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Volumn 335, Issue 1, 1997, Pages 65-72

The rat mGlu(1d) receptor splice variant shares functional properties with the other short isoforms of mGlu1 receptor

Author keywords

Alternative splicing; Constitutive activity; G protein coupled receptor; Metabotropic glutamate receptor; Phospholipase C coupling

Indexed keywords

1 AMINO 1,3 CYCLOPENTANEDICARBOXYLIC ACID; GLUTAMIC ACID; METABOTROPIC RECEPTOR; PHOSPHOLIPASE C; QUISQUALIC ACID; COMPLEMENTARY DNA;

EID: 0030609103     PISSN: 00142999     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-2999(97)01155-2     Document Type: Article
Times cited : (28)

References (36)
  • 1
    • 0026596597 scopus 로고
    • Signal transduction and pharmacological characteristics of a metabotropic glutamate receptor, mGluR1, in transfected CHO cells
    • Aramori I., Nakanishi S. Signal transduction and pharmacological characteristics of a metabotropic glutamate receptor, mGluR1, in transfected CHO cells. Neuron. 8:1992;757-765.
    • (1992) Neuron , vol.8 , pp. 757-765
    • Aramori, I.1    Nakanishi, S.2
  • 3
    • 0030995878 scopus 로고    scopus 로고
    • Pharmacology and functions of metabotropic glutamate receptors
    • Conn P., Pin J.-P. Pharmacology and functions of metabotropic glutamate receptors. Ann. Rev. Pharmacol. Toxicol. 37:1997;205-237.
    • (1997) Ann. Rev. Pharmacol. Toxicol. , vol.37 , pp. 205-237
    • Conn, P.1    Pin, J.-P.2
  • 5
    • 0030010985 scopus 로고    scopus 로고
    • The C-terminal domain of the mGluR1 metabotropic glutamate receptor affects sensitivity to agonists
    • Flor P.J., Gomeza J., Tones M.A., Kuhn R., Pin J.P., Knöpfel T. The C-terminal domain of the mGluR1 metabotropic glutamate receptor affects sensitivity to agonists. J. Neurochem. 67:1996;58-63.
    • (1996) J. Neurochem. , vol.67 , pp. 58-63
    • Flor, P.J.1    Gomeza, J.2    Tones, M.A.3    Kuhn, R.4    Pin, J.P.5    Knöpfel, T.6
  • 6
    • 0026503927 scopus 로고
    • Differential activation of intracellular effector by two isoforms of human neurokinin-1 receptor
    • Fong T.M., Anderson S.A., Yu H., Huang R.-R., Strader C.D. Differential activation of intracellular effector by two isoforms of human neurokinin-1 receptor. Mol. Pharmacol. 41:1992;24-30.
    • (1992) Mol. Pharmacol. , vol.41 , pp. 24-30
    • Fong, T.M.1    Anderson, S.A.2    Yu, H.3    Huang, R.-R.4    Strader, C.D.5
  • 7
    • 0027284829 scopus 로고
    • Carboxyl domain of glutamate receptor directs its coupling to metabolic pathways
    • Gabellini N., Manev R.M., Candeo P., Favaron M., Manev H. Carboxyl domain of glutamate receptor directs its coupling to metabolic pathways. NeuroReport. 4:1993;531-534.
    • (1993) NeuroReport , vol.4 , pp. 531-534
    • Gabellini, N.1    Manev, R.M.2    Candeo, P.3    Favaron, M.4    Manev, H.5
  • 8
    • 0028332673 scopus 로고
    • Is the heterologous expression of metabotropic glutamate receptors (mGluRs) an appropriate method to study the mGluR function? Experience with human embryonic kidney 293 cells transfected with mGluR1
    • Gabellini N., Manev R.M., Manev H. Is the heterologous expression of metabotropic glutamate receptors (mGluRs) an appropriate method to study the mGluR function? Experience with human embryonic kidney 293 cells transfected with mGluR1. Neurochem. Int. 24:1994;533-539.
    • (1994) Neurochem. Int. , vol.24 , pp. 533-539
