메뉴 건너뛰기




Volumn 43, Issue 2, 2009, Pages 53-61

Calmodulin interacts with PAC1 and VPAC2 receptors and regulates PACAP-induced FOS expression in human neuroblastoma cells

Author keywords

Chinese hamster ovary cells; co immunoprecipitation; FOS; G protein coupled receptors; Gene expression; Neuropeptides; Protein interaction; Signaling; W 5; W 7

Indexed keywords

CALCIUM; CALMODULIN; DUAL SPECIFICITY PHOSPHATASE 2; HYPOPHYSIS ADENYLATE CYCLASE ACTIVATING POLYPEPTIDE; MESSENGER RNA; N (6 AMINOHEXYL) 5 CHLORO 1 NAPHTHALENESULFONAMIDE; PROTEIN FOS; VASOACTIVE INTESTINAL POLYPEPTIDE RECEPTOR 2;

EID: 62949089891     PISSN: 01434179     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.npep.2009.02.001     Document Type: Article
Times cited : (6)

References (54)
  • 1
    • 0034899908 scopus 로고    scopus 로고
    • Calcium and pituitary adenylate cyclase-activating polypeptide induced expression of circadian clock gene mPer1 in the mouse cerebellar granule cell culture
    • Akiyama M., Minami Y., Nakajima T., Moriya T., and Shibata S. Calcium and pituitary adenylate cyclase-activating polypeptide induced expression of circadian clock gene mPer1 in the mouse cerebellar granule cell culture. J. Neurochem. 78 (2001) 499-508
    • (2001) J. Neurochem. , vol.78 , pp. 499-508
    • Akiyama, M.1    Minami, Y.2    Nakajima, T.3    Moriya, T.4    Shibata, S.5
  • 2
    • 0034692687 scopus 로고    scopus 로고
    • Binding of calmodulin to the D2-dopamine receptor reduces receptor signaling by arresting the G protein activation switch
    • Bofill-Cardona E., Kudlacek O., Yang Q., Ahorn H., Freissmuth M., and Nanoff C. Binding of calmodulin to the D2-dopamine receptor reduces receptor signaling by arresting the G protein activation switch. J. Biol. Chem. 275 (2000) 32672-32680
    • (2000) J. Biol. Chem. , vol.275 , pp. 32672-32680
    • Bofill-Cardona, E.1    Kudlacek, O.2    Yang, Q.3    Ahorn, H.4    Freissmuth, M.5    Nanoff, C.6
  • 3
    • 34548421934 scopus 로고    scopus 로고
    • Microarray analyses of pituitary adenylate cyclase activating polypeptide (PACAP)-regulated gene targets in sympathetic neurons
    • Braas K.M., Schutz K.C., Bond J.P., Vizzard M.A., Girard B.M., and May V. Microarray analyses of pituitary adenylate cyclase activating polypeptide (PACAP)-regulated gene targets in sympathetic neurons. Peptides 28 (2007) 1856-1870
    • (2007) Peptides , vol.28 , pp. 1856-1870
    • Braas, K.M.1    Schutz, K.C.2    Bond, J.P.3    Vizzard, M.A.4    Girard, B.M.5    May, V.6
  • 5
    • 0035132949 scopus 로고    scopus 로고
    • G-protein-coupled receptor kinase 3- and protein kinase C-mediated desensitization of the PACAP receptor type 1 in human Y-79 retinoblastoma cells
    • Dautzenberg F.M., and Hauger R.L. G-protein-coupled receptor kinase 3- and protein kinase C-mediated desensitization of the PACAP receptor type 1 in human Y-79 retinoblastoma cells. Neuropharmacology 40 (2001) 394-407
    • (2001) Neuropharmacology , vol.40 , pp. 394-407
    • Dautzenberg, F.M.1    Hauger, R.L.2
  • 6
    • 33947589410 scopus 로고    scopus 로고
    • PACAP type I receptor transactivation is essential for IGF-1 receptor signalling and antiapoptotic activity in neurons
