Methods for treating hormone disorders

Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues

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C07K 100

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061110779

ABSTRACT:
Method for screening for a non-hormone agent potentially useful to treat a hormone disorder The method involves contacting a potential agent with a system containing a cellular component and a translation factor. The component and factor interact with one another in an intact normal cell in a manner responsive to the hormone to cause a modulation of translation in the cell. The method involves determining whether the agent causes a modulation of translation by the component and the factor analogous to that which occurs in intact cells in response to the hormone.

REFERENCES:
patent: 4948729 (1990-08-01), Piatak et al.
patent: 5324637 (1994-06-01), Thompson et al.
patent: 5464758 (1995-11-01), Gossen et al.
patent: 5492817 (1996-02-01), Thompson et al.
Adams MD, Sequence identification of 2,375 human brain genes. Nature. Feb. 13, 1992;355(6361):632-4.
Avruch et al., 1985, "Protein Phosphorylation as a Mode of Insulin Action" in Molecular Basis of Insulin Action, Czech (ed.) Plenum Press, New York, pp. 263-296.
Belsham GJ and Brangwyn, A region of the 5' noncoding region of foot-and-mouth disease virus RNA directs efficient internal initiation of protein synthesis within cells: involvement with the role of L protease in translational control. J Virol. Nov. 1990;64(11):5389-95.
Belsham GJ, Reversibility of the insulin-stimulated phosphorylation of ATP citrate lyase and a cytoplasmic protein of subunit Mr 22000 in adipose tissue. Biochem J. Apr. 15, 1982;204(1):345-52.
Belsham GJ, Anti-insulin receptor antibodies mimic the effects of insulin on the activities of pyruvate dehydrogenase and acetylCoA carboxylase and on specific protein phosphorylation in rat epididymal fat cells. Diabetologia. Apr. 1980;18(4):307-12.
Blackshear PJ, Insulin and growth factors stimulate the phosphorylation of a Mr-22000 protein in 3T3-L1 adipocytes. Biochem J. Jul. 15, 1983;214(1):11-9.
Blanar MA and Rutter, Interaction cloning: identification of a helix-loop-helix zipper protein that interacts with c-Fos. Science. May 15, 1992;256(5059):1014-8.
Brannon PM, Adaptation of the exocrine pancreas to diet. Annu Rev Nutr. 1990;10-85-105.
Buse MG, Muscle protein synthesis: regulation of a translational inhibitor. Am J Physiol. Jun. 1984;246(6 Pt 1):E510-5.
Chien CT, The two-hybrid system: a method to identify and clone genes for proteins that interact with a protein of interest. Proc Natl Acad Sci U S A. Nov. 1, 1991;88(21):9578-82.
de Groot CJ, Developmental and hormonal regulation of carbamoyl-phosphate synthase gene expression in rat liver: evidence for control mechanisms at different levels in the perinatal period. Biochim Biophys Acta. Feb. 24, 1986;866(1):61-7.
De Benedetti A and Rhoads, Overexpression of eukaryotic protein synthesis initiation factor 4E in HeLa cells results in aberrant growth and morphology. Proc Natl Acad Sci U S A. Nov. 1990;87(21):8212-6.
Denton RM, A partial view of the mechanism of insulin action. Diabetologia, Oct. 1981;21(4):347-62.
Duncan R, Regulated phosphorylation and low abundance of HeLa cell initiation factor eIF-4F suggest a role in translational control. Heat shock effects on eIF-4F. J Biol Chem. Jan. 5, 1987;262(1):380-8.
Fagan RJ, Translational control of ornithine aminotransferase. Modulation by initiation factor eIF-4E. J Biol Chem. Sep. 5, 1991;266(25):16518-23.
Fields S and Song, A novel genetic system to detect protein-protein interactions. Nature. Jul. 20, 1989;340(6230):245-6.
Fuerst TR, Eukaryotic transient-expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase. Proc Natl Acad Sci U S A. Nov. 1986;83(21):8122-6.
Gallie DR and Traugh, Serum and insulin regulate cap function in 3T3-L1 cells. J Biol Chem. Mar. 11, 1994;269(10):7174-9.
Hager SR, Divergence between GLUT4 mRNA and protein abundance in skeletal muscle of insulin resistant rats. Biochem Biophys Res Commun. Nov. 27, 1991;181(1):240-5.
