Drug – bio-affecting and body treating compositions – Designated organic active ingredient containing – Peptide containing doai
Reexamination Certificate
2008-07-15
2008-07-15
Gupta, Anish (Department: 1654)
Drug, bio-affecting and body treating compositions
Designated organic active ingredient containing
Peptide containing doai
C514S002600
Reexamination Certificate
active
07399746
ABSTRACT:
The present invention relates to pharmaceutical compositions containing fragments of alpha-1 proteinase inhibitor (API) or chimeric proteins of API and insulin-like growth factor for use in stimulating wound healing.
REFERENCES:
patent: 5093316 (1992-03-01), Lezdey et al.
patent: 5190917 (1993-03-01), Lezdey et al.
patent: 5412073 (1995-05-01), Kalsheker
patent: 6150332 (2000-11-01), Wright et al.
patent: 6638909 (2003-10-01), Grady et al.
patent: 2318732 (1998-06-01), None
P. Brand et al. (2003). “Peripheral deposition of alpha1-protease inhibitor using commercial inhalation devices,” The European Respiratory Journal vol. 22, pp. 263-267.
M.D. Wewers et al. (1987). “Replacement therapy for alpha1-antitrypsin deficiency associated with emphysema,” New England Journal of Medicine vol. 316, pp. 1055-1062.
C. Sandoval et al. (2003). “The fusion of IGF I with stromal cell-derived factor I or alpha1 proteinase inhibitor alters their mitogenic or chemotactic activities which keeping their ability to inhibit HIV-1-gp120 binding,” Biochemical Pharmacology vol. 65, pp. 2055-2063.
C. Sandoval et al. (2002). “Enhanced proliferative effects of a caculovirus-produced fusion protein of insulin-like growth factor and alpha1-proteinase inhibitor and improved anti-elastase activity of the inhibitor with glutamate at position 351,” Protein Engineering vol. 15, pp. 413-418.
Congote et al., The C-terminal 26-residue peptide of serpin A1 stimulates proliferation of breast and liver cancer cells:role of protein kinase C and CD47, 2004, FEBS letters, v576, 343-347.
Catanese et al., Oppossum serum alpha-1 proteinase inhibitor, 1993, Biochemistry, v32, 509-515.
Merck on-line manual (www.merck.com/mmhe) 'alpha-1 antitrypsin deficiency entry accessed 2007, 2 pages.
Crisp et al., “Roles of the Heparin and Low Density Lipid Receptor-related Protein-binding Sites of Protease Nexin 1 (PN1) in Urokinase-PN1 Complex Catabolism”, J. Biol. Chem. 2000.
Cullen et al., “Mechanism of action of PROMOGRAN, a protease modulating matrix, for the treatment of diabetic foot ulcers”, Wound Repair and Regeneration 2002 10(1):16-25.
Dabbagh et al., “Alpha-1-Antitrypsin Stimulates Fibroblast Proliferation and Procollagen Production and Activates Classical MAP Kinase Signalling Pathways”, J. Cell. Physiol. 2001 186(1):73-81.
Galiano et al., “Interaction between the Insulin-like Growth Factor Family and the Integrin Receptor Family in Tissue Repair Processes”, J. Clin. Invest. 1996 98(11):2462-2668.
Johansson et al., “Identification of hydrophobic fragments of α1-antitrypsin and C1 and protease inhibitor in human bile, plasma and spleen”, FEBS 1992 299(2):146-148.
Ledoux-Corbusier et al., “α1-Antitrypsin Deficiency and Skin Abnormalities”, J. Cutan. Pathol. 1975 2(1):25-29.
Loots et al., “Fibroblasts derived from chronic diabetic ulcers differ in their response to stimulation with EGF, IGF-1, bFGF and PDGF-AB compared to controls”, Eur. J. Cell Biol. 2002 81(3):153-160.
Nwomeh et al., “Physiology of the Chronic Wound”, Clinics in Plastic Surgery 1998 25(3):341-356.
Rao et al., “α1-Antitrypsin Is Degraded and Non-Functional in Chronic Wounds But Intact and Functional in Acute Wounds:The Inhibitor Protects Fibronectin from Degradation by Chronic Wound Fluid Enzymes”, J. Invest. Dermatol. 1995 105(4):572-578.
Sandoval et al., “Enhanced proliferative effects of a baculovirus-produced fusion protein of insulin-like growth factor and α1-proteinase inhibitor and improved anti-elastase activity of the inhibitor with glutamate at position 351”, Protein Engineering 2002 15(5):413418.
Sandoval et al., “The fusion of IGF I with stromal cell-derived factor I or α1 proteinase inhibitor alters their mitogenic or chemotactic activities while keeping their ability to inhibit HIV-1-gp120 binding”, Biochemical Pharmacology 2003 65:2055-2063.
Schwede et al., “Swiss-Model:an automated protein homology-modeling server”, Nucleic Acids Research 2003 31(13):3381-3385.
Stockley et al., “Effect of Alpha-1-Proteinase Inhibitor on Neutrophil Chemotaxis”, Am. J. Respir. Cell Mol. Biol. 1990 2:163-170.
Wachter et al., “Treatment of atopic dermatitis with alpha1-proteinase inhibitor”, Annals of Allergy 1992 69(5):407414.
Gupta Anish
Licata & Tyrrell PC
McGill University
Niebauer Ronald T
LandOfFree
Agents for wound healing does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Agents for wound healing, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Agents for wound healing will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-2809469