    • Delcourt N., Thouvenot E., Chanrion B., Galéotti N., Jouin P., Bockaert J., and Marin P. PACAP type I receptor transactivation is essential for IGF-1 receptor signalling and antiapoptotic activity in neurons. EMBO J. 26 (2007) 1542-1551
    • (2007) EMBO J. , vol.26 , pp. 1542-1551
    • Delcourt, N.1    Thouvenot, E.2    Chanrion, B.3    Galéotti, N.4    Jouin, P.5    Bockaert, J.6    Marin, P.7
  • 7
    • 0029991047 scopus 로고    scopus 로고
    • Inactivation of NMDA receptors by direct interaction of calmodulin with the NR1 subunit
    • Ehlers M.D., Zhang S., Bernhadt J.P., and Huganir R.L. Inactivation of NMDA receptors by direct interaction of calmodulin with the NR1 subunit. Cell 84 (1996) 745-755
    • (1996) Cell , vol.84 , pp. 745-755
    • Ehlers, M.D.1    Zhang, S.2    Bernhadt, J.P.3    Huganir, R.L.4
  • 8
    • 22244457085 scopus 로고    scopus 로고
    • Altered calmodulin response to light in the suprachiasmatic nucleus of PAC1 receptor knockout mice revealed by proteomic analysis
    • Fahrenkrug J., Hannibal J., Honoré B., and Vorum H. Altered calmodulin response to light in the suprachiasmatic nucleus of PAC1 receptor knockout mice revealed by proteomic analysis. J. Mol. Neurosci. 25 (2005) 251-258
    • (2005) J. Mol. Neurosci. , vol.25 , pp. 251-258
    • Fahrenkrug, J.1    Hannibal, J.2    Honoré, B.3    Vorum, H.4
  • 9
    • 0034705347 scopus 로고    scopus 로고
    • Pituitary adelylate cyclase-activating peptide is an activator of vasoactive intestinal polypeptide gene transcription in human neuroblastoma cells
    • Georg B., and Fahrenkrug J. Pituitary adelylate cyclase-activating peptide is an activator of vasoactive intestinal polypeptide gene transcription in human neuroblastoma cells. Brain Res.: Mol. Brain Res. 79 (2000) 67-76
    • (2000) Brain Res.: Mol. Brain Res. , vol.79 , pp. 67-76
    • Georg, B.1    Fahrenkrug, J.2
  • 10
    • 33846616939 scopus 로고    scopus 로고
    • Lack of the PAC1 receptor alters the circadian expression of VIP mRNA in the suprachiasmatic nucleus of mice
    • Georg B., Hannibal J., and Fahrenkrug J. Lack of the PAC1 receptor alters the circadian expression of VIP mRNA in the suprachiasmatic nucleus of mice. Brain Res. 1135 (2007) 52-57
    • (2007) Brain Res. , vol.1135 , pp. 52-57
    • Georg, B.1    Hannibal, J.2    Fahrenkrug, J.3
  • 11
    • 0038412577 scopus 로고    scopus 로고
    • Microarray and suppression subtractive hybridization analyses of gene expression in pheochromocytoma cells reveal pleiotropic effects of pituitary adenylate cyclase-activating polypeptide on cell proliferation, survival, and adhesion
    • Grumolato L., Elkahloun A.G., Ghzili H., Alexandre D., Coulouarn C., Yon L., Salier J.P., Eiden L.E., Fournier A., Vaudry H., and Anouar Y. Microarray and suppression subtractive hybridization analyses of gene expression in pheochromocytoma cells reveal pleiotropic effects of pituitary adenylate cyclase-activating polypeptide on cell proliferation, survival, and adhesion. Endocrinology 144 (2003) 2368-2379
    • (2003) Endocrinology , vol.144 , pp. 2368-2379
    • Grumolato, L.1    Elkahloun, A.G.2    Ghzili, H.3    Alexandre, D.4    Coulouarn, C.5    Yon, L.6    Salier, J.P.7    Eiden, L.E.8    Fournier, A.9    Vaudry, H.10    Anouar, Y.11
  • 12
