Drug – bio-affecting and body treating compositions – Designated organic active ingredient containing – Peptide containing doai
Reexamination Certificate
2003-10-29
2008-08-05
Kam, Chih-Min (Department: 1656)
Drug, bio-affecting and body treating compositions
Designated organic active ingredient containing
Peptide containing doai
C530S350000, C424S094630, C435S226000
Reexamination Certificate
active
07407933
ABSTRACT:
The medicine containing angiotensin-converting enzyme or its peptidase-inactivated mutants that specifically releasing GPI-anchored proteins from the cell surface, for preventing or curing diseases, such as prion-related diseases, inflammatory diseases, bacterial infectious diseases and male infertility due to sperm-egg binding insufficiency.
REFERENCES:
patent: 2001-316287 (2001-11-01), None
patent: 91/00354 (1991-01-01), None
patent: 95/32725 (1995-12-01), None
Sen et al. , J. Biol. Chem. 268, 25748-25754 (1993).
Chemical Abstract, 1995, vol. 123, Abstract No. 330713, abstract & A. Israel et al., “Angiotensin II receptor subtypes and phosphoinositide hydrolysis in rat adrenal modulla”, Brain Research Bulletin, 1995, vol. 38, No. 5, pp. 441-446.
Chemical Abstract, 1993, vol. 118, Abstract No. 252487, abstract & M. Raizada et al., “Increased angiotensin II type-1 gene expression in neuronal cultures from spontaneously hypertensive rats”, 1993, vol. 132, No. 4, pp. 1715-1722.
Chemical Abstract, 1989, vol. 113, Abstract No. 126431, abstract & A. J. Robinson-White et al., “Inhibition of inositol phospholipid hydrolysis in endothelial cells by pentobarbital”, European J. Pharmacol., Molecular Pharmacology Section, 1989, vol. 172, No. 3, pp. 291-303.
G. Kondoh et al., “Angiotensin-converting enzyme is a GPI-anchored protein releasing factor crucial for fertilization”, Nature Medicine, vol. 11, No. 2, pp. 160-166, Feb. 2005.
H. Kondo, “Mouse Seishoku Saibo GPI Anchor-gata Tanpakushitsu Yuri Inshi no Tanri to Kino Kaiseki” Seishoku Saibo no Seigyo Kiko to Hassei Kogaku, Heisei 11-14, Nendo, No. 11234101, pp. 69-72, (2003), English translation.
E. Jaspard et al., “Differences in the properties and enzymatic specificities of the two active sites of angiotensin I-converting enzyme (kininase II). Studies with bradykinin and other natural peptides”, J. Biol. Chem., 1993, vol. 268, No. 13, pp. 9496-9503.
L. Wei et al., “The two homologous domains of human angiotensin I-converting enzyme are both catalytically active”, J. Biol. Chem., 1991, vol. 266, No. 14, pp. 9002-9008.
L. Wei et al., “The two homologous domain of human angiotensin I-converting enzyme interact differently with competitive inhibitors”, J. Biol. Chem., 1992, vol. 267, No. 19, pp. 13398-13405.
S. Pang et al., “Roles of the juxtamembrane and extracellular domains of angiotensin-converting enzyme in ectodomain Shedding”, Biochem. J., 2001, vol. 358, (Pt 1), pp. 185-192.
B. Maric et al., “Replacement of the transmembrane anchor in angiotensin I-converting enzyme (ACE) with a glycosylphosphatidylinositol tail affects activation of the B2 bradykinin receptor by ACE inhibitors”, J. Biol. Chem., 2000, vol. 275, No. 21, pp. 16110-16118.
S. Pang et al., “The ectodomain of angiotensin converting enzyme does not dictate sensitivity to sacretase cleavage”, Biochemical Society transactions, 2000, vol. 28, No. 5, p. A262.
Kam Chih-Min
Wenderoth , Lind & Ponack, L.L.P.
LandOfFree
Drug containing angiotensin convertase does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Drug containing angiotensin convertase, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Drug containing angiotensin convertase will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-3998644