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- Nachgewiesen in: USPTO Patent Grants
- Sprachen: English
- Patent Number: 7,368,546
- Publication Date: May 06, 2008
- Appl. No: 10/348304
- Application Filed: January 21, 2003
- Assignees: The Board of Regents of the University of Nebraska (Lincoln, NE, US)
- Claim: 1. An isolated nucleic acid molecule, said molecule encoding an SAA3 protein wherein said nucleic acid molecule comprises a nucleotide sequence comprising the sequence set forth in SEQ ID NO: 1 that encodes a protein with the biological activity of said SAA3 protein.
- Claim: 2. A vector comprising the nucleic acid molecule of claim 1 .
- Claim: 3. A host cell transformed with the vector of claim 2 .
- Claim: 4. The host cell of claim 3 wherein said host cell is a bacterial cell.
- Claim: 5. The host cell of claim 3 wherein said host cell is an animal cell.
- Claim: 6. The host cell of claim 5 , wherein said animal cell is from a Homo sapien.
- Claim: 7. The host cell of claim 5 wherein said animal cell is a mammary cell.
- Claim: 8. A nucleotide construct comprising: a nucleic acid molecule of claim 1 , wherein said nucleic acid molecule is operably linked to a promoter that drives expression in a host cell.
- Claim: 9. The isolated nucleic acid molecule of claim 1 wherein said SAA3 biological activity is stimulation of mucin 3 (MUC3) production in mammary epithelial cells.
- Current U.S. Class: 536/231
- Patent References Cited: 4377569 March 1983 Plymate ; 4425330 January 1984 Norcross et al. ; 4755380 July 1988 Grubb ; 4952496 August 1990 Studier ; 5227301 July 1993 Turner et al. ; 5536640 July 1996 Sipe et al. ; 5585098 December 1996 Coleman ; 5700465 December 1997 Tao et al. ; 5807684 September 1998 Simmons et al. ; 5853985 December 1998 Salbaum ; 5952313 September 1999 Carlson ; 5958883 September 1999 Snow ; 6004936 December 1999 Kisilevsky ; 6013857 January 2000 Deboer ; 0872 558 October 1998 ; 1 067 194 January 2001 ; WO/95/21625 August 1995 ; WO/97/04317 February 1997 ; WO/97/06184 February 1997 ; WO/98/03206 January 1998 ; WO/98/40506 September 1998 ; WO/99/18227 April 1999 ; WO 01 14580 March 2001 ; WO/01/31006 March 2001
- Other References: Bowie, et al. Science, 247: 1306-10, 1990. cited by examiner ; Skolnick et al. TIBTECH 18:34-39, 2000. cited by examiner ; Bauman, H., et al., “The acute phase response”, IT Review, 1994 Elsevier Science Ltd., 0167-5699/94. cited by other ; Benson, M. Douglas, “A unique insertion in the primary structure of bovine amyloid AA protein” J. Lab Clin Med., vol. 113:67-72, 1989. cited by other ; Hirvonen, Juhani, et al, “Acute phase response in heifers with experimentally induced mastitis” Journal of Dairy Research (1996) 63 352-360. cited by other ; Hulten, C., et al., “The acute phase serum amyloid A protein (SAA) in the horse: isolation and characterization of three isoforms”, Veterinary Immmunology and Immunopathology 57(1997) 215-227. cited by other ; Huszenicza, Gy., et al. “Diagnostic Value of Certain Mastitis Markers in Following up the Clinical and Bacteriological Change in Pharmacotherapeutic Studies” University of Veterinary Science, Budapest, Hungary 45(4) pp. 409-416 (1997). cited by other ; Jensen, L., et al., “Regulation of serum amyloid A protein expression during the acute-phase response”, Biochem J. (1998) 334:489-503. cited by other ; Kho Y.J., et al., “Cloning and characterization of involution-specific genes from the bovine mammary gland” Database EMBL accession No. AF160867 'Online! Jun. 30, 2000. cited by other ; Kho, Y.J., et al., GenBank Submission AAF77630, serum amyloid A protein [Bos tauru]. cited by other ; Kho, Y.J., et al., Rapid Communication: Cloning of bovine serum amyloid A3 cDNA1, American Society of Animal Science, May 19, 2000. cited by other ; Kluve-Beckerman, Barbara et al., “Primary Structures of Dog and Cat Amyloid A Proteins: Comparison to Human AA” Comp. Biochem. Physiol. vol. 94B, No. 1, pp. 175-183, 1989. cited by other ; Kluve-Beckerman, Barbara, et al. “Human Serum Amyloid A—Three Hepatic mRNAs and the Coresponding Proteins in One Person” The Journal of Clinical Investigation, Inc., vol. 82, Nov. 1988 pp. 1670-1675. cited by other ; Liang, Jun-shan, et al., “Amino terminao region of acute phase, but not constitutive, serym amyloid A (apoSAA) specifically binds and transports cholesterol into aortic smooth muscle and