    • 0035400086 scopus 로고    scopus 로고
    • Dissociation between light-induced phase shift of the circadian rhythm and clock gene expression in mice lacking the pituitary adenylate cyclase activating polypeptide type 1 receptor
    • Hannibal J., Jamen F., Nielsen H.S., Journot L., Brabet P., and Fahrenkrug J. Dissociation between light-induced phase shift of the circadian rhythm and clock gene expression in mice lacking the pituitary adenylate cyclase activating polypeptide type 1 receptor. J. Neurosci. 21 (2001) 4883-4890
    • (2001) J. Neurosci. , vol.21 , pp. 4883-4890
    • Hannibal, J.1    Jamen, F.2    Nielsen, H.S.3    Journot, L.4    Brabet, P.5    Fahrenkrug, J.6
  • 13
    • 33846586382 scopus 로고    scopus 로고
    • Melanopsin changes in neonatal albino rat independent of rods and cones
    • Hannibal J., Georg B., and Fahrenkrug J. Melanopsin changes in neonatal albino rat independent of rods and cones. Neuroreport 18 (2007) 81-85
    • (2007) Neuroreport , vol.18 , pp. 81-85
    • Hannibal, J.1    Georg, B.2    Fahrenkrug, J.3
  • 15
    • 1542500762 scopus 로고    scopus 로고
    • The neuropeptides vasoactive intestinal peptide (VIP) and pituitary adenylate cyclase activating polypeptide (PACAP) modulate several biochemical pathways in human leukemic myeloid cells
    • Hayez N., Harfi I., Lema-Kisoka R., Svoboda M., Corazza F., and Sariban E. The neuropeptides vasoactive intestinal peptide (VIP) and pituitary adenylate cyclase activating polypeptide (PACAP) modulate several biochemical pathways in human leukemic myeloid cells. J. Neuroimmunol. 149 (2004) 167-181
    • (2004) J. Neuroimmunol. , vol.149 , pp. 167-181
    • Hayez, N.1    Harfi, I.2    Lema-Kisoka, R.3    Svoboda, M.4    Corazza, F.5    Sariban, E.6
  • 16
    • 0343374101 scopus 로고
    • N-(6-aminohexyl)-5-chloro-1-naphthalenesulfonamide, a calmodulin antagonist, inhibits cell proliferation
    • Hidaka H., Sasaki Y., Tanaka T., Endo T., Ohno S., Fujii Y., and Nagata T. N-(6-aminohexyl)-5-chloro-1-naphthalenesulfonamide, a calmodulin antagonist, inhibits cell proliferation. Proc. Natl. Acad. Sci. USA 78 (1981) 4354-4357
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 4354-4357
    • Hidaka, H.1    Sasaki, Y.2    Tanaka, T.3    Endo, T.4    Ohno, S.5    Fujii, Y.6    Nagata, T.7
  • 19
    • 7044239253 scopus 로고    scopus 로고
    • Transcriptome of pituitary adenylate cyclase-activating polypeptide-differentiated PC12 cells
    • Ishido M., and Masuo Y. Transcriptome of pituitary adenylate cyclase-activating polypeptide-differentiated PC12 cells. Regul. Peptides 123 (2004) 15-21
    • (2004) Regul. Peptides , vol.123 , pp. 15-21
    • Ishido, M.1    Masuo, Y.2
  • 21
    • 0024997541 scopus 로고
    • Photic and circadian regulation of c-fos gene expression in the hamster suprachiasmatic nucleus
    • Kornhauser J.M., Nelson D.E., Mayo K.E., and Takahashi J.S. Photic and circadian regulation of c-fos gene expression in the hamster suprachiasmatic nucleus. Neuron 5 (1990) 127-134
    • (1990) Neuron , vol.5 , pp. 127-134
    • Kornhauser, J.M.1    Nelson, D.E.2    Mayo, K.E.3    Takahashi, J.S.4
  • 22
    • 4644359972 scopus 로고    scopus 로고
    • 2+]i increase but not adenylate cyclase stimulation