    • Gabellini, N.1    Manev, R.M.2    Manev, H.3
  • 9
    • 0030050977 scopus 로고    scopus 로고
    • The second intracellular loop of mGluR1 cooperates with the other intracellular domains to control coupling to G-protein
    • Gomeza J., Joly C., Kuhn R., Knöpfel T., Bockaert J., Pin J.-P. The second intracellular loop of mGluR1 cooperates with the other intracellular domains to control coupling to G-protein. J. Biol. Chem. 271:1996;2199-2205.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2199-2205
    • Gomeza, J.1    Joly, C.2    Kuhn, R.3    Knöpfel, T.4    Bockaert, J.5    Pin, J.-P.6
  • 10
    • 0029908501 scopus 로고    scopus 로고
    • Coupling of mGluR2 and mGluR4 to Gα15, Gα16 and chimeric Gαq/i proteins: Characterization of new antagonists
    • Gomeza J., Mary S., Brabet I., Parmentier M.-L., Restituito S., Bockaert J., Pin J.-P. Coupling of mGluR2 and mGluR4 to Gα15, Gα16 and chimeric Gαq/i proteins: Characterization of new antagonists. Mol. Pharmacol. 50:1996;923-930.
    • (1996) Mol. Pharmacol. , vol.50 , pp. 923-930
    • Gomeza, J.1    Mary, S.2    Brabet, I.3    Parmentier, M.-L.4    Restituito, S.5    Bockaert, J.6    Pin, J.-P.7
  • 11
    • 0028319159 scopus 로고
    • Characterization of two alternatively spliced forms of a metabotropic glutamate receptor in the central nervous system of the rat
    • Hampson D.R., Theriault E., Huang X.P., Kristensen P., Pickering D.S., Franck J.E., Mulvihill E.R. Characterization of two alternatively spliced forms of a metabotropic glutamate receptor in the central nervous system of the rat. Neuroscience. 60:1994;325-336.
    • (1994) Neuroscience , vol.60 , pp. 325-336
    • Hampson, D.R.1    Theriault, E.2    Huang, X.P.3    Kristensen, P.4    Pickering, D.S.5    Franck, J.E.6    Mulvihill, E.R.7
  • 13
    • 0029043591 scopus 로고
    • Molecular, functional and pharmacological characterization of the metabotropic glutamate receptor type 5 splice variants: Comparison with mGluR1
    • Joly C., Gomeza J., Brabet I., Curry K., Bockaert J., Pin J.-P. Molecular, functional and pharmacological characterization of the metabotropic glutamate receptor type 5 splice variants: Comparison with mGluR1. J. Neurosci. 15:1995;3970-3981.
    • (1995) J. Neurosci. , vol.15 , pp. 3970-3981
    • Joly, C.1    Gomeza, J.2    Brabet, I.3    Curry, K.4    Bockaert, J.5    Pin, J.-P.6
  • 15
    • 0027328071 scopus 로고
    • Charged amino acids required for signal transduction by the m3 muscarinic acetylcholine receptor
    • Kunkel M.T., Peralta E.G. Charged amino acids required for signal transduction by the m3 muscarinic acetylcholine receptor. EMBO J. 12:1993;3809-3815.
    • (1993) EMBO J. , vol.12 , pp. 3809-3815
    • Kunkel, M.T.1    Peralta, E.G.2
  • 16
    • 0029670666 scopus 로고    scopus 로고
    • HmGlu1d, a novel splice variant of the human type-I metabotropic glutamate receptor
    • Laurie D.J., Boddeke H.W.G.M., Hiltscher R., Sommer B. HmGlu1d, a novel splice variant of the human type-I metabotropic glutamate receptor. Eur. J. Pharmacol. 296:1996;R1-R3.
    • (1996) Eur. J. Pharmacol. , vol.296 , pp. 1-R3
    • Laurie, D.J.1    Boddeke, H.W.G.M.2    Hiltscher, R.3    Sommer, B.4
  • 17
    • 0025600997 scopus 로고
    • Distinct sequence elements control the specificity of G protein activation by muscarinic acetylcholine receptor subtypes
