Chemistry: molecular biology and microbiology – Maintaining blood or sperm in a physiologically active state...
Patent
1995-06-07
1999-01-19
Weber, Jon P.
Chemistry: molecular biology and microbiology
Maintaining blood or sperm in a physiologically active state...
435206, 514 2, A01N 102, C12N 936, A61K 3803
Patent
active
058612386
ABSTRACT:
The present invention is directed to methods for partitioning advanced glycosylation endproducts out of a biological sample using the unexpected discovery that certain antibacterial proteins, in particular lysozyme and particular fragments thereof, bind to advanced glycosylation endproducts (AGEs) with high affinity, and that this binding activity is substantially noncompetitive with binding of bacterial carbohydrates to the antibacterial proteins. Accordingly, the invention relates to therapeutic methods for treating diseases and disorders associated with increased levels of AGEs, by using compositions having associated therewith a molecule having a hydrophilic loop domain, which domain is associated with AGE-binding activity, and compositions comprising such a domain to remove AGEs from biological material. The invention further relates to compositions and devices for partitioning AGEs away from a sample.
REFERENCES:
Yang et al. (1991) J. Exp. Med., 174, "Two Novel Rat Liver Membrane Proteins that Bind Advanced Glycosylation Endproducts: Relationship to Macrophage Receptor for Glucose-Modified Proteins", pp. 515-524.
Schmidt et al. (1992) J. Biol. Chem., 267(21), "Isolation and Characterization of Two Binding Proteins for Advanced Glycosylation End Products from Bovine Lung Which are Present on the Endothelial Cell Surface", pp. 14987-14997.
Neeper et al. (1992) J. Biol. Chem., 267(21), "Cloning and Expression of a Cell Surface Receptors for Advanced Glycosylation End Products of Proteins", pp. 14998-15004.
Vlassara et al. (1994) Lab. Invest., 20(2), "Pathogenic Effects of Advanced Glycosylation: Biochemical, Biologic, and Clinical Implications for Diabetes and Aging", pp. 138-151.
Schmidt et al. (1994a) J. Biol. Chem., 269(13), "The Endothelial Cell Binding Site for Advanced Glycation End Products Consists of a Complex: An Integral Membrane Protein and a Lactoferrin-Like Polypeptide", pp. 9882-9888.
Khoury et al. (1994) J. Biol. Chem., 269(14), "Macrophages Adhere to Glucose-Modified Basement Collagen IV via Their Scavenger Receptors", pp. 10197-10200.
Schmidt et al. (1994b) Artheriosclerosis and Thrombosis, 14(10), "Cellular Receptors for Advanced Glycation End Products: Implications for Induction of Oxidant Stress and Cellular Dysfunction in the Pathogenesis of Vascular Lesions", pp. 1521-1528.
Schmidt et al. (1994c) Proc. Nat. Acad. Sci. USA, 97(19), "Receptor for Advanced Glycation End-products (Ages) Has a Central Role In-vessel Wall Intraactions and Gene Activation in Response to Circulating age Proteins", pp. 8807-8811.
Li et al. (1995) Nature Medicine 1:1057-61.
Schmidt et al. (1995) Nature Medicine 1:1002-4.
Taylor et al. (1995) Clin. Exp. Immunol. 102:406-16.
Moshchin'ski et al. (1990) Lab Delo (USSR)(6):57-60 (Medline Abstract).
Moszczyniski et al. (1990) Pol. Arch. Med. Wewn. (Poland) 83(4-6):194-9 (Medline Abstract).
Thompson et al. (1990) J. Lab. Clin. Med. 115:148-58 (Medline Abstract).
Wagnerova et al. (1988) J. Hyg. Epidemiol. Microbiol. Immunol. (Czechoslovakia) 32(3):265-72 (Medline Abstract).
Olson et al. (1985) J. Dent. Res. 64(5):826-30 (Medline Abstract).
Wagnerova et al. (1986) Czech. Med. 9(4):210-7 (Medline Abstract).
Wagner et al. (1987) Czech. Med. 10(2):70-8 (Medline Abstract).
Moszczyniski, P. (1992) Wiad. Lek. (Poland) 45(4-6):180-4 (Abstract).
Moszczyniski et al. (1991) Gig. Tr. Prof. Zabol. (USSR) 3:34-6 (Abstract).
Moszczyniski et al. (1991 Pneumonol. Alergol. Pol. (Poland) 59:17-21 (Medline Abstract).
Knibbs et al. (1993) J. Biol. Chem. 268:140940-7.
Cerami Anthony
Li Yong Ming
Vlassara Helen
The Picower Institute for Medical Research
Weber Jon P.
LandOfFree
Methods for partitioning advanced glycosylation endproducts does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Methods for partitioning advanced glycosylation endproducts, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Methods for partitioning advanced glycosylation endproducts will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-1245624