    • 2+]i increase but not adenylate cyclase stimulation. Cell. Signal. 17 (2005) 17-24
    • (2005) Cell. Signal. , vol.17 , pp. 17-24
    • Langer, I.1    Robberecht, P.2
  • 23
    • 17844389615 scopus 로고    scopus 로고
    • Effect of inactivating mutations on phosphorylation and internalization of the human VPAC2 receptor
    • Langer I., Langlet C., and Robberecht P. Effect of inactivating mutations on phosphorylation and internalization of the human VPAC2 receptor. J. Mol. Endocrinol. 34 (2005) 405-414
    • (2005) J. Mol. Endocrinol. , vol.34 , pp. 405-414
    • Langer, I.1    Langlet, C.2    Robberecht, P.3
  • 25
    • 0036499476 scopus 로고    scopus 로고
    • Evidence for the direct interaction between calmodulin and the human epidermal growth factor receptor
    • Li H., and Villalobo A. Evidence for the direct interaction between calmodulin and the human epidermal growth factor receptor. Biochem. J. 362 (2002) 499-505
    • (2002) Biochem. J. , vol.362 , pp. 499-505
    • Li, H.1    Villalobo, A.2
  • 26
    • 0442292089 scopus 로고    scopus 로고
    • Endogenous calmodulin interacts with the epidermal growth factor receptor in living cells
    • Li H., Ruano M.J., and Villalobo A. Endogenous calmodulin interacts with the epidermal growth factor receptor in living cells. FEBS Lett. 559 (2004) 175-180
    • (2004) FEBS Lett. , vol.559 , pp. 175-180
    • Li, H.1    Ruano, M.J.2    Villalobo, A.3
  • 27
    • 33847029594 scopus 로고    scopus 로고
    • Evidence that calmodulin binding to the dopamine D2 receptor enhances receptor signaling
    • Liu Y., Buck D.C., Macey T.A., Lan H., and Neve K.A. Evidence that calmodulin binding to the dopamine D2 receptor enhances receptor signaling. J. Recept. Signal Transduct. Res. 27 (2007) 47-65
    • (2007) J. Recept. Signal Transduct. Res. , vol.27 , pp. 47-65
    • Liu, Y.1    Buck, D.C.2    Macey, T.A.3    Lan, H.4    Neve, K.A.5
  • 29
    • 0034680832 scopus 로고    scopus 로고
    • Identification of an essential amino acid motif within the C terminus of the pituitary adenylate cyclase-activating polypeptide type I receptor that is critical for signal transduction but not for receptor internalization
    • Lyu R.M., Germano P.M., Choi J.K., Le S.V., and Pisegna J.R. Identification of an essential amino acid motif within the C terminus of the pituitary adenylate cyclase-activating polypeptide type I receptor that is critical for signal transduction but not for receptor internalization. J. Biol. Chem. 275 (2000) 36134-36142
    • (2000) J. Biol. Chem. , vol.275 , pp. 36134-36142
    • Lyu, R.M.1    Germano, P.M.2    Choi, J.K.3    Le, S.V.4    Pisegna, J.R.5
  • 30
    • 33947386278 scopus 로고    scopus 로고
    • G protein-coupled receptors control NMDARs and metaplasticity in the hippocampus
    • MacDonald J.F., Jackson M.F., and Beazely M.A. G protein-coupled receptors control NMDARs and metaplasticity in the hippocampus. Biochim. Biophys. Acta 1768 (2007) 941-951
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 941-951
    • MacDonald, J.F.1    Jackson, M.F.2    Beazely, M.A.3
  • 31
    • 12744281523 scopus 로고    scopus 로고
    • Calmodulin interacts with the cytoplasmic tails of the parathyroid hormone 1 receptor and a sub-set of class b G-protein coupled receptors
