Jones et al.
patent: 5962216 (1999-10-01), Trouet et al.
patent: 20020103133 (2002-08-01), Copeland et al.
patent: WO 9605863 (1996-02-01), None
patent: WO 9852966 (1998-11-01), None
patent: WO 0033888 (2000-06-01), None
patent: WO 0069472 (2000-11-01), None
DATABASE: GenBank, Acc. No. Y00811, Sep. 12, 1993.
Baraniuk JN, et al., “Identification of neutral endopeptidase mRNA in human nasal mucosa.” J Appl Physiol. Jan 1993;74(1):272-9.
Barker PE, et al., “The common acute lymphoblastic leukemia antigen gene maps to chromosomal region 3 (q21-q27).” J Immunol. Jan. 1, 1989;142(1):283-7.
Bateman RC Jr, et al., “Identification of the active-site arginine in rat neutral endopeptidase 24.11 (enkephalinase) as arginine 102 and analysis of a glutamine 102 mutant.” J Biol Chem. Apr. 15, 1989;264(11):6151-7.
Bricout H, et al., “Synthetic and Kinetic Aspects of Nickel-Catalysed Amination of Allylic Alcohol Derivatives,” Tet. Lett., 54:1073 (1998).
Casey ML, et al., “Progesterone-regulated cyclic modulation of membrane metalloendopeptidase (enkephalinase) in human endometrium.” J Biol Chem. Dec. 5, 1991;266(34):23041-7.
Casimir Jr, et al., “First Application of the Dakin-West Reaction to Fmoc Chemistry: Synthesis of the ketomethylene tripeptide Fmox-Nα-Asp(tBu)-(R,S)Tyr(tBu) ψ(CO-CH2)Gly-OH,” Tet. Lett. 36(27):4797-4800 (1995).
Chaires JB, et al., “Self-association of daunomycin.” Biochemistry. Aug. 17, 1982;21(17):3927-32.
Chu P, and Arber DA. “Paraffin-section detection of CD10 in 505 nonhematopoietic neoplasms. Frequent expression in renal cell carcinoma and endometrial stromal sarcoma.” Am J Clin Pathol. Mar. 2000;113(3):374-82.
Connelly JC, et al., “Neutral endopeptidase 24.11 in human neutrophils: cleavage of chemotactic peptide.” Proc Natl Acad Sci U S A Dec. 1985;82(24):8737-41.
Devault A, et al. “Amino acid sequence of rabbit kidney neutral endopeptidase 24.11 (enkephalinase) deduced from a complementary DNA.” EMBO J. May 1987;6(5):1317-22. Erratum in: EMBO J Aug. 1987;6(8):2506.
Genet J-P, et al., “Practical Palladium-Mediated Deprotective Method of Allyloxycarbonly in Aqueous Media,” Tetrahedron, 50(2):497-503 (1994).
Genet J-P, et al., “A General and Simple Removal of the Allyloxycarbonyl Protecting Group by Palladium-Catalyzed Reactions Using Nitrogen and Sulfur Necleophiles,” Synlett, 680-682 (1993).
Greaves MF, et al., “Selective expression of the common acute lymphoblastic leukemia (gp 100) antigen on immature lymphoid cells and their malignant counterparts.” Blood. Apr. 1983;61(4):628-39.
Hayakawa E, et al., “Viscosity Study on the Self-Association of Doxorubicin in Aqueous Solution,” Chem. Pharm. Bull., 39:1282-6 (1991).
Head JR, et al., “Cellular localizaton of membrane metalloendopeptidase (enkephalinase) in human endometrium during the ovarian cycle.” J Clin Endocrinol Metab. Mar. 1993;76(3):769-76.
Hersh LB, and Morihara K. “Comparison of the subsite specificity of the mammalian neutral endopeptidase 24.11 (enkephalinase) to the bacterial neutral endopeptidase thermolysin.” J Biol Chem. May 15, 1986;261(14):6433-7.
Indig FE, et al., “Investigation of neutral endopeptidases (EC 3.4.24.11) and of neutral proteinases (EC 3.4.24.4) using a new sensitive two-stage enzymatic reaction.” FEBS Lett. Sep. 25, 1989;255(2):237-40. Erratum in: FEBS Lett Feb. 12, 1990;261(1):217.
