DNA encoding mammalian phosphodiesterases

Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Hydrolase

Reexamination Certificate

Rate now

  [ 0.00 ] – not rated yet Voters 0   Comments 0

Details

C435S252300, C435S325000, C536S023200

Reexamination Certificate

active

07122363

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:
Manganiello et al. (1990) Cyclic GMP-stimulated cyclic nucleotide phosphodiesterases. In: Beavo and Houslay (Eds), Isoenzymes of cyclic nucleotide phosphodiesterases. John Wiley and Sons, NY, pp. 61-85.
Martins et al. (1982) J. Biol. Chem., vol. 257 (4), pp. 1973-1979.
Murashima et al. (Jun. 5, 1990) Biochemistry, vol. 29, pp. 5285-5292.
Sonneburg et al. (Sep. 15, 1991) J. Biol. Chem., vol. 266 (26), pp. 17655-17661.
LeTrong et al (1990) Biochemistry, vol. 29, 10280-10288.
Ausubel, et al., eds.,Current Protocols in Molecular Biology, 1: 1.7.7-1.7.2 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).
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).
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 ofDisruption of Dictyostelium 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 Endonuclease 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).
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).
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-KmRolipram-Sensitive Cyclic AMP Phosphodiesterase,”Mol. Cell. Biol., 10: 2678-2686 (1990).
Manganiello, V.A., 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,”FEBS, 223: 169-173 (1987).
Sanger, F., et al., “DNA Sequencing with Chain-Terminating Inhibitors,”Proc. Nat'l. Acad. Sci.(USA), 74: 5463-5467 (1977).
Sass, P., et al., “Cloning and Characterization of the HIgh-Affinity cAMP Phosphodiesterase ofSaccharomyces cerevisiae,” Proc. Nat'l. Acad. Sci.(USA), 83: 9303-9307 (1986).
Seed, B., “An LFA-3 cDNA encodes a Phospholipid-Linked Membrane Protein Homologous to Its Receptor CD2,”Nature, 329: 840-842 (19870.
Sharma, R.K., et al., “Demonstration of Bovine Brain Calmodulin-Dependent Cyclic Nucleotide Phosphodiesterase Isozymes by Mo

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

DNA encoding mammalian phosphodiesterases does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with DNA encoding mammalian phosphodiesterases, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and DNA encoding mammalian phosphodiesterases will most certainly appreciate the feedback.

Rate now

     

Profile ID: LFUS-PAI-O-3682904

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