DRUG ANALYSIS BASED ON SIGNALING RESPONSES TO G-PROTEIN-COUPLED RECEPTORS

REFERENCES

• Rall T. W., Sutherland E. W., Berthet J. The relationship of epinephrine and glucagon to liver phosphorylase. IV. Effect of epinephrine and glucagon on the reactivation of phosphorylase in liver homogenates. J. Biol. Chem. 1957; 224: 463–475
   PubMedGoogle Scholar
• Robison G. A., Butcher R. W., Sutherland E. W. Cyclic AMP. Academic Press, New York 1971
   Google Scholar
• Hardman J. G., O'Malley B. W. Methods in Enzymology: Hormone Action. Academic Press, San Diego 1974; 38
   Google Scholar
• Conn P. M., Means A. R. Methods in Enzymology: Cellular Regulators. Academic Press, San Diego 1987; 141
   Google Scholar
• Murphy R. C., Fitzpatrick F. A. Methods in Enzymology: Arachidonate Related Lipid Mediators. Academic Press, San Diego 1990; 187
   Google Scholar
• Johnson R. A., Corbin J. D. Methods in Enzymology: Adenylyl Cyclase, G Proteins, and Guanylyl Cyclase. Academic Press, San Diego 1991; 195
   Google Scholar
• Dennis E. A. Methods in Enzymology: Phospholipases. Academic Press, San Diego 1991; 197
   Google Scholar
• Iyengar R. Methods in Enzymology: Heterotrimeric G Proteins. Academic Press, San Diego 1994; 237
   Google Scholar
• Iyengar R. Methods in Enzymology: Heterotrimeric G Protein Effectors. Academic Press, San Diego 1994; 238
   Google Scholar
• Simon M. I., Strathmann M. P., Gautam N. Diversity of G proteins in signal transduction. Science 1991; 252: 802–808
   PubMed Web of Science ®Google Scholar
• Hepler J. R., Gilman A. G. G proteins. Trends Biochem. Sci. 1992; 17: 383–387
   PubMed Web of Science ®Google Scholar
• Nathans J., Hogness D. S. Isolation, sequence analysis, and intron-exon arrangement of the gene encoding bovine rhodopsin. Cell 1983; 34: 807–814
   PubMed Web of Science ®Google Scholar
• Dixon R. A.F., Kobilka B. K., Strader D. J., Benovic J. L., Dohlman H. G., Frielle T., et al. Cloning of the gene and cDNA for mammalian beta-adrenoceptor and homology with rhodopsin. Nature 1986; 321: 75–79
   PubMed Web of Science ®Google Scholar
• Yarden Y., Rodriguez H., Wong S. K.-F., Brandt D. R., May D. C., Burnier J., et al. The avian β-adrenoceptor: primary structure and membrane topology. Proc. Natl. Acad. Sci. USA 1986; 83: 6795–6799
   PubMed Web of Science ®Google Scholar
• Strader C. D., Fong T. M., Graziano M. P., Tota M. R. The family of G-protein-coupled receptors. FASEB J. 1995; 9: 745–754
   PubMed Web of Science ®Google Scholar
• van Rhee A. M., Jacobson K. A. Molecular architecture of G protein-coupled receptors. Drug Dev. Res. 1996; 37: 1–38
   PubMed Web of Science ®Google Scholar
• Coughlin S. R. Expanding horizons for receptors coupled to G proteins: diversity and disease. Curr. Opin. Cell Biol. 1994; 6: 191–197
   PubMed Web of Science ®Google Scholar
• Henderson R., Baldwin J. M., Cesca T. A., Zemlin F., Beckman E., Downing K. H. Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J. Mol. Biol. 1990; 213: 899–929
   PubMed Web of Science ®Google Scholar
• Schertler G. F., Villa C., Henderson R. Projection structure of rhodoopsin. Nature 1993; 362: 770–772
   PubMed Web of Science ®Google Scholar