Kenny, A.J. et al., “Cell surface peptidases,” inMammalian Ectoenzymes, Kenny, A.J. et al. (eds). pp. 169-210 Elsevier, Amsterdam, New York, Oxford (1987).
Kenny, A.J., “Cell surface peptidases are neither peptide- nor organ-specific,” Trends Biochem. Sci. 11:40-42 (1986).
Krongrad A, et al., “Endopeptidase 24.11 activity in the human prostate cancer cell lines LNCaP and PPC-1.” Urol Res. 1997;25(2):113-6.
Letarte M, et al., “Common acute lymphocytic leukemia antigen is identical to neutral endopeptidase.” J Exp Med. Oct. 1, 1988;168(4):1247-53.
Li C, and Hersh LB. “Neprilysin: assay methods, purification, and characterization.” Methods Enzymol. 1995;248:253-63.
Liu AY. “Differential expression of cell surface molecules in prostate cancer cells.” Cancer Res. Jul. 1, 2000;60(13):3429-34.
Malfroy B, et al., “High-affinity enkephalin-degrading peptidase in brain is increased after morphine.” Nature. Nov. 30, 1978;276(5687):523-6.
Matsas R, et al., “The metabolism of neuropeptides. The hydrolysis of peptides, including enkephalins, tachykinins and their analogues, by endopeptidase-24.11.” Biochem J. Oct. 15, 1984,223(2):433-40.
Matzanke BF, et al., “Evidence for polynuclear aggregates of ferric daunomycin. A Mossbauer, EPR, X-ray absorption spectroscopy and magnetic susceptibility study.” Eur J Biochem. Jul. 15, 1992;207(2):747-55.
Pozsgay M, et al., “Substrate and Inhibitor studies of thermolysin-like neutral metalloendopeptidase from kidney membrane fractions. Comparison with bacterial thermolycin.” Biochemistry. Mar. 25, 1986;25(6):1292-9.
Sales, N. et al., “Neutral endopeptidase 24.11 in rat peripheral tissues: comparative localization by ‘ex vivo’ and ‘in vitro’ autoradiography,” Regul. Pept. 33:209 (1991).
Schmittberger T and Waldman H, “Synthesis of the Palmitoylated and Prenylated C-terminal Lipopeptides of the Human R- and N-Ras Proteins,” Bioorg. Med. Chem., 7:749-762 (1999).
Shapiro G, and Buechler D., “Mild and Rapid Azide-Mediated, Palladium Catalyzed Cleavage of Allylester Based Protecting Groups,” Tet. Lett., 35(30):5421-5424 (1994).
Suzuki T, et al., “Imbalance between neutral endopeptidase 24.11 and endothelin-1 expression in human endometrial carcinoma.” Oncology. 2001;60(3):258-67.
Tabrizi-Fard, et al., “Evaluation of the Pharmacokinetic Properties of a Doxorubicin Prodrug in Female ICR (CDI® Mice following intravenous administration.” Proc. American Association for Cancer Research, 42:324 (2001).
Turner, A.J., “Neprilysin” in Handbook of Proteolytic Enzymes, Barrett, A.J. et al, (eds.) Ch. 362, pp. 1080-1085 Academic Press (1998).
Van Der Vijgh WJ, et al., “Comparative metabolism and pharmacokinetics of doxorubicin and 4′-epidoxorubicin in plasma, heart and tumor of tumor-bearing mice.” Cancer Chemother Pharmacol. 1990;26(1):9-12.
Waksman G, et al., “Binding of the bidentate inhibitor [3H]HACBO-Gly to the rat brain neutral endopeptidase “enkephalinase”.” Biochem Biophys Res Commun. Aug. 30, 1985;131(1):262-8.
Weiss LM, et al., “Lymphobalstic lymphoma: an immunophenotype study of 26 cases with comparison to T cell acute lymphoblastic leukemia.” Blood. Feb. 1986;67(2):474-8.
Wong-Leung YL, and Kenny AJ. “Some properties of a microsomal peptidase in rat kidney.” Biochem J. Nov. 1968;110(2):5P.
Zajac JM, et al., “Enkephalin-degrading enzymes and angiotensin-converting enzyme in human and rat meninges.” FEBS Lett. May 25, 1987;216(1):118-22.

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