Method for reducing the viscosity of pathological mucoid airway

Drug – bio-affecting and body treating compositions – Designated organic active ingredient containing – Peptide containing doai

Patent

Rate now

  [ 0.00 ] – not rated yet Voters 0   Comments 0

Details

514 12, 514851, 514826, 514958, 424 941, 530350, 530324, 530325, 530326, 530327, 530328, 530329, 530330, 435 681, 435183, C12N 900, C07K 1400, C07K 700

Patent

active

054648173

ABSTRACT:
The invention is generally directed to methods of promoting normal respiratory tract airflow in subjects with restricted airflow and ciliary clearance caused by the presence of pathological airway contents, and particularly mucoid contents. Actin-binding proteins are administered into the respiratory tract of a subject with a pathological respiratory condition involving the presence of such contents. The actin-binding protein binds to actin polymers in the contents and decreases the viscosity. The actin binding proteins also prevent actin from binding to exogenous or endogenous DNase, thus increasing the degradation of DNA polymers in the contents.

REFERENCES:
Hubbard et al. 1992 New Engl. J. Med. 326:812-815.
Way et al. 1988 J. Mol. Biol. 203: 1127-1133.
Vasconcellos et al. 1994 Science 263:969-971.
Lieberman 1968 JAMA 205:114-115.
Smith et al. 1985 Clinical Research 33: 472A.
Van Vaelen et al. 1980 J. Biol. Chem. 255:2270-2272.
Chaponnier et al. 1986 J. Cell Biol. 103:1473-1481.
Aitken et al., Recombinant human DNase inhalation in normal subjects and patients with cystic fibrosis, JAMA 267:1947-1951 (1992).
Andre et al., Severin, gelsolin, and villin share a homologous sequence in regions presumed to contain F-actin severing domains, J. Biol. Chem. 263:722-727 (1988).
Bryan, Gelsolin h as three actin-binding sites, J. Cell Biol. 106:1553-1562 (1988).
Chaponnier et al., Reversibility of gelsolin/actin interaction in macrophages, J. Exp. Med. 165:97-106 (1987).
Cooke et al., Serum vitamin D-binding protein is a third member of the albumin and alpha fetoprotein gene family, J. Clin. Invest. 76:2420-2424 (1985).
Cooper et al., Microinjection of gelsolin into living cells, J. Cell Biol. 104:491-501 (1987).
Coue et al., Effects of serum vitamin-D-binding protein on actin in the presence of the plasma gelsolin, Eur. J. Biochem. 160:273-277 (1986).
Goldschmidt-Clermont et al., Proportion of circulating Gc (vitamin D-binding protein) in complexed form: relation to clinical outcome in fulminant hepatic necrosis, Gastroenterology 94:1454-1458 (1988).
Haddad et al., Angiopathic consequences of saturating the plasma scavenger system for actin, Proc. Natl. Acad. Sci. USA 87:1381-1385 (1990).
Harper et al., G-actin infusions: plasma vitamin D binding protein protects against endothelial damage and intra-vascular filament formation, Clin. Res. 36:625A (1988).
Janmey, Mechanical properties of cytoskeletal polymers, Curr. Opin. Cell Biol. 2:4-11 (1991).
Janmey et al., Effects of semi-dilute actin solutions on the mobility of fibrin protofibrils during clot formation, Biochim. Biophys. Acta 841:151-158 (1985).
Janmey et al., Capacity of human serum to depolymerize actin filaments, Blood 70:524-530 (1987).
Janmey et al., Modulation of gelsolin function by phospatidylinositol-4,5-biphosphate, Nature 325: 362-364 (1987).
Janmey et al., Polyphosphonositide micelles and polyphosphoinositide-containing vesicles dissociate endogenous gelsolin-actin complexes and promote actin assembly from the fast-growing end of actin filaments blocked by gelsolin, J. Biol. Chem. 262:12228-12236 (1987).
Janmey et al., Viscoelasticity of F-actin and F-actin/gelsolin complexes, Biochem. 27:8218-8227 (1988).
Janmey et al., Effects of actin filaments on fibrin clot structure and lysis, Blood 80:928-936 (1992).