• Gilman A. G. G proteins and regulation of adenylate cyclase. Angew Chem. Int. Ed. Engl. 1995; 34: 1406–1419
   Google Scholar
• Biddlecome G. H., Bernstein G., Ross E. M. Regulation of phospholipase C-β1 by Gq and m1 muscarinic cholinergic receptor. Steady-state balance of receptor-mediated activation and GTPase-activating protein-promoted deactivation. J. Biol. Chem. 1996; 271: 7999–8007
   PubMedGoogle Scholar
• Clapham D. E., Neer E. J. New roles for G-protein βγ-dimers in transmembrane signalling. Nature 1993; 365: 403–406
   PubMed Web of Science ®Google Scholar
• Boyer J. L., Paterson A., Harden T. K. G-protein-mediated regulation of phospholipase C: involvement of βγ subunits. Trends Cardiovascular Med. 1994; 4: 88–95
   PubMedGoogle Scholar
• Noel J. P., Hamm H. E., Sigler P. B. The 2.2 A crystal structure of transducin-α complexed with GTPγS. Nature 1993; 366: 654–663
   PubMed Web of Science ®Google Scholar
• Lambright D. G., Noel J. P., Hamm H. E., Sigler P. B. Structural determinants for activation of the α-subunit of a heterotrimeric G protein. Nature 1994; 369: 621–628
   PubMedGoogle Scholar
• Coleman D. E., Berghuis A. M., Lee E., Linder M. E., Gilman A. G., Sprang S. R. Structures of active conformations of Giα1 and the mechanism of GTP hydrolysis. Science 1994; 269: 1405–1412
   Google Scholar
• Sondek J., Bohm A., Lambright D. G., Hamm H. E., Sigler P. B. Crystal structure of a G-protein beta gamma dimer at 2.1A resolution. Nature 1996; 379: 369–374
   PubMed Web of Science ®Google Scholar
• Offermanns S., Simon M. I. Gα15 and Gα16 couple a wide variety of receptors to phospholipase C. J. Biol. Chem. 1995; 270: 15175–15180
   PubMed Web of Science ®Google Scholar
• Camps M., Hou C., Sidiropoulos D., Stock J. B., Jakobs K. H., Gierschik P. Stimulation of phospholipase C by guanine-nucleotide-binding protein βγ subunits. Eur. J. Biochem. 1992; 206: 821–831
   PubMedGoogle Scholar
• Boyer J. L., Waldo G. L., Harden T. K. βγ-Subunit activation of G-protein-regulated phospholipase C. J. Biol. Chem. 1992; 267: 25451–25456
   PubMed Web of Science ®Google Scholar
• Blank J. L., Brittain K. A., Exton J. H. Activation of cytosolic phosphoinositide phospholipase C by G protein βγ-subunits. J. Biol. Chem. 1992; 267: 23069–23075
   PubMedGoogle Scholar
• Boyer J. L., Graber S. G., Waldo G. L., Harden T. K., Garrison J. C. Selective activation of phospholipase C by recombinant G-protein α- and βγ-subunits. J. Biol. Chem. 1994; 269: 2814–2819
   PubMed Web of Science ®Google Scholar
• Kleuss C., Scherübl H., Hescheler J., Schultz G., Wittig B. Selectivity in signal transduction determined by γ subunits of heterotrimeric G proteins. Science 1993; 259: 832–834
   PubMed Web of Science ®Google Scholar
• Iyengar R. Molecular and functional diversity of mammalian Gs-stimulated adenylyl cyclases. FASEB J. 1993; 7: 768–775
   PubMedGoogle Scholar
• Taussig R., Gilman A. G. Mammalian membrane-bound adenylyl cyclases. J. Biol. Chem. 1995; 270: 1–4
   PubMed Web of Science ®Google Scholar
• Exton J. H. Phosphoinositide phospholipases and G proteins in hormone action. Annu. Rev. Physiol. 1994; 56: 349–369
   PubMed Web of Science ®Google Scholar
