Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues
Reexamination Certificate
2005-10-31
2008-11-18
Kam, Chih-Min (Department: 1656)
Chemistry: natural resins or derivatives; peptides or proteins;
Proteins, i.e., more than 100 amino acid residues
C530S370000, C530S387100, C530S391700, C530S396000, C530S403000, C514S002600, C514S012200, C435S069100, C435S252300, C435S320100, C424S183100
Reexamination Certificate
active
07452971
ABSTRACT:
The present invention provides methods to produce immunotoxins (ITs) and cytokines with a reduced ability to promote vascular leak syndrome (VLS). The invention also provides ITs and cytokines which have been mutated to lack amino acid sequences which induce VLS.
REFERENCES:
patent: 4664911 (1987-05-01), Uhr et al.
patent: 4792447 (1988-12-01), Uhr et al.
patent: 5045451 (1991-09-01), Uhr et al.
patent: 5510332 (1996-04-01), Kogan et al.
patent: 5578706 (1996-11-01), Ghetie et al.
patent: 5686072 (1997-11-01), Uhr et al.
patent: 5688913 (1997-11-01), Arrhenius et al.
patent: 5730978 (1998-03-01), Wayner
patent: 5736536 (1998-04-01), Siegall et al.
patent: 5767072 (1998-06-01), Vitetta et al.
patent: 5770573 (1998-06-01), Arrhenius et al.
patent: 5811391 (1998-09-01), Arrhenius et al.
patent: 5821231 (1998-10-01), Arrhenius et al.
patent: 6566500 (2003-05-01), Vitetta et al.
patent: WO 00/58456 (2000-10-01), None
Baluna and Vitetta, “An in vivo model to study immunotoxin-induced vascular leak in human tissue,”J. of Immunotherapy, 22:41-47, 1999.
Baluna and Vitetta, “Vascular leak syndrome: a side effect of immunotherapy,”Immunopharmacology, 37:117-132, 1997.
Baluna et al., “Decreases in levels of serum fibronectin predict the severity of vascular leak syndrome in patients treated with Ricin A chain-containing immunotoxins,”Clin. Cancer Res., 2(10):1705-1712, 1996.
Baluna et al., “Evidence for a structural motif in toxins and interleukin-2 that may be responsible for binding to endothelial cells and initiating vascular leak syndrome,”Proc. Natl. Acad. Sci. USA, 96:3957-3962, 1999.
Baluna et al., “The effect of a monoclonal antibody coupled to ricin A chain-derived peptides on endothelial cells in vitro: insights into toxin-mediated vascular damage,”Experimental Cell Research, 258(2):417-424, 2000.
Baluna et al., “Fibronectin inhibits the cytotoxic effect of ricin A chain of endothelial cells,”Int. J. Immunopharm., 18:355-361, 1996.
Blobel and White, “Structure, function and evolutionary relationship of proteins containing a disintegrin domain,”Curr. Opin. Cell Biol., 4:760-765, 1992.
Clements et al., “Identification of a key integrin-binding sequence in VCAM-1 homologous to the LDV active site in fibronectin,”J. Cell Sci., 107:2127-2135, 1994.
Collins et al., “Identification of specific residues of human interleukin 2 that affect binding to the 70-kDa subunit (p70) of the interleukin 2 receptor,”Proc. Natl. Acad. Sci. USA, 85:7709-7713, 1988.
Coulson et al., “Rotavirus contains integrin ligand sequences and a disintegrin-like domain that are implicated in virus entry into cells,”Proc. Natl. Acad. Sci. USA, 94:5389-5394, 1997.
Downie et al., “Interleukin-2 directly increases albumin permeability of bovine and human vascular endothelium in vitro,”Am. J. Respir. Cell Mol. Biol., 7:58-65, 1992.
Dutcher et al., “A phase II study of high-dose continuous infusion interleukin-2 with lymphokine-activated killer cells in patients with metastatic melanoma,”J. Clin.Oncol., 9:641-648, 1991.
Engert et al., The emerging role of ricin A-chain immunotoxins in leukemia and lymphoma,In: Clinical Applications of Immunotoxins, Frankel (ed.), 2:13-33, 1997.
Frankel et al., “Role of arginine 180 glutamic acid 177 of ricin toxin a chain in enzymatic inactivation of ribosomes,” Mol. Cell. Biol; 10:6257-6263,1990.
Ghetie et al., “The GLP large scale preparation of immunotoxins containing deglycosylated ricin A chain and a hindered disulfide bond,”J. Immunol Methods, 142(2):223-230, 1991.
Greenspoon et al., “Novel ψ-S-CH2peptide-bond replacement and its utilization in the synthesis of nonpeptide surrogates of the Leu-Asp-Val sequence that exhibit specific inhibitory activities on CD4+ T cell binding to fibronectin,”Int. J. Pept. Res., 43:417-424, 1994.
