Chemistry: molecular biology and microbiology – Animal cell – per se ; composition thereof; process of...
Reexamination Certificate
2005-04-11
2008-12-02
Saoud, Christine J (Department: 1647)
Chemistry: molecular biology and microbiology
Animal cell, per se ; composition thereof; process of...
C435S069100, C435S252300, C435S320100, C536S023500
Reexamination Certificate
active
07459310
ABSTRACT:
An isolated and purified GnRH protein receptor protein including an amino acid sequence selected from the group and an isolated and purified DNA which comprises a nucleotide sequence coding for the GnRH protein receptor protein. Also, a vector comprising the DNA of the GnRH protein receptor protein, a transformant carrying the vector comprising the DNA of the GnRH protein receptor protein, a process for producing a GnRH protein receptor protein or a salt thereof including culturing the transformant carrying the vector comprising the DNA of the GnRH protein receptor protein under sufficient conditions and for appropriate time to express the GnRH protein receptor protein, and a method of screening for a ligand to the GnRH protein receptor protein including contacting the GnRH protein receptor protein or a salt thereof with a sample to be tested. A screening method for a compound capable of inhibiting binding of the GnRH protein receptor protein with a ligand. Also, a kit for screening a compound capable of inhibiting binding of the GnRH protein receptor protein with a ligand including the GnRH protein receptor protein or a salt.
REFERENCES:
patent: 5985583 (1999-11-01), Sealfon
Wells, J.A. (1990). Additivity of mutational effects in proteins. Biochemistry. 29(37):8509-8517.
Ngo et al. (1994). Computational complexity, protein structure prediction, and the Levinthal paradox. In Merz and Le Grand (Eds.) The Protein Folding Problem and Tertiary Structure Prediction. Birkhauser:Boston, pp. 491-495.
Skolnick et al. (2000). From genes to protein structure and function: novel applications of computational approaches in the genomic era. Trends in Biotechnology. 18:34-39.
Sower et al. (2001). Molecular cloning of the GNRH receptor cDNA in the sea lamprey. Society for Neuroscience Abstracts. 27(2):1948.
Norman, Anthony et al., Hormones Second Edition, 1997, p. 96, Academic Press, San Diego, CA.
Nozaki, Masumi, et al., The Distribution of Lamprey GnRH-III in Brains of Adult Sea Lampreys (Petromyzon marinus), General and Comparative Endocrinology, 2000, pp. 57-67, 118, Academic Press.
Sower, Stacia A., Evolution of GnRH in Fish of Ancient Organs, GnRH Neurons Gene to Behavior, 1997, pp. 27-49, Tokyo, Japan.
Sower, Stacia A., Brain and Pituitary Hormones of Lampreys, Recent Findings and their Evolutionary Significance, American Zoology, 1998, pp. 14-38, vol. 38.
Sower, Stacia A., Update: brain and pituitary hormones of lampreys, Comparative Biochemistry and Physiology Part B, 2001, pp. 291-302, vol. 129, Elsevier Science Inc.
Sower, Stacia A., Gonadotropin-Releasing Hormone in Primitive Fishes, Progress in Comparative Endocrinology, 1990, pp. 73-78, Wiley-Liss, Inc.
Knox, Christopher J., et al., Characterization and Localization of Gonadotropin-Releasing Hormone Receptors in the Adult Female Sea Lamprey,Petromyzon marinus, Endocrinology, 1994, pp. 492-498, vol. 134, No. 1, The Endocrine Society.
Matsuo, H., et al., Structure of the Porcine LH- and FSH-Releasing Hormone. I. The Proposed Amino Acid Sequence, Biochemical and Biophysical Research Communications, 1971, pp. 1334-1340, vol. 43, No. 6.
Burgus, Roger, et al., Primary Structure of the Ovine Hypothalamic Luteinizing Hormone-Releasing Factor (LRF), Proc. Nat. Acad. Sci. USA, Jan. 1972, pp. 278-282, vol. 69, No. 1.
Gupta, H.M., et al., A Novel Computer Modeling Approach to the Structures of Small Bioactive Peptides: The Structure of Gonadotropin-Releasing Hormone, Proteins: Structure, Function and Genetics, 1993, pp. 48-56.
Sealfon, S.C., et al. Molecular Mechanisms of Ligand Interaction with the Gonadotropin- Releasing Hormone Receptor, Endocrine Reviews, 1997, pp. 180-205, The Endocrine Society.
Sower, S.A., Goodman, et al., In Vivo Effects of Lamprey GnRH-I and Cyclized Analogs: A Structure- Activity Study, Neuropeptides, 1995, pp. 151-156, Pearson Professional Ltd.
Habibi, Hamid R., et al., Activity of Vertebrate Gonadotropin-Releasing Hormones and Analogs with Variant Amino Acid Residues in Positions 5, 7 and 8 in the Goldfish Pituitary, Regulatory Peptides, 1992, pp. 271-284, Elsevier Science Publishers B.V.
Pati, Debananda, et al., Inhibition of Human Hepatocarcinoma Cell Proliferation by Mammalian and Fish Gonadotropin-Releasing Hormones, Endocrinology, 1995, pp. 75-84, vol. 135, No. 1, The Endocrine Society.