    • Mahon M.J., and Shimada M. Calmodulin interacts with the cytoplasmic tails of the parathyroid hormone 1 receptor and a sub-set of class b G-protein coupled receptors. FEBS Lett. 579 (2005) 803-807
    • (2005) FEBS Lett. , vol.579 , pp. 803-807
    • Mahon, M.J.1    Shimada, M.2
  • 32
    • 0026564640 scopus 로고
    • Cyclic AMP accumulation alters calmodulin localization in SK-N-SH human neuroblastoma cells
    • Mangels L.A., and Gnegy M.E. Cyclic AMP accumulation alters calmodulin localization in SK-N-SH human neuroblastoma cells. Brain Res.: Mol. Brain Res. 12 (1992) 103-110
    • (1992) Brain Res.: Mol. Brain Res. , vol.12 , pp. 103-110
    • Mangels, L.A.1    Gnegy, M.E.2
  • 33
    • 0346366926 scopus 로고    scopus 로고
    • Serine 447 in the carboxyl tail of human VPAC1 receptor is crucial for agonist-induced desensitization but not internalization of the receptor
    • Marie J.C., Rouyer-Fessard C., Couvineau A., Nicole P., Devaud H., El Benna J., and Laburthe M. Serine 447 in the carboxyl tail of human VPAC1 receptor is crucial for agonist-induced desensitization but not internalization of the receptor. Mol. Pharmacol. 64 (2003) 1565-1574
    • (2003) Mol. Pharmacol. , vol.64 , pp. 1565-1574
    • Marie, J.C.1    Rouyer-Fessard, C.2    Couvineau, A.3    Nicole, P.4    Devaud, H.5    El Benna, J.6    Laburthe, M.7
  • 34
    • 0029017113 scopus 로고
    • Vasoactive intestinal peptide and pituitary adenylate cyclase-activating polypeptide potentiate c-fos expression induced by glutamate in cultured cortical neurons
    • Martin J.L., Gasser D., and Magistretti P.J. Vasoactive intestinal peptide and pituitary adenylate cyclase-activating polypeptide potentiate c-fos expression induced by glutamate in cultured cortical neurons. J. Neurochem. 65 (1995) 1-9
    • (1995) J. Neurochem. , vol.65 , pp. 1-9
    • Martin, J.L.1    Gasser, D.2    Magistretti, P.J.3
  • 35
    • 0028365872 scopus 로고
    • Vasoactive intestinal peptide/pituitary adenylate cyclase-activating peptide-dependent activation of membrane-bound NO synthase in smooth muscle mediated by pertussis toxin-sensitive Gi1-2
    • Murthy K.S., and Makhlouf G.M. Vasoactive intestinal peptide/pituitary adenylate cyclase-activating peptide-dependent activation of membrane-bound NO synthase in smooth muscle mediated by pertussis toxin-sensitive Gi1-2. J. Biol. Chem. 269 (1994) 15977-15980
    • (1994) J. Biol. Chem. , vol.269 , pp. 15977-15980
    • Murthy, K.S.1    Makhlouf, G.M.2
  • 36
    • 39349088096 scopus 로고    scopus 로고
    • Phosphorylation of GRK2 by PKA augments GRK2-mediated phosphorylation, internalization, and desensitization of VPAC2 receptors in smooth muscle
    • Murthy K.S., Mahavadi S., Huang J., Zhou H., and Sriwai W. Phosphorylation of GRK2 by PKA augments GRK2-mediated phosphorylation, internalization, and desensitization of VPAC2 receptors in smooth muscle. Am. J. Physiol. - Cell Physiol. 294 (2008) C477-C487
    • (2008) Am. J. Physiol. - Cell Physiol. , vol.294
    • Murthy, K.S.1    Mahavadi, S.2    Huang, J.3    Zhou, H.4    Sriwai, W.5
  • 37
    • 33750314184 scopus 로고    scopus 로고
    • Asn229 in the third helix of VPAC1 receptor is essential for receptor activation but not for receptor phosphorylation and internalization: comparison with Asn216 in VPAC2 receptor