Hershey JW, Protein phosphorylation controls translation rates. J Biol Chem. Dec. 15, 1989;264(35):20823-6.
Hershey et al., 1996, Translational Control, Cold Spring Harbor Laboratory Press, pp. 245-269.
Hu C, Molecular cloning and tissue distribution of PHAS-I, an intracellular target for insulin and growth factors. Proc Natl Acad Sci U S A. Apr. 26, 1994;91(9):3730-4.
Joshi-Barve S, Alteration of the major phosphorylation site of eukaryotic protein synthesis initiation factor 4E prevents its association with the 48 S initiation complex. J Biol Chem. Feb. 15, 1990;265(5):2979-83.
Kaiser N, Differential regulation of glucose transport and transporters by glucose in vascular endothelial and smooth muscle cells. Diabetes. Jan. 1993;42(1):80-9.
Lazaris-Karatzas A and Sonenberg, The mRNA 5' cap-binding protein, eIF-4E, cooperates with v-myc or E1A in the transformtion of primary rodent fibroblasts. Mol Cell Biol. Mar. 1992;12(3):1234-8.
Lazaris-Karatzas A and Sonenberg, Malignant transformation by a eukaryotic initiation factor subunit that binds to mRNA 5' cap. Nature. Jun. 7, 1990;345(6275):544-7.
Lazaris-Karatzas A, Ras mediates translation initiation factor 4E-induced malignant transformation. Genes Dev. Sep. 1992;6(9):1631-42.
Levenson RM, Insulin rapidly induces the biosynthesis of elongation factor 2. J Biol Chem. Jul. 15, 1989;264(20):11904-11.
Lin TA, PHAS-I as a link between mitogen-activated protein kinase and translation initiation. Science. Oct. 28, 1994;266(5185):653-6.
Lyons RT, Effects of fasting and insulin administration on polyribosome formation in rat epididymal fat cells. J Biol Chem. Jul. 10, 1980;255(13):6330-4.
Manzella JM, Insulin induction of ornithine decarboxylase. Importance of mRNA secondary structure and phosphorylation of eucaryotic initiation factors eIF-4B and eIF-4E. J Biol Chem. Feb. 5, 1991;266(4):2383-9.
Merrick WC, Mechanism and regulation of eukaryotic protein synthesis. Microbiol Rev. Jun. 1992;56(2):291-315.
Methot N, The translation initiation factor eIF-4B contains an RNA-binding region that is distinct and independent from its ribonucleoprotein consensus sequence. Mol Cell Biol. Apr. 1994;14(4):2307-16.
Morgan HE, Regulation of protein synthesis in heart muscle. II. Effect of amino acid levels and insulin on ribosomal aggregation. J Biol Chem. Apr. 10, 1971;246(7):2163-70.
Morley SJ and Thomas, Intracellular messengers and the control of protein synthesis. Pharmacol Ther. 1991;50(3):291-319.
Morley SJ and Traugh, Differential stimulation of phosphorylation of initiation factors eIF-4F, eIF-4B, eIF-3, and ribosomal protein S6 by insulin and phorbol esters. J Biol Chem. Jun. 25, 1990;265(18):10611-6.
O'Brien C, Missing link in insulin's path to protein production. Science. Oct. 28, 1994;266(5185):542-3.
O'Leary NE, A translational inhibitor from muscles of diabetic rats: identification as histone H1. Am J Physiol. Jul. 1987;253(1 Pt 1):E81-9.
Pause A, Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5'-cap function. Nature. Oct. 27, 1994;371(6500):762-7.
Pelletier J and Sonenberg, Internal binding of eucaryotic ribosomes on poliovirus RNA: translation in HeLa cell extracts. J Virol. Jan. 1989;63(1):441-4.
Rhoads RE, Regulation of eukaryotic protein synthesis by initiation factors. J Biol Chem. Feb. 15, 1993;268(5):3017-20.
Rhoads RE, Mechanism of action and regulation of protein synthesis initiation factor 4E: effects on mRNA discrimination, cellular growth rate, and oncogenesis. Prog Nucleic Acid Res Mol Biol. 1993;46:183-219.
Serra D, Regulation of mitochondrial 3-hydroxy-3-methylglutaryl-coenzyme A synthase protein by starvation, fat feeding, and diabetes. Arch Biochem Biophys. Nov. 15, 1993;307(1):40-5.
Shantz LM and Pegg, Overproduction of ornithine decarboxylase caused by relief of translational repression is associated with neoplastic transformation. Cancer Res. May 1, 1994;54(9):2313-6.
Shantz LM, Overproduction of ornithine decarboxylase caused by relief of translational repression is associated with neoplastic transformation. Cancer Res. May 1, 1994;54(9):2313-6.
Smith MR, Translation initiation factors induce DNA synthesis and transform

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