Yu, Wen H., et al., A Hypothalamic Follicle-Stimulating Hormone-Releasing Decapeptide in the Rat, Proc. Natl. Acad. Sci. USA, Aug. 1997, pp. 9499-9503.
Dees, W.L., et al., Localization of Immunoreactive Lamprey Gonadotropin-Releasing Hormone in the Rat Brain, Peptides, 1999, pp. 1503-1511, Elsevier Science Inc.
Hiney, J.K., et al., Gonadotropin-Releasing Hormone Neurons in the Preoptic-Hypothalamic Region of the Rat Contain Lamprey Gonadotropin-Releasing Hormone III, Mammalian Luteinizing Hormone-Releasing Hormone, or Both Peptides, PNAS, Feb. 19, 2002, pp. 2386-2391, vol. 99, No. 4.
Tsutsumi, M., et al., Cloning and Functional Expression of a Mouse Gonadotrophin-Releasing Hormone Receptor, Molecular Endocrinology, 1992, pp. 1163-1169.
Kakar, S.S., et al., Cloning, Sequencing, and Expression of Human Gonadotropin-Releasing Hormone (GnRH) Receptor, Biochemical and Biophysical Research Communications, Nov. 30, 1992, pp. 289-295, vol. 189, No. 1, 1992, Academic Press, Inc.
Reinhart, J., et al., Molecular Cloning and Expression of cDNA Encoding the Murine Gonadotropin-Releasing Hormone Receptor, The Journal of Biological Chemistry, Oct. 25, 2002, pp. 21281-21284, vol. 267, No. 30.
Chi, L., et al., Cloning and Characterization of the Human GnRH Receptor, Molecular and Cellular Endocrinology, 1993, pp. R1-R6, vol. 91, Elsevier Scientific Publishers Ireland Ltd.
Perrin, M.H., et al., Molecular and Functional Characterization of GnRH Receptors Cloned from Rat Pituitary and a Mouse Pituitary Tumor Cell Line, Biochemical and Biophysical Research Communications, Mar. 31, 1993, pp. 1139-1144, vol. 191, No. 3, 1993, Academic Press, Inc.
Tensen, C., et al., Distinct Efficacies for Two Endogenous Ligands on a Single Cognate Gonadoliberin Receptor, Eur J Biochem, 1997, pp. 134-140.
Pawson, A.J., et al., Contrasting Internalization Kinetics of Human and Chicken Gonadotropin-Releasing Hormone Receptors Mediated by C-terminal Tail, Journal of Endocrinology, 1998, pp. R9-R12, vol. 156, Journal of Endocrinology Ltd., Great Britain.
Blomenrohr, M., et al., Pivotal Role for the Cytoplasmic Carboxyl-Terminal Tait of a Nonmammalian Gonadotropin-Releasing Hormone Receptor in Cell Surface Expression, Ligand Binding, and Receptor Phosphorylation and Internalization, Molecular Pharmacology, 1999, pp. 1229-1237, vol. 56, The American Society for Pharmacology and Experimental Therapeutics.
Lin, X., et al., Addition of Catfish Gonadotrophin-Releasing Hormone (GnRH) Receptor Intracellular Carboxyl-Terminal Tail to Rat GnRH Receptor Alters Receptor Expression and Regulation, Molecular Endocrinology, 1998, pp. 161-171, The Endocrine Society.
McArdle, C.A., et al., The Tail of the Gonadotropin-Releasing Hormone Receptor: Desensitization at, and Distal to, G Protein-Coupled Receptors, Molecular and Cellular Endocrinology, 1999, pp. 129-136, vol. 141, Elsevier Science Ireland Ltd.
McArdle, C.A., et al., Signalling, Cycling, and Desensitization of Gonadotropin-Releasing Hormone Receptors, Journal of Endocrinology, 2002, pp. 1-11, vol. 173, Society for Endocrinology, Great Britain.
Heding, A., et al., The Rat Gonadotropin-Releasing Hormone Receptor Internalizes via a β-Arrestin-Independent but Dynamin-Dependent, Pathway: Addition of a Carboxyl-Terminal Tail Confers β -Arrestin Dependency, Endocrinology, 2000, pp. 299-306, The Endocrine Society, United States.
Heding, A., et al., 1998. Gonadotropin-Releasing Hormone Receptors with Intracellular Carboxyl-Terminal Tails Undergo Acute Desensitization of Total Inositol Phosphate Production and Exhibit Accelerated Internalization Kinetics, The Journal of Biological Chemistry, 1998, pp. 11472-11477, vol. 273, No. 19, The American Society for Biochemistry and Molecular Biology, Inc., United States.
Hislop, J.
Nucci Nathaniel V.
Silver Matthew R.
Sower Stacia
Bruttomesso, Jr. Raymond I.
Devine, Millimet & Branch
Lockard Jon M
Remus Paul C.
Saoud Christine J
LandOfFree
Cloning and expression of gonadotropin-releasing hormone... does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Cloning and expression of gonadotropin-releasing hormone..., we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Cloning and expression of gonadotropin-releasing hormone... will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-4033532