Halling et al., “Genomic cloning and characterization of a ricin gene fromRicinus communis,” Nucleic Acids Res., 13(22):8019-8033, 1985.
Huang, “What have snakes taught us about integrins?”Cellular and Molecular Life Sciences, 54:527-540, 1998.
Hur et al., “Isolation and characterization of pokeweed antiviral protein mutations inSaccharomyces cerevisiae: identification of residues important for toxicity,”Proc. Natl. Acad. Sci., USA, 92:8448-8452, 1995.
Husain and Bieniarz, “Fc site-specific labeling of immunoglobulins with calf intestinal alkaline phosphatase,”Bioconjug. Chem., 5:482-490, 1994.
Jackson et al., “Potent α4β1 peptide antagonists as potential anti-inflammatory agents,”J. Med. Chem., 40:3359-3368, 1997.
Lamb et al., “Nucleotide sequence of cloned cDNA coding for preproricin,”Eur. J. Biochem., 148(2):265-270, 1985.
Lazarus and McDowell, “Structural and functional aspects of RGD-containing protein antagonists of glycprotein IIb-IIIa,”Curr. Opin. Biotechnology, 4:438-445, 1993.
Li et al., “The crystal structure ofPseudomonas aeruginosaexotoxin domain III with nicotinamide and AMP: conformational differences with the intact exotoxin,”Proc. Natl. Acad. Sci. USA, 92:9308-9312, 1995.
Lu et al., “Substitutions of proline 42 to alanine and methionine 46 to asparagine around the RGD domain of the neurotoxin dendroaspin alter its preferential antagonism to that resembling the disintegrin elegantin,”J. Biol. Chem., 271:289-294, 1996.
Maeda et al., “Amino acids and peptides. XXXII: a bifunctioanl poly(ethylene glycol) hybrid of fibronectin-related peptides,”Biochem. Biophys. Res. Commun., 241:595-598, 1997.
Makarem and Humphries, “LDV, a novel cell adhesion motif recognized by the integrin α4β1,”Biochemical Society Transactions, 19:380S-381S, 1991.
McLane et al., “Viper venom disintegrins and related molecules (44322),”Proc. Soc. Exp. Biol. Med., 219:109-119, 1998.
Mlsna et al., “Structure of recombinant ricin A chain at 2.3 Å,”Protein Sci., 2:429-435, 1993.
Munishkin and Wool, “Systematic deletion analysis if ricin A-chain function,”J. Biol. Chem., 270:30581-30587, 1995.
Nowlin et al., “A novel cyclic pentapeptide inhibits α4β1 and α5β1 integrin-mediated cell adhesion,”J. Biol. Chem., 268:20352-20359, 1993.
O'Hare et al., “Expression of ricin A chain inEscherichia coli,” FEBS Lett., 216(1):73-78, 1987.
Orucevic and Lala, “NG-nitro-L-arginine methyl ester, an inhibitor of nitric oxide synthesis, ameliorates interleukin-2-induced capillary leak syndrome in healthy mice,”J. Immunother., 18:210-220, 1996.
Rosenberg et al., “A progress report on the treatment of 157 patients with advanced cancer using lymphokine-activated killer cells and interleukin-2 or high-dose interleukin-2 alone,”N. Engl. J. Med., 316:889-897, 1987.
Rosenstein et al., “Extravasation of intravascular fluid mediated by the systemic administration of recombinant interleukin 2,”J. Immunol., 137:1735-1742, 1986.
Sausville and Vitetta, “Clinical studies with deglycosylated ricin A-chain immunotoxins,”In: Monoclonal Antibody-Based Therapy of Cancer, Grossbard (ed.), 4:81-89, 1997.
Schindler et al., “The toxicity of deglycosylated Ricin A chain-containing immunotoxins in patients with non-Hodgkin's lymphoma is exacerbated by prior radiotherapy: a retrospective analysis of patients in five clinical trials,”Clin. Cancer Res., 7(2):255-258, 2001.
Shen et al., “Participation of lysine 516 and phenylalanine 530 of diphtheria toxin in receptor recognition,”J. Biol. Chem., 269(46):29077-29084, 1994.
Simpson et al., “Point mutations in the hdrophobic C-terminal region of ricin A chain indicate that Pro250 plays a key role in membrane translocation,”Eur. J. Biochem., 232:458-463, 1995.
Smallshaw et al., “A novel reco
Baluna Roxana G.
Ghetie Victor F.
Smallshaw Joan E.
Vitetta Ellen S.
Board of Regents , The University of Texas System
Fulbright & Jaworski
Kam Chih-Min
LandOfFree
Compositions and methods for modifying toxic effects of... does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Compositions and methods for modifying toxic effects of..., we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Compositions and methods for modifying toxic effects of... will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-4021255