    • Lechleiter J., Hellmiss R., Duerson K., Ennulat D., David N., Clapham D., Peralta E. Distinct sequence elements control the specificity of G protein activation by muscarinic acetylcholine receptor subtypes. EMBO J. 9:1990;4381-4390.
    • (1990) EMBO J. , vol.9 , pp. 4381-4390
    • Lechleiter, J.1    Hellmiss, R.2    Duerson, K.3    Ennulat, D.4    David, N.5    Clapham, D.6    Peralta, E.7
  • 18
    • 0025730818 scopus 로고
    • Subcellular patterns of calcium release determined by G protein-specific residues of muscarinic receptors
    • Lechleiter J., Girard S., Clapham D., Peralta E. Subcellular patterns of calcium release determined by G protein-specific residues of muscarinic receptors. Nature. 350:1991;505-508.
    • (1991) Nature , vol.350 , pp. 505-508
    • Lechleiter, J.1    Girard, S.2    Clapham, D.3    Peralta, E.4
  • 19
    • 0026093312 scopus 로고
    • Sequence and expression of a metabotropic glutamate receptor
    • Masu M., Tanabe Y., Tsuchida K., Shigemoto R., Nakanishi S. Sequence and expression of a metabotropic glutamate receptor. Nature. 349:1991;760-765.
    • (1991) Nature , vol.349 , pp. 760-765
    • Masu, M.1    Tanabe, Y.2    Tsuchida, K.3    Shigemoto, R.4    Nakanishi, S.5
  • 20
    • 0027938848 scopus 로고
    • Metabotropic glutamate receptors: Synaptic transmission, modulation, and plasticity
    • Nakanishi S. Metabotropic glutamate receptors: Synaptic transmission, modulation, and plasticity. Neuron. 13:1994;1031-1037.
    • (1994) Neuron , vol.13 , pp. 1031-1037
    • Nakanishi, S.1
  • 23
    • 0028912822 scopus 로고
    • The metabotropic glutamate receptors: Structure and functions
    • Pin J.-P., Duvoisin R. The metabotropic glutamate receptors: Structure and functions. Neuropharmacology. 34:1995;1-26.
    • (1995) Neuropharmacology , vol.34 , pp. 1-26
    • Pin, J.-P.1    Duvoisin, R.2
  • 24
    • 0026476478 scopus 로고
    • Alternative splicing generates metabotropic glutamate receptors inducing different patterns of calcium release in Xenopus oocytes
    • Pin J.-P., Waeber C., Prézeau L., Bockaert J., Heinemann S.F. Alternative splicing generates metabotropic glutamate receptors inducing different patterns of calcium release in Xenopus oocytes. Proc. Natl. Acad. Sci. USA. 89:1992;10331-10335.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10331-10335
    • Pin, J.-P.1    Waeber, C.2    Prézeau, L.3    Bockaert, J.4    Heinemann, S.F.5
  • 25
    • 0028012253 scopus 로고
    • Domains involved in the specificity of G protein activation in phospholipase C coupled metabotropic glutamate receptor
    • Pin J.-P., Joly C., Heinemann S.F., Bockaert J. Domains involved in the specificity of G protein activation in phospholipase C coupled metabotropic glutamate receptor. EMBO J. 13:1994;342-348.
    • (1994) EMBO J. , vol.13 , pp. 342-348
    • Pin, J.-P.1    Joly, C.2    Heinemann, S.F.3    Bockaert, J.4
  • 26
    • 0342951609 scopus 로고    scopus 로고
    • The metabotropic glutamate receptors: Differences and similarities with the other G-protein coupled receptors
    • In: Schwartz, T.W., Hjorth, S.A., Sandholm Kastrup, J. (Eds.), Munksgaard, Copenhagen
    • Pin, J.-P., Gomeza, J., Prézeau, L., Joly, C., Bockaert, J., 1996. The metabotropic glutamate receptors: Differences and similarities with the other G-protein coupled receptors. In: Schwartz, T.W., Hjorth, S.A., Sandholm Kastrup, J. (Eds.), Alfred Benzon Symposium 39 - Structure and Function of 7TM Receptors. Munksgaard, Copenhagen, pp. 343-356.