    • Nachtergael I., Gaspard N., Langlet C., Robberecht P., and Langer I. Asn229 in the third helix of VPAC1 receptor is essential for receptor activation but not for receptor phosphorylation and internalization: comparison with Asn216 in VPAC2 receptor. Cell. Signal. 18 (2006) 2121-2130
    • (2006) Cell. Signal. , vol.18 , pp. 2121-2130
    • Nachtergael, I.1    Gaspard, N.2    Langlet, C.3    Robberecht, P.4    Langer, I.5
  • 38
    • 8744296089 scopus 로고    scopus 로고
    • Calmodulin interacts with the V2 vasopressin receptor: elimination of binding to the C terminus also eliminates arginine vasopressin-stimulated elevation of intracellular calcium
    • Nickols H.H., Shah V.N., Chazin W.J., and Limbird L.E. Calmodulin interacts with the V2 vasopressin receptor: elimination of binding to the C terminus also eliminates arginine vasopressin-stimulated elevation of intracellular calcium. J. Biol. Chem. 279 (2004) 46969-46980
    • (2004) J. Biol. Chem. , vol.279 , pp. 46969-46980
    • Nickols, H.H.1    Shah, V.N.2    Chazin, W.J.3    Limbird, L.E.4
  • 39
    • 3342884404 scopus 로고    scopus 로고
    • Transactivation of Trk neurotrophin receptors by G-protein-coupled receptor ligands occurs on intracellular membranes
    • Rajagopal R., Chen Z.Y., Lee F.S., and Chao M.V. Transactivation of Trk neurotrophin receptors by G-protein-coupled receptor ligands occurs on intracellular membranes. J. Neurosci. 24 (2004) 6650-6658
    • (2004) J. Neurosci. , vol.24 , pp. 6650-6658
    • Rajagopal, R.1    Chen, Z.Y.2    Lee, F.S.3    Chao, M.V.4
  • 41
    • 33746384584 scopus 로고    scopus 로고
    • Cycloheximide treatment to identify components of the transitional transcriptome in PACAP-induced PC12 cell differentiation
    • Ravni A., Eiden L.E., Vaudry H., Gonzalez B.J., and Vaudry D. Cycloheximide treatment to identify components of the transitional transcriptome in PACAP-induced PC12 cell differentiation. J. Neurochem. 98 (2006) 1229-1241
    • (2006) J. Neurochem. , vol.98 , pp. 1229-1241
    • Ravni, A.1    Eiden, L.E.2    Vaudry, H.3    Gonzalez, B.J.4    Vaudry, D.5
  • 43
    • 0037365177 scopus 로고    scopus 로고
    • Serotonin inhibits glutamate- but not PACAP-induced per gene expression in the rat suprachiasmatic nucleus at night
    • Sanggaard K.M., Hannibal J., and Fahrenkrug J. Serotonin inhibits glutamate- but not PACAP-induced per gene expression in the rat suprachiasmatic nucleus at night. Eur. J. Neurosci. 17 (2003) 1245-1252
    • (2003) Eur. J. Neurosci. , vol.17 , pp. 1245-1252
    • Sanggaard, K.M.1    Hannibal, J.2    Fahrenkrug, J.3
  • 44
    • 0030430746 scopus 로고    scopus 로고
    • Pituitary adenylate-cyclase-activating polypeptide stimulates proto-oncogene expression and activates the AP-1 (c-Fos/c-Jun) transcription factor in AR4-2J pancreatic carcinoma cells
    • Schäfer H., Zheng J., Gundlach F., Günther R., Siegel E.G., Fölsch U.R., and Schmidt W.E. Pituitary adenylate-cyclase-activating polypeptide stimulates proto-oncogene expression and activates the AP-1 (c-Fos/c-Jun) transcription factor in AR4-2J pancreatic carcinoma cells. Eur. J. Biochem. 242 (1996) 467-476