• Neer E. J. Heterotrimeric G proteins: organizers of transmembrane signals. Cell 1995; 80: 249–257
   PubMed Web of Science ®Google Scholar
• Brunton L. L., Mayer S. E. Extrusion of cyclic AMP from pigeon erythrocytes. J. Biol. Chem. 1979; 254: 9714–9720
   PubMedGoogle Scholar
• Berridge M. J., Irvine R. F. Inositol trisphosphate and diacylglycerol: two interacting second messengers. Annu. Rev. Biochem. 1987; 56: 159–193
   PubMed Web of Science ®Google Scholar
• Michell R. H., Drummond A. H., Downes C. P. Inositol Lipids in Cell Signalling. Academic Press, London 1989
   Google Scholar
• Divecha N., Irvine R. F. Phospholipid signaling. Cell 1995; 80: 269–278
   PubMed Web of Science ®Google Scholar
• Putney J. W. Advances in Second Messenger and Phosphoprotein Research: Inositol Phosphates and Calcium Signaling. Raven Press, New York 1992; 26
   Google Scholar
• Dennis E. A. Diversity of group types, regulation, and function of phospholipase A2. J. Biol. Chem. 1994; 269: 13057–13060
   PubMed Web of Science ®Google Scholar
• Mosior M., McLaughlin S. Peptides that mimic the pseudosubstrate region of protein kinase C bind to acidic lipids in membranes. Biophys. J. 1991; 60: 149–159
   PubMedGoogle Scholar
• Morris A. J., Engebrecht J., Frohman M. A. Structure and regulation of phospholipase D. Trends Pharmacol. Sci. 1996; 17: 182–185
   PubMed Web of Science ®Google Scholar
• Exton J. H. Phosphatidylcholine breakdown and signal transduction. Biochim. Biophys. Acta 1994; 1212: 26–42
   PubMed Web of Science ®Google Scholar
• English D. Phosphatidic acid: a lipid messenger involved in intracellular and extracellular signaling. Cell Signaling 1996; 8: 341–347
   PubMed Web of Science ®Google Scholar
• Singer W. D., Brown H. A., Jiang X., Sternweis P. C. Regulation of phospholipase D by protein kinase C is synergistic with ADP-ribosylation factor and independent of protein kinase activity. J. Biol. Chem. 1996; 271: 4504–4510
   PubMed Web of Science ®Google Scholar
• Cockcroft S., Thomas G. M.H., Fensome A., Geny B., Cunningham E., Gout I., et al. Phospholipase D: a downstream effector of ARF in granulocytes. Science 1994; 263: 523–526
   PubMed Web of Science ®Google Scholar
• Brown H. A., Gutowski S., Moomaw C. R., Slaughter C., Sternweis P. C. ADP-ribosylation factor, a small GTP-dependent regulatory protein, stimulates phospholipase D activity. Cell 1993; 75: 1137–1144
   PubMed Web of Science ®Google Scholar
• Ohguchi K., Banno Y., Nakashima S., Nozawa Y. Regulation of membrane-bound phospholipase D by protein kinase C in HL60 cells. J. Biol. Chem. 1996; 271: 4366–4372
   PubMedGoogle Scholar
• Singer W. D., Brown H. A., Bokoch G. M., Sternweis P. C. Resolved phospholipase D activity is modulated by cytosolic factors other than ARF. J. Biol. Chem. 1995; 270: 14944–14950
   PubMedGoogle Scholar
• Cockcroft S. Ca2+-dependent conversion of phosphatidylinositol to phosphatidate in neutrophils stimulated with fMet-Leu-Phe or ionophore A23187. Biochim. Biophys. Acta 1984; 795: 37–46
   PubMedGoogle Scholar
• Brown A. M. Membrane-delimited cell signaling complexes: direct ion channel regulation by G proteins. J. Membr. Biol. 1993; 131: 93–104
   PubMedGoogle Scholar
