In vitro selection of peptides acting at a new site of Nmda glutamate receptors

Nature Biotechnology

Volumn 14, Issue 8, 1996, Pages 986-991

  Li, Min ^b   Yu, Weifeng ^b   Chen, Chien Huan ^b   Cwirla, Steve ^a   Whitehorn, Erik ^a   Tate, Emily ^a   Raab, Ron ^a   Bremer, Meire ^a   Dower, Bill ^a  

^a AFFYMAX RESEARCH INSTITUTE   (United States)

^b JOHNS HOPKINS UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

GLUTAMATE RECEPTOR; N METHYL DEXTRO ASPARTIC ACID RECEPTOR;

ANIMAL CELL; ARTICLE; CALCIUM TRANSPORT; CHANNEL GATING; CHO CELL; LIGAND BINDING; NERVE CELL PLASTICITY; NEUROTOXICITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DETERMINATION; RECEPTOR DENSITY; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; ANIMALS; BRAIN; CELL LINE; CHO CELLS; CLONING, MOLECULAR; CRICETINAE; DIZOCILPINE MALEATE; EXCITATORY AMINO ACID ANTAGONISTS; HUMANS; MOLECULAR SEQUENCE DATA; MUTAGENESIS; PEPTIDES; PROTEIN BINDING; RATS; RECEPTORS, N-METHYL-D-ASPARTATE;

EID: 0029846632     PISSN: 10870156     EISSN: 15461696     Source Type: Journal    
DOI: 10.1038/nbt0896-986     Document Type: Article

References (45)

