DNA encoding mammalian phosphodiesterases

Details DNA encoding mammalian phosphodiesterases DNA encoding mammalian phosphodiesterases

2006-08-09

2010-11-30

Robinson, Hope A (Department: 1652)

Chemistry: molecular biology and microbiology

Micro-organism, tissue cell culture or enzyme using process...

Recombinant dna technique included in method of making a...

C435S007100, C435S320100, C435S325000, C530S350000

Reexamination Certificate

active

07842478

ABSTRACT:
The present invention relates to novel purified and isolated nucleotide sequences encoding mammalian Ca2+/calmodulin stimulated phosphodiesterases (CaM-PDEs) and cyclic-GMP-stimulated phosphodiesterases (cGS-PDEs). Also provided are the corresponding recombinant expression products of said nucleotide sequences, immunological reagents specifically reactive therewith, and procedures for identifying compounds which modulate the enzymatic activity of such expression products.

REFERENCES:
Ausubel, et al.,eds., Current Protocols in Molecular Biology, 1: 1.7.1-1.7.2 and 9.2.1-9.2.3, John Wiley & Sons, New York (1989).
Beavo, J.A., “Multiple Isozymes of Cyclic Nucleotide Phosphodiesterase,”Advances in Second Messenger and Phosphoprotein Research, 22: 1-38 (1988).
Beavo, J.A., “Multiple Phosphodiesterase Isoenzymes Background, Nomenclature and Implications”, pp. 3-15;Cyclic Nucleotide Phosphodiesterases; Structure, Regulation and Drug Action, J. Beavo and Houslay, M.D., Eds.; John Wiley & Sond, Ltd., New York (1990).
Birnstiel, M.L., et al., “Transcription Termination and 3′ Processing: The End Is in Sight!”,Cell, 41: 349-359 (1985).
Bourne, H.R., et al., “Somatic Genetic Analysis of Cyclic AMP Action: Characterization of Unresponsive Mutants,”J. Cell. Physiol., 85: 611-620 (1985).
Bradford, M.M., “A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye Binding,”Analytical Biochem., 72: 248-254 (1976).
Chen, C-N., et al., “Molecular Analysis of cDNA Clones and the Corresponding Genomic Coding Sequences of theDrosophiladunce+Gene, the Structural Gene for cAMP Phosphodiesterase,”Proc. Nat'l. Acad. Sci. (USA), 83: 9313-9317 (1986).
Charbonneau, H., et al., “Identification of a conserved domain among cyclic nucleotide phosphodiesterases from diverse species,”Proc. Nat'l. Acad. Sci. (USA), 83: 9308-9312 (1986).
Chomczynski, P., et al., “Single-Step Method of RNA Isolation by Acid Guanidinium Thiocyanate-Phenol-Chloroform Extraction,”Analytical Biochem., 162: 156-159 (1987).
Colicelli, J., et al., “Isolation and Characterization of a Mammalian Gene Encoding a High-Affinity cAMP Phosphodiesterase,”Proc. Nat'l. Acad. Sci. (USA), 86: 3599-3603 1989.
Davis, R.L., “Molecular Genetics of the Cyclic Nucleotide Phosphodiesterases”, pp. 227-241 inCyclic Nucleotide Phosphodiesterases: Structure, Regulation and Drug Action, J. Beavo and Houslay, M.D., Eds.; John Wiley & Sons, Ltd., New York (1990).
Davis, R.L., et al., “Cloning and Characterization of Mammalian Homologs of theDrosophiladunce+Gene,”Proc. Nat'l. Acad. Sci. (USA), 86: 3604-3608 (1989).
Devereux, J., et al., “A Comprehensive Set of Sequence Analysis Programs for the VAX,”Nucleic Acids Res., 12: 387-395 (1984).
Epstein, P.M. et al., “Identification and characterization of a Ca2+ -calmodulin-sensitive cyclic nucleotide phosphodiesterase in a human lymphoblastoid cell line,”Biochem. J., 243:533-539 (1987).
Erneux, C., et al., “A Mechanism in the Control of Intracellular cAMP Level: The Activation of a Calmodulin-Sensitive Phosphodiesterase by a Rise of Intracellular Free Calcium,”Mol. Cell. Endocranial., 43: 123-134 (1985).
Faure, M., et al., “Disruption ofDictyostelium discoideumMorphogenesis by Overproduction of cAMP Phosphodiesterase,”Proc. Nat'l. Acad. Sci.(USA), 85: 8076-8080 (1988).
Feinberg, A.P., et al., “A Technique for Radiolabeling DNA Restriction Endonucleas Fragments to High Specific Activity ”Analytical Biochem., 137: 266-267 (1984).
Greenberg, L.H., et al., “Enzymatic Regulation of the Concentration of Cyclic GMP in Mouse Brain,”Neuropharmacology, 17: 737-745 (1978).