Kwiatkowski et al., Isolation and properties of two actin-binding domains in gelsolin, J. Biol. Chem. 260:15232-15238 (1985).
Kwiatkowski et al., Plasma and cytoplasmic gelsolins are encoded by a single gene and contain a duplicated actin-binding domain, Nature 323:455-458 (1986).
Kwiatkowski et al., Muscle is the major source of plasma gelsolin, J. Biol. Chem. 263:8239-8243 (1988).
Kwiatkowski et al., Genomic organization and biosynthesis of secreted and cytoplasmic forms of gelsolin, J. Cell Biol. 106:375-384 (1988).
Kwiatkowski et al., Identification of critical functional and regulatory domains in gelsolin, J. Cell Biol. 108:1717-1726 (1989).
Lazarides et al., Actin is the naturally occurring inhibitor of deoxyribonuclease I, Proc. Natl. Acad. Sci. USA 71:4742-4746 (1974).
Lind et al., Human plasma gelsolin binds to fibronectin, J. Biol. Chem. 259:13262-13266 (1984).
Lind et al., Role of plasma gelsolin and the vitamin D-binding protein in clearing actin from the circulation, J. Clin. Invest. 78:736-742 (1986).
Lind et al., Depression of gelsolin levels and detection of gelsolin-actin complexes in plasma of patients with acute lung injury, Am. Rev. Respir. Dis. 138:429-434 (1988).
Matsudaira et al., Pieces in the actin-severing protein puzzle, Cell 54:139-140 (1988).
Peitsch et al., Characterization of the endogenous deoxyribunuclease involved in nuclear DNA degradation during apoptosis (programmed cell death), The EMBO Journal 12:371-377 (1993).
Pollard et al., Actin and actin-binding proteins. A critical evaluation of mechanisms and functions, Ann. Rev. Biochem. 55:987-1035 (1986).
Scarborouugh et al., Aggregation of platelets by muscle actin. A multivalent interaction model of platelet aggregation by ADP, Biochem. Biophys. Res. Commun. 100:1314-1319 (1981).
Shak et al., Recombinant human DNase I reduces the viscosity of cystic fibrosis sputum, Proc. natl. Acad. Sci. USA 87:9188-9192 (1990).
Smith et al., Circulating actin-gelsolin complexes following oleic acid-induced lung injury, Am. J. Path. 130:261-267 (1988).
Smith et al., Decreased plasma gelsolin levels in patients with Plasmodium falciparum malaria: a consequence of hemolysis?, Blood 72:214-218 (1988).
Stossel et al., Nonmuscle actin-binding proteins, Ann. Rev. Cell Biol. 1:353-402 (1985).
Stossel, The actin system and the rheology of peripheral cytoplasma, Biorheology 23:621-631 (1986).
Way et al., Expression of human plasma gelsolin in Escherichia coli and dissection of actin binding sites by segmental deletion mutagensis, J. Cell Biol. 109:593-605 (1989).
Yang et al., Human group-specific component (Gc) is a member of the albumin family, Proc. Natl. Acad. Sci. USA 82:7994-7998 (1985).
Yin et al., Actin filament servering by gelsolin, J. Cell Biol. 107:465a (1988).
Yin et al., Identification of a polyphosphoinositide-modulated domain in gelsolin which binds to the sides of actin filaments, J. Cell Biol. 106:805-812 (1988).
Young et al., Correlation between extent of liver damage in fulminant hepatic necrosis and complexing of circulating group-specific component . . . , J. Lab. Clin. Med. 110:83-90 (1987).

LandOfFree

Say what you really think

Search LandOfFree.com for the USA inventors and patents. Rate them and share your experience with other people.

Rating

Method for reducing the viscosity of pathological mucoid airway does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Method for reducing the viscosity of pathological mucoid airway , we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Method for reducing the viscosity of pathological mucoid airway will most certainly appreciate the feedback.

Rate now

     

Profile ID: LFUS-PAI-O-197260

  Search
All data on this website is collected from public sources. Our data reflects the most accurate information available at the time of publication.