    • (1996) Alfred Benzon Symposium 39 - Structure and Function of 7TM Receptors , pp. 343-356
    • Pin, J.-P.1    Gomeza, J.2    Prézeau, L.3    Joly, C.4    Bockaert, J.5
  • 27
    • 0026555152 scopus 로고
    • PCR amplification of long DNA fragments
    • Ponce M., Micol J. PCR amplification of long DNA fragments. Nucleic Acids Res. 20:1992;623.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 623
    • Ponce, M.1    Micol, J.2
  • 28
    • 0029963929 scopus 로고    scopus 로고
    • Changes of the C-terminal domain of mGluR1 by alternative splicing generate receptors with different agonist independent activity
    • Prézeau L., Gomeza J., Ahern S., Mary S., Galvez T., Bockaert J., Pin J.-P. Changes of the C-terminal domain of mGluR1 by alternative splicing generate receptors with different agonist independent activity. Mol. Pharmacol. 49:1996;422-429.
    • (1996) Mol. Pharmacol. , vol.49 , pp. 422-429
    • Prézeau, L.1    Gomeza, J.2    Ahern, S.3    Mary, S.4    Galvez, T.5    Bockaert, J.6    Pin, J.-P.7
  • 29
    • 0029903640 scopus 로고    scopus 로고
    • Metabotropic glutamate receptor 5 is a disulfide-linked dimer
    • Romano C., Yang W.-L., O'Malley K.L. Metabotropic glutamate receptor 5 is a disulfide-linked dimer. J. Biol. Chem. 271:1996;28612-28616.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28612-28616
    • Romano, C.1    Yang, W.-L.2    O'Malley, K.L.3
  • 31
    • 0005438046 scopus 로고
    • Functional characterization of metabotropic glutamate receptor subtypes
    • Simoncini L., Haldeman B.A., Yamagiwa T., Mulvihill E. Functional characterization of metabotropic glutamate receptor subtypes. Biophys. J. 64:1993;A84.
    • (1993) Biophys. J. , vol.64 , pp. 84
    • Simoncini, L.1    Haldeman, B.A.2    Yamagiwa, T.3    Mulvihill, E.4
  • 33
    • 0027282265 scopus 로고
    • Role of the large extracellular domain of metabotropic glutamate receptors in agonist selectivity determination
    • Takahashi K., Tsuchida K., Tanabe Y., Masu M., Nakanishi S. Role of the large extracellular domain of metabotropic glutamate receptors in agonist selectivity determination. J. Biol. Chem. 268:1993;19341-19345.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19341-19345
    • Takahashi, K.1    Tsuchida, K.2    Tanabe, Y.3    Masu, M.4    Nakanishi, S.5
  • 35
    • 0030152970 scopus 로고    scopus 로고
    • Metabotropic glutamate receptor subtype 1A activates adenylate cyclase when expressed in baby hamster kidney cells
    • Thomsen C. Metabotropic glutamate receptor subtype 1A activates adenylate cyclase when expressed in baby hamster kidney cells. Prog. Neuro-Psych. Biol. Psych. 20:1996;709-726.
    • (1996) Prog. Neuro-Psych. Biol. Psych. , vol.20 , pp. 709-726
    • Thomsen, C.1
  • 36
    • 0029554137 scopus 로고
    • The agonist selectivity of a class III metabotropic glutamate receptor, human mGluR4a, is determined by the N-terminal extracellular domain
    • Tones M.A., Bendali H., Flor P.J., Knopfel T., Kuhn R. The agonist selectivity of a class III metabotropic glutamate receptor, human mGluR4a, is determined by the N-terminal extracellular domain. Neuroreport. 7:1995;117-120.
    • (1995) Neuroreport , vol.7 , pp. 117-120
    • Tones, M.A.1    Bendali, H.2    Flor, P.J.3    Knopfel, T.4    Kuhn, R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.