Hansen, R.S., et al., “Differential Recognition of Calmodulin-Enzyme Complexes by a Conformation-Specific Anti-Calmodulin Monoclonal Antibody,”J. Biol. Chem., 261: 14636-14645 (1986).
Hansen, R.S., et al., “Purification of Calmodulin-Stimulated Cyclic Nucleotide Phosphodiesterase by Monoclonal Antibody Affinity Chromatography,”Meth. Enzymol., 159: 543-557 (1988).
Hansen, R.S., et al., “Purification of Two Calcium/Calmodulin-Dependent Forms of Cyclic Nucleotide Phosphodiesterase by Using Conformation-Specific Monoclonal antibody Chromatography,”Proc. Nat'l. Acad. Sci. (USA), 79: 2788-2792 1982.
Hashimoto, Y., et al.,“Regulation of Ca2+/Calmodulin-Dependent Cyclic Nucleotide Phosphodiesterase by the Autophosphorylated Form of Ca2+/Calmodulin-Dependent Protein Kinase II,”J. Biol. Chem., 264: 10884-10887 (1989).
Henikoff, S., “Unidirectional Digestion with Exonuclease III Creates Targeted Breakpoints for DNA Sequencing,”Gene, 28: 351-359 (1984).
Hurwitz, R.L. et al. “Induction of a Calcium/Calmodulin-dependent Phosphodiesterase during Phytohemagglutinin-stimulated Lymphocyte Mitogenesis”,J. Biol. Chem., 265(15):8901-8907 (1990).
Kincaid, R.L., et al., “Differential Localization of Calmodulin-Dependent Enzymes in Rat Brain: Evidence for Selective Expression of Cyclic Nucleotide Phosphodiesterase in Specific Neurons,”Proc. Nat'l. Acad. Sci. (USA), 84: 1118-1122 (1987).
Kozak, M., “The Scanning Model for Translation: An Update,”J. Cell Biol., 108: 229-241 (1989).
Krinks, M.H., et al., “Reversible and Irreversible Activation of Cyclic Nucleotide Phosphodiesterase: Separation of the Regulatory and Catalytic Domains by Limited Proteolysis,”Advances in Cyclic Nucleotide and Protein Phosphorylation Research, 16: 31-47 (1984).
LaPorte, D.C., et al., “Cross-Linking of Iodine-125-Labeled, Calcium-Dependent Regulatory Protein to the Ca2+-Sensitive Phosphodiesterase Purified from Bovine Heart,”Biochemistry, 18: 2820-2825(1979).
Lerner, Richard L. “Tapping the immunological repertoire to produce antibodies of predetermined specificity”,Nature299(14) 592-596 (1987).
LeTrong, H., et al., “Amino Acid Sequence of the Cyclic GMP Stimulated Cyclic Nucleotide Phosphodiesterase from Bovine Heart,”Biochemistry, 29: 10280-10288 (1990).
Livi, G.P., et al., “Cloning and Expression of cDNA for a Human Low-Km, Rolipram-Sensitive Cyclic AMP Phosphodiesterase,”Mol.Cell. Biol., 10: 2678-2686 (1990).
Manganiello, V.C., et al., “Cyclic GMP-Stimulated Cyclic Nucleotide Phosphodiesterases”, pp. 62-85 inCyclic Nucleotide Phosphodiesterases: Structure, Regulation and Drug Action, Beavo, J. and Houslay, M.D., Eds.; John Wiley & Sons, Ltd., New York (1990).
Maniatis, et al.,Molecular Cloning: A Laboratory Manual, pp. 324-328, Cold Spring Harbor Laboratory, Cold Spring Harbor, New York (1982).
Martins, T.J., et al., “Purification and Characterization of a Cyclic GMP-Stimulated Cyclic Nucleotide Phosphodiesterase from Bovine Tissues,”J. Biol. Chem., 257: 1973-1979 (1982).
Nikawa, J-I., et al., “Cloning and Characterization of the Low-Affinity Cyclic AMP Phosphodiesterase Gene ofSaccharomyces cerevisiae,” Mol. Cell. Biol., 7: 3629-3636 (1987).
Nomenclature Committee of the International Union of Biochemistry (NCIUB), “Nomenclature for Incompletely Specified Bases in Nucleic Acid Sequences,”J. Biol. Chem., 261:13-17 (1986).
Novack, J.P., et al., “Sequence Comparison of the 63-, 61-, and 59-kDa Calmodulin-Dependent Cyclic Nucleotide Phosphodiesterases,”Biochemistry, 30: 7940-7947 (1991).
Ovchinnikov, Y.A., et al., “Cyclic GMP Phosphodiesterase from Bovine Retina,”FBS, 223: 169-173(1987).
Pennypacker, K.R. et al., “Expression of Calmodulin-Dependent Phosphodiesterase Calmodulin-Dependent Protein Phosphatase, and Other Calmodulin-Binding Proteins in Human SMS-KCNR Neuroblastoma Cells,”Journal of Neurochemistry, 52(5)1438-1448 (1989).
Sanger, F., et al., “DNA Sequencing with Chain-Terminating Inhibitors,&#

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