HepG2 cells”, Journal of Lipid Research (1996) 37:2109-2116. cited by other ; Liepnieks, J., et al., “The primary structure of serum amyloid A protein in the rabbit: Comparison with serum amyloid A proteins in other species”, J Lab Clin Med (1991) 118(6):570-576. cited by other ; Malle, E., “Human serum amyloid A (SAA) protein: a prominent acute-phase reactant for clinical practice”, European Journal of Clinical Investigation (1996) 26::427-435. cited by other ; Marhaug, Gudmund, et al. “Mink Serum Amyloid A Protein. Expression and primary structure based on cDNA”, J. Biol. Chem., vol. 265:10049-10054, 1990. cited by other ; McDonald, T., et al., “A monoclonal antibody sandwich immunoassay for serum amyloid A (SAA) protein”, J. of Immunological Methods, 144 (1991) 149-155. cited by other ; McDoanld, T., et al. “Elevated extrahepatic expression and secretion of mammary-associated serum amyloid A3 (M-SAA3) into colostrums” Veterinary Immunology and Immunopathology 6528 (2001) 1-9. cited by other ; Migita, K., et al., “Serum Amyloid A Protein Induces Production of Matrix Metalloproteinases by Human Synovial Fibroblasts”, Laboratory Investigation, 78(5):535-539 (1998). cited by other ; Mitchell, T., et al., “The acute phase reactant serum amyloid A (SAA3) is a novel substrate for degradation by the metalloproteinases collagenase and stromelysin”, Biochem et Biophysica Acta. 1156 (1998) 245-254. cited by other ; Mitchell, T.I., et al., “Serum Amyloid A (SAA3) Produced by Rabbit Synovial Fibroblasts Treated with Phorbol Esters or Interlaukin 1 induces Synthesis of Collagenase and is Neutralized with Specific Antiserum”, J. Clinical Investigation 87(4):1177-1185 (1991). cited by other ; Patel, H., “Human Serium Amyloid A has Cytokine-Like Properties”, Scand. J. Immunol. 1998, 48:410-418. cited by other ; Peristeris, P., “Effects of serum amyloid A protein on lymphocytes, HeLa, and MRC5 cells in culture”, Biochem. Cell Biol., (1989) 67:365-370. cited by other ; Rossevatn, K., et al., “The complete amino acid sequence of bovine serum amyloid protein A (SAA) and of subspecies of the tissue-deposited amyloid fibril protein A”, Scand. J. Immunol. 35(2):217-24 (1992). cited by other ; Satoh, Megumi, et al, “Sandwich enzyme-linked immunosorbent assay for quantitative measurement of serum amyloid A protein in horses” Am J Vet Res., vol. 56, No. 10, Oct. 1995. cited by other ; Sletten, K., “The Primary Structure of Equine Serum Amyloid A (SAA) Protein”, Scand. J. Immunol. 30(1):117-122 (1989). cited by other ; Sletten, K., et al., “The Amino Acid Sequence of an Amyloid Fibril Protein AA Isolated from the Horse”, Scand. J. Immunol. 26, 79-84, 1987. cited by other ; Smith, J., et al., “Comparison of Serum Amyloid A and C-Reactive Protein as Indicators of Lung Inflammation in Corticosteroid Treated and Non-Corticosteroid Treated Cystic Fibrosis Patients”, Journal of Clinical Laboratory Analysis 6:219-224 (1992). cited by other ; Smith, J., et al., “Production of serum amyloid A and C-reactive Protein by HepG2 cells stimulated with combinations of cytokines or monocyte conditioned media: the effects of prednisolone”, Clin. exp. Immunol. (1992) 783. cited by other ; Smith, J., et al., “Use of Ethanol-Eluted Hydrophobic Interaction Chromatography in the Purification of Serum Amyloid A”, Protein Expression and Purification 2:158-161 (1991). cited by other ; Steel, D., et al., “Expression and regulation of Constitutive and Acute Phase Serum Amyloid A mRNAs in Hepatic and Non-Hepatic Cell Lines”, 1996, Blackwell Science Ltd., Scandinavian Journal of Immunology, 44:493-500. cited by other ; Steel, D., et al., “The major acute phase reactants: C-reactive protein, serum amyloid P component and serum and amyloid A protein”, Review, 1994 Elsevier Science Ltd, 0167-5699/94. cited by other ; Syversen, P.V., et al., “The Primary Structure of Serum Amyloid A Protein in the Sheep; Comparison with Serum Amyloid A in Other Species” Scand. J. Immuno., vol. 39:88-94, 1994. cited by other ; Taktak, Y.S., et al., “A solid phase enzyme immunoassay for serum amyloid A (SAA) protein”, Journal of Immunological Methods, 136 (1991) 11-16. cited by other ; Thompson, D., et al., “The value of acute phase protein measurements in clinical practice”, Ann Clin Biochem 1992, 29:123-131. cited by other ; Uhlar, C., “Evolution of the Serum Amyloid A (SAA) Protein Superfamily”, Genomics 