1. Choi, D.W. 1990. Possible mechanisms limiting N-methyl-O-aspartate receptor overactivation and the therapeutic efficacy of N-methyl-D-aspartate antagonists. Stroke 21:11120-22.
2. Bliss, T.V. and Collingridge, G.L. 1993. A synaptic model of memory: long-term potentiation in the hippocampus. Nature 361:31-39.
3. Hollmann, M. and Heinemann, S. 1994. Cloned glutamate receptors. Annu. Rev. Neurosci. 17:31-108.
4. Monaghan, D.T., Bridges, R.J., and Cotman, C.W. 1989. The excitatory amino acid receptors: their classes, pharmacology, and distinct properties in the function of the central nervous system. Annu. Rev. Pharmacol. Toxicol. 29:365-402.
5. Nakanishi, S. 1992. Molecular diversity of glutamate receptors and implications for brain function. Science 258:597-603.
6. Moriyoshi, K., et al. 1991. Molecular cloning and characterization of the rat NMDA receptor. Nature 354:31-37.
7. Johnson, J.W. and Ascher, P. 1987. Glycine potentiates the NMDA response in cultured mouse brain neurons. Nature 325:529-531.
8. Mayer, M.L., Westbrook, G.L., and Guthrie, RB. 1984. Voltage-dependent block by Mg2+ of NMDA responses in spinal cord neurones. Nature 309:261-263.
9. McGurk, J.F., Bennett, M.V., and Zukin, R.S. 1990. Polyamines potentiate responses of N-methyl-D-aspartate receptors expressed in xenopus oocytes. Proc. Natl. Acad. Sci. USA 87:9971-9974.
10. Nowak, L, Bregestovski, P., Ascher, P., Herbet, A., and Prochiantz, A. 1984. Magnesium gates glutamate-activated channels in mouse central neurones. Nature 307:462-465.
11. Peters, S., Koh, J., and Choi, D.W. 1987. Zinc selectively blocks the action of N-methyl-D-aspartate on cortical neurons. Science 236:589-593.
12. Westbrook, G.L. and Mayer, M.L. 1987. Micromolar concentrations of Zn2+ antagonize NMDA and GABA responses of hippocampal neurons. Nature 328:640-643.
13. Wong, E.H., et al. 1986. The anticonvulsant MK-801 is a potent N-methyl-D-aspartate antagonist. Proc. Natl. Acad. Sci. USA 83:7104-7108.
14. Smith, G.P. 1985. Filamentous fusion phage: novel expression vectors that display cloned antigens on the virion surface. Science 228:1315-1317.
15. Scott, J.K. and Smith, G.P. 1990. Searching for peptide ligands with an epitope library. Science 249:386-390.
16. Devlin, J.J., Panganiban, L.C., and Devlin, P.E. 1990. Random peptide libraries: a source of specific protein binding molecules. Science 249:404-406.
17. Cwirla, S.E., Peters, E.A., Barrett, R.W., and Dower, W.J. 1990. Peptides on phage: a vast library of peptides for identifying ligands. Proc. Natl. Acad. Sci. USA 87:6378-6382.
18. Whitehorn, E.A., Tate, E., Yanofsky, S.D., Kochersperger, L, Davis, A., Mortensen, R.B., et al. 1995. A generic method for expression and use of “tagged” soluble versions of cell surface receptors. Bio/Technology 13:1215-1219.
19. Chazot, P.L., Cik, M., and Stephenson, F.A. 1992. Immunological detection of the NMDAR1 glutamate receptor subunit expressed in embryonic kidney 293 cells and in rat brain. J. Neurochem. 59:1176-1178.
20. Barrett, R.W., et al. 1992. Selective enrichment and characterization of high affinity ligands from collections of random peptides on filamentous phage. Anal. Biochem. 204:357-364.
21. Hollmann, M., O’Shea-Greenfield, A., Rogers, S.W., and Heinemann, S. 1989. Cloning by functional expression of a member of the glutamate receptor family. Nature 342:643-648.
22. Hollmann, M., et al. 1993. Zinc potentiates agonist-induced currents at certain splice variants of the NMDA receptor. Neuron 10:943-954.
23. Haack, J.A., et al. 1990. Conantokin-T. A gamma-carboxyglutamate containing peptide with N-methyl-D-aspartate antagonist activity. J. Biol. Chem. 265:6025-6029.
24. Huettner, J.E. and Bean, B.P. 1988. Block of N-methyl-D-aspartate-activated current by the anticonvulsant MK-801: selective binding to open channels. Proc. Natl. Acad. Sci. USA 85:1307-1311.
25. Mori, H., Masakl, H., Yamakura, T, and Mishina, M. 1992. Identification by mutagenesis of a Mg(2+)-block site of the NMDA receptor channel. Nature 358:673-675.
26. Monyer, H., et al. 1992. Heteromeric NMDA receptors: molecular and functional distinction of subtypes. Science 256:1217-1221.
27. Tingley, W.G., Roche, K.W., Thompson, A.K., and Huganir, R.L. 1993. Regulation of NMDA receptor phosphorylation by alternative splicing of the C-terminal domain. Nature 364:70-73.
28. Kutsuwada, T, et al. 1992. Molecular diversity of the NMDA receptor channel. Nature 358:36-41.
29. Lucas, D.R. and Newhouse, J. 1957. The toxic effect of sodium L-glutamate on the inner layers of retina. Arch. Ophthalmol. 58:193-204.
30. Choi, D.W. and Rothman, S.M. 1990. The role of glutamate neurotoxicity in hypoxic-ischemic neuronal death. Annu. Rev. Neurosci. 13:171-182.
31. Miller, R.J., Murphy, S.N., and Glaum, S.R. 1989. Neuronal Ca2+ channels and their regulation by excitatory amino acids. Ann. NY Acad. Sci. 568:149-158.
32. Young, A.B., Penney, J.B., Dauth, G.W., Bromberg, M.B., and Gilman, S. 1983. Glutamate or aspartate as a possible neurotransmitter of cerebral corticofugal fibers in the monkey. Neurology 33:1513-1516.
33. Rothstein, J.D., et al. 1991. Excitatory amino acids in amyotrophic lateral sclerosis: an update. Ann. Neurol. 30:224-225.
34. Rothstein, J.D., Martin, L.J., and Kuncl, R.W. 1992. Decreased glutamate transport by the brain and spinal cord in amyotrophic lateral sclerosis. N. Engl. J. Med. 326:1464-1468.
35. Rothstein, J.D., Jin, L, Dykes-Hoberg, M., and Kuncl, R.W. 1993. Chronic inhibition of glutamate uptake produces a model of slow neurotoxicity. Proc. Natl. Acad. Sci. USA 90:6591-6595.
36. Rothstein, J.D., et al. 1994. Localization of neuronal and glial glutamate transporters. Neuron 13:713-725.
37. Storm-Mathisen, J. and Ottersen, O.P. 1987. Tracing of neurons with glutamate or gamma-aminobutyrate as putative transmitters. Biochem. Soc. Trans. 15:210-213.
38. Storm-Mathisen, J. and Ottersen, O.R 1990. Immunocytochemistry of glutamate at the synaptic level. J. Histochem. Cytochem. 38:1733-1743.
39. O’Brien, R.J. and Fischbach, G.D. 1986. Modulation of embryonic chick motoneuron glutamate sensitivity by intemeurons and agonists. J. Neurosci. 6:3290-3296.
40. Tsai, G.C., et al. 1991. Reductions in acidic amino acids and N-acetylaspartylglu-tamate in amyotrophic lateral sclerosis CNS. Brain Res. 556:151-156.
41. Shaw, P.J. 1994. Excitotoxicity and motor neurone disease: a review of the evidence. J. Neurol. Sci. 124:6-13.
42. Shaw, P.J. 1994. Excitotoxicity and motor neurone disease: a review of the evidence. J. Neurol. Sci. 124:6-13.
43. Upton, S.A. and Stamler, J.S. 1994. Actions of redox-related congeners of nitric oxide at the NMDA receptor. Neuropharmacology 33:1229-12233.
44. Li, M., Jan, Y.N., and Jan, L.Y. 1992. Specification of subunit assembly by the hydrophilic amino-terminal domain of the Shaker potassium channel. Science 257:1225-1230.
45. Guzman, L.M., Belin, D., Carson, M.J., and Beckwith, J. 1995. Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter. J. Bacterid. 177:4121-4130.