• Brini M., Marsault R., Bastianutto C., Alvarez J., Pozzan T., Rizzuto R. Transfected aequorin in the measurement of cytosolic Ca2+ concentration ([Ca2+]). J. Biol. Chem. 1995; 270: 9896–9903
   PubMed Web of Science ®Google Scholar
• Schroeder K. S., Neagle B. D. FLIPR: a new instrument for accurate, high throughput optical screening. J. Biomol. Screening 1996; 1: 75–80
   Google Scholar
• Hill C. S., Treisman R. Transcriptional regulation by extracellular signals: mechanisms and specificity. Cell 1995; 80: 199–211
   PubMed Web of Science ®Google Scholar
• Sista P., Edmiston S., Darges J. W., Robinson S., Burns D. J. A cell-based reporter assay for the identification of protein kinase C activators and inhibitors. Mol. Cell Biochem. 1994; 141: 129–134
   PubMedGoogle Scholar
• Chen W., Shields T. S., Stork P. J.S., Cone R. D. A colorimetric assay for measuring activation of Gs- and Gq-coupled signaling pathways. Anal. Biochem. 1995; 226: 349–354
   PubMedGoogle Scholar
• Dhundale A., Goddard C. Reporter assays in the high throughput screening laboratory: a rapid and robust first look?. J. Biomol. Screening 1996; 1: 115–118
   Google Scholar
• Bronstein I., Fortin J., Stanley P. E., Stewart G. S.A.B., Kricka L. J. Chemiluminescent and bioluminescent reporter gene assays. Anal. Biochem. 1994; 219: 169–181
   PubMed Web of Science ®Google Scholar
• Jayawickreme C. K., Graminski G. F., Quillan J. M., Lerner M. R. Creation and functional screening of a multi-use peptide library. Proc. Natl. Acad. Sci. USA 1994; 91: 1614–1618
   PubMed Web of Science ®Google Scholar
• Lerner M. R. Tools for investigating functional interactions between ligands and G-protein-coupled receptors. Trends Neurosci. 1994; 17: 142–146
   PubMedGoogle Scholar
• McConnell H. M., Owicki J. C., Parce J. W., Miller D. L., Baxter G. T., Wada H. G., et al. The cytosensor microphysiometer: biological applications of silicon technology. Science 1992; 257: 1906–1912
   PubMed Web of Science ®Google Scholar
• Boyer J. L., Zohn I., Jacobson K. A., Harden T. K. Differential effects of putative P2-purinergic receptor antagonists on adenylyl cyclase- and phospholipase C-coupled P2Y-purinergic receptors. Br. J. Pharmacol. 1994; 113: 614–620
   PubMedGoogle Scholar
• Boyer J. L., Schachter J. B., Romero T., Harden T. K. Identification of competitive antagonists of the P2Y1-purinergic receptor. Mol. Pharmacol. 1996; 50: 1323–1329
   PubMed Web of Science ®Google Scholar
• Bond R. A., Leff P., Johnson T. D., Milano C. A., Rockman H. A., McMinn T. R., et al. Physiological effects of inverse agonists in transgenic mice with myocardial overexpression of the β2-adrenoceptor. Nature 1995; 374: 272–276
   PubMed Web of Science ®Google Scholar
• Milligan G., Bond R. A., Lee M. Inverse agonism: pharmacological curiosity or potential therapeutic strategy?. Trends Pharmacol. Sci. 1995; 16: 10–13
   PubMed Web of Science ®Google Scholar
• Leff P. The two-state model of receptor activation. Trends Pharmacol. Sci. 1995; 16: 259–260
   PubMedGoogle Scholar
• Costa T., Herz A. Antagonists with negative intrinsic activity at δ opioid receptors coupled to GTP-binding proteins. Proc. Natl. Acad. Sci. USA 1989; 86: 7321–7325
   PubMed Web of Science ®Google Scholar