19:228-235 (1994). cited by other ; Urieli-Shoval, S., et al., “Widespread Expression of Serum Amyloid A in Histologically Normal Human Tissues: Predominant Localization of the Epithelium”, The Journal of Histochemistry & Cytochemistry 46(12):1377-1384 (1998). cited by other ; Waalen, Kristian, et al., “The Primary Structure of Amyloid Fibril Protein AA in Endotoxin-Induced Amyloidosis of the Mink”, European Journal of Biochem, vol. 104:407-412 (1980). cited by other ; Wilkins, Julie, et al., “Rapid Automated Enzyme Immunoassay of Serum Amyloid A”, Clin. Chem. 40/7, 1284-1290 (1994). cited by other ; Zank, W., et al., “Assessment of Subacute Mammary Inflammation by Soluble Biomarkers in Comparison to Somatic Cell Counts in Quarter Milk Samples from Dairy Cows”, J. Vet. Med. A45, 41-51 (1998). cited by other ; Zimlichman, S., “Serum amyloid A, an acute phase protein, inhibits platelet activation”, Serum amyloid A and platelet activation, 116(2):180-186. cited by other ; Database CAPLUS on STN, AN 1993: 11776, Kluve-Beckerman, B. et al. “Sequence Analysis of a Third Human SAA gene”., Amyloid Amyloidosis Int. Symp. Amyloidosis, 1991. Meeting abstract. cited by other ; Sellar, et al. Organization of the Region Encompassing the Human Serum Amyloid A (SAA) Gene Family on Chromosome 11p15.1. Genomics. 1994, vol. 23, pp. 492-495. cited by other ; Larson et al., “Human serum amyloid A3 peptide enhances intestinal MUC3 expression and inhibits EPEC adherence”, pp. 531-540, Biochemical and Biophysical Research Communications 300, Elsevier Science, 2002. cited by other ; Larson et al., “Induction of human mammary-associated serum amyloid A3 expression by prolactin or lipopolysaccharide”, pp. 1030-1037, Biochemical and Biophysical Research Communications 301, Elsevier Science, 2003. cited by other ; Newstead, D.F., Acceptable levels of bovine immunoglobulin in colostrums testing:, New Zealand Journal of Dairy science and Technology, vol. 6, No. 2, p. 2, Xp008036075, 1971. cited by other ; Nielsen et al., “Acute phase protein concentrations in serum and milk from healthy cows, cows with clinical mastitis and cows with extramammary inflammatory conditions”, The Veterinary Record, vol. 154, No. 12, pp. 361-365, ISSN: 0042-4900, Mar. 20, 2004. cited by other ; Rygg et al., “In vitro evaluation of an enhanced Human Serum Amyloid A (SAA) Promoter-regulated soluble TNF Receptor Fusion Protein for Anti-inflammatory Gene Therapy”, Scand J Immunol, 2001. cited by other ; Schrodl et al., “C-reaction protein as a new parameter of mastitis's!”, Tierarztlich Praxis, vol. 23, No. 4, pp. 337-341, XP008036085, ISSN: 0303-6286, 1995. cited by other ; Sipe et al., “Direct binding enzyme-linked immunosorbent assay (Elisa) for serum amyloid A (SAA)”, Journal of Immunological Methods, Elsevier Science, Publishers B.V. Amsterdam, NL, vol. 125, No. 1/2, pp. 125-135, XP002018648, ISSN: 0022-1759, 1989. cited by other ; Kluve-Beckerman, “Nonexpression of the Human Serum Amyloid A Three (SAA3) Gene”, DNA and Cell Biology, 10(9):651-661 (1991). cited by other ; McDonald, “A monoclonal antibody sandwich immunoassay for serum amyloid A (SAA) protein”, J. of Immunolog. Methods, 144:149-155 (1991). cited by other ; McDonald, “Elevated extrahepatic expression and secretion of mammary-associated serum amyloid A3 (M-SAA3) into colostrum”, Veterinary Immunology & Immunopathology 6528:1-9 (2001). cited by other ; Pedersen, “The biology of eukaryotic promoter prediction-a review”, Computers & Chemistry 23:191-207 (1999). cited by other ; Sack, “The human serum amyloid A (SAA)-encoding gene GSAA1:nucleotide sequence and possible autocrine-collagenase-inducer function”, Gene, 84:509-515 (1989). cited by other ; Sletten, “The Primary Structure of Equine Serum Amyloid A (SAA) Protein”, Scand. J. Immunol. 30:117-122 (1989). cited by other ; Zimlichman, S., “Serum amyloid A, an acute phase protein, inhibits platelet activation”, Serum amyloid A and platelet activation, 116(2):180-186, (1990). cited by other ; Kho Y.J., et al., “Cloning and characterization of involution-specific genes from the bovine mammary gland” DATABASE EMBL accession No. AF160867 'Online! Jun. 30, 2000. cited by other
- Assistant Examiner: Sajjadi, Fereydoun G.
- Primary Examiner: Wehbe, Anne Marie
- Attorney, Agent or Firm: McKee, Voorhees & Sease, P.L.C.
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