Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Hydrolase
Reexamination Certificate
2005-02-15
2005-02-15
Prouty, Rebecca E. (Department: 1652)
Chemistry: molecular biology and microbiology
Enzyme , proenzyme; compositions thereof; process for...
Hydrolase
C424S094670
Reexamination Certificate
active
06855532
ABSTRACT:
This invention relates to newly identified polypeptides which have zinc metalloprotease activities and are referred to as IGS5, and polynucleotides encoding such polypeptides, to their use in therapy and in identifying compounds which may be stimulators and/or inhibitors which are useful in therapy, and to production of such polypeptides and polynucleotides.
REFERENCES:
patent: 5965425 (1999-10-01), Barr et al.
patent: 6548284 (2003-04-01), Matsuo et al.
patent: 20020086405 (2002-07-01), Silos-Santiago et al.
patent: 20020102707 (2002-08-01), Harrow et al.
patent: 20020177689 (2002-11-01), Benson et al.
patent: 20030119714 (2003-06-01), Naylor et al.
patent: 2260376 (1999-02-01), None
patent: 1069188 (2001-01-01), None
patent: 1 275 733 (2003-01-01), None
patent: 1 308 459 (2003-05-01), None
patent: WO 9953 077 (1999-10-01), None
patent: WO 0047750 (2000-08-01), None
patent: WO 0136 610 (2001-05-01), None
patent: WO 0183 782 (2001-11-01), None
patent: WO 0206 492 (2002-01-01), None
patent: WO 0208 396 (2002-01-01), None
patent: WO 0226 958 (2002-04-01), None
patent: WO 0247 670 (2002-06-01), None
patent: WO 0294 176 (2002-11-01), None
patent: WO 0340 393 (2003-05-01), None
patent: WO 0351 370 (2003-06-01), None
Bonvouloir N. et al., Molecular cloning, Tissue Distribution, and Chromosomal localization of MMEL2, a Gene Coding for a Novel Human Member of the Neutral Endopeptidase-24.11 Family, DNA and Cell Biology, 2001, 20, 493-498.*
Raharjo et al., “Alternative splicing regulates the endoplasmic reticulum localization or secretion of soluble secreted endopeptidase”J. Biol. Chem. Jul. 6, 2001; 276(27):25612-20. Epub May 7, 2001.
Ikeda et al., “Molecular identification and characterization of novel membrane-bound metalloprotease, the soluble secreted form of which hydrolyzes a variety of vasoactive peptides”.J. Biol. Chem. Nov. 5, 1999; 274 (45) :32469-77.
Beaumont, A. et al, Evidence that both arginine 102 and arginine 747 are involved in substrate binding to neutral endopeptidase (EC 3.4.24.11) (1991)J. Biol. Chem. 266, pp. 214-220.
Beynon, R. et al., “Characterization of the soluble, secreted form of urinary meprin”Biochem. J. (1996) 315, pp. 461-466.
Bollen, A-M. et al. “Purification and characterization of a soluble endopeptidase from rat bone” (1991) Calcif Tissue Int., 48(2), pp. 111-119.
Costa, E. et al. “Opioid peptide biosynthesis: enzymatic selectivity and regulatory mechanisms” (1987) FASEB 1(1), pp. 16-21.
Crine, P. et al. “Endopeptidase-24.11” Cell-Surface Peptidases in Health and Disease, Chapter 6, A.J. Kenny and C.M. Boustead, eds. (1997), pp. 79-98, BIOS Scientific Publishers, Oxford.
Crine, P. et al. The production and characterization of a monoclonal antibody specific for the 94,000 dalton enkephalin-degrading peptidase from rabbit kidney brush border.Biochem. Biophy. Res. Commun. (1985) 131, pp. 255-261.
Devault, A. et al. Exploration of the catalytic site of endopeptidases 24.11 by site directed mutagensis.FEBS Lett. (1988) 231, pp. 54-58.
Dion, N. et al. Kinetic evidence that the His-711 of neutral endopeptidase 24.11 is involved in stabilization of the transition state.FEBS Lett. (1993) 318, pp. 301-304.
Dion, N. et al. “Evidence that Asn542 of neprilysin (EC 3.4.24.11) is involved in binding of the P2residue of substrates and inhibitors”Biochem. J. (1995). 311, pp. 623-627.
Facchinetti, P. et al. “Ontogeny, regional and cellular distribution of the novel metalloprotease neprilysin 2 in the rat: a comparison with neprilysin and endothelin-converting enzyme-1”Neuroscience(2003) 118(3), pp. 627-639.
Ghaddar, G. et al. “Molecular cloning and biochemical characterization of a new mouse testis soluble-zine-metallopeptidase of the neprilysin family”Biochem. J. (2000) 347(Pt.2) pp. 419-429.
Glucksman, M. et al. “Strategies for characterizing, cloning, and expressing soluble endopeptidases” (1995)Methods in Neurosciences23, pp. 296-316.
Hooper, N. “Families of zinc metalloproteases” (1994)FEBS Lett. 354, pp. 1-6.
Le Moual, H. et al. Identification of glutamic acid 646 as a zinc-coordinating residue in endopeptidase-24.11. (1991)J. Biol. Chem. 266, pp. 15670-15674.
Le Moual, H. et al. Asp650 is crucial for catalytic activity of neutral endopeptidase 24-11. (1994)Eur. J. Biochem. 221, pp. 475-480.
Marie-Claire, C. et al. Evidence by site-directed mutagenesis that arginine 203 of thermolysin and arginine 717 of neprilysin (neutral endopeptidase) play equivalent critical roles in substrate hydrolysis and inhibitor binding. (1997)Biochemistry36, pp. 13938-13945.
Orlowski, M. et al. “A soluble metalloendopeptidase from rat brain. Purification of the enzyme and determination of specificity with synthetic and natural peptides” (1983)Eur. J. Biochem. 135(1) pp. 81-88.
Orlowski, M. et al. “Purification and specificity of a membrane-bound metalloendopeptidase from bovine pituitaries” (1981)Biochemistry20(17) pp. 4942-4950.
Roques, B. “Zinc metallopeptidases: Active site structure and design of selective and mixed inhibitors: New approaches in the search for analgesics and anti-hypertensives” (1993)Biochemical Society Transactions21(3) pp. 678-685.
Rose, C. et al. “Cell-specific activity of neprilysin 2 isoforms and enzymic specificity compared with neprilysin” (2002)Biochem. J. 363(Pt3) pp. 697-705.
Shirotani, K. et al. “Neprilysin degrades both amyloid β peptides 1-40 and 1-42 most rapidly and efficiently among thiorphan- and phosphoramidon-sensitive endopeptidases”J. Biol. Chem. (2001) 276(24) pp. 21895-21901.
Sohar, I. et al. “Soluble metalloendopeptidase (MMP-7ase) activity in mouse kidney cytosol” (1991)Acta Biol Hung, 42(1-3) 265-274.
Tanja, O. et al. “Neprilysin II: A putative novel metalloprotease and its isoforms in CNS and testis” Biochem Biophys Res Commun. May 2000 271(3) pp. 565-570. Erratum in: Biochem Biophys Res Commun. Aug. 2000, 275(1) pp. 247.
Vida, T. et al. “Glycosylation variants of endopeptidase-24.11 (‘Enkephalinase’)” (1992) Neuropeptides 21(4) pp. 245-255.
Deleersnijder Willy
Weske Michael
Wiegers Rico
Crowell & Moring LLP
Prouty Rebecca E.
Solvay Pharmaceuticals B.V.
Walicka M
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