    • (1996) Eur. J. Biochem. , vol.242 , pp. 467-476
    • Schäfer, H.1    Zheng, J.2    Gundlach, F.3    Günther, R.4    Siegel, E.G.5    Fölsch, U.R.6    Schmidt, W.E.7
  • 45
    • 11144230455 scopus 로고    scopus 로고
    • Immunocytochemical identification of VPAC1, VPAC2, and PAC1 receptors in normal and neoplastic human tissues with subtype-specific antibodies
    • Schulz S., Röcken C., Mawrin C., Weise W., Höllt V., and Schulz S. Immunocytochemical identification of VPAC1, VPAC2, and PAC1 receptors in normal and neoplastic human tissues with subtype-specific antibodies. Clin. Cancer Res. 10 (2004) 8235-8242
    • (2004) Clin. Cancer Res. , vol.10 , pp. 8235-8242
    • Schulz, S.1    Röcken, C.2    Mawrin, C.3    Weise, W.4    Höllt, V.5    Schulz, S.6
  • 46
    • 34247189583 scopus 로고    scopus 로고
    • Membrane-permeable calmodulin inhibitors (e.g. W-7/W-13) bind to membranes, changing the electrostatic surface potential: dual effect of W-13 on epidermal growth factor receptor activation
    • Sengupta P., Ruano M.J., Tebar F., Golebiewska U., Zaitseva I., Enrich C., McLaughlin S., and Villalobo A. Membrane-permeable calmodulin inhibitors (e.g. W-7/W-13) bind to membranes, changing the electrostatic surface potential: dual effect of W-13 on epidermal growth factor receptor activation. J. Biol. Chem. 282 (2007) 8474-8486
    • (2007) J. Biol. Chem. , vol.282 , pp. 8474-8486
    • Sengupta, P.1    Ruano, M.J.2    Tebar, F.3    Golebiewska, U.4    Zaitseva, I.5    Enrich, C.6    McLaughlin, S.7    Villalobo, A.8
  • 47
    • 0037067693 scopus 로고    scopus 로고
    • Vasoactive intestinal polypeptide type-1 receptor regulation. Desensitization, phosphorylation, and sequestration
    • Shetzline M.A., Walker J.K., Valenzano K.J., and Premont R.T. Vasoactive intestinal polypeptide type-1 receptor regulation. Desensitization, phosphorylation, and sequestration. J. Biol. Chem. 277 (2002) 25519-25526
    • (2002) J. Biol. Chem. , vol.277 , pp. 25519-25526
    • Shetzline, M.A.1    Walker, J.K.2    Valenzano, K.J.3    Premont, R.T.4
  • 48
    • 0032587550 scopus 로고    scopus 로고
    • 2+/calmodulin-binding domain within the carboxyl-terminus of the angiotensin II (AT1A) receptor
    • 2+/calmodulin-binding domain within the carboxyl-terminus of the angiotensin II (AT1A) receptor. FEBS Lett. 455 (1999) 367-371
    • (1999) FEBS Lett. , vol.455 , pp. 367-371
    • Thomas, W.G.1    Pipolo, L.2    Qian, H.3
  • 49
    • 24744463670 scopus 로고    scopus 로고
    • Interaction of calmodulin with the serotonin 5-hydroxytryptamine2A receptor. A putative regulator of G protein coupling and receptor phosphorylation by protein kinase C
    • Turner J.H., and Raymond J.R. Interaction of calmodulin with the serotonin 5-hydroxytryptamine2A receptor. A putative regulator of G protein coupling and receptor phosphorylation by protein kinase C. J. Biol. Chem. 280 (2005) 30741-30750
    • (2005) J. Biol. Chem. , vol.280 , pp. 30741-30750
    • Turner, J.H.1    Raymond, J.R.2
  • 50
    • 2342425115 scopus 로고    scopus 로고
    • Calmodulin interacts with the third intracellular loop of the serotonin 5-hydroxytryptamine1A receptor at two distinct sites: putative role in receptor phosphorylation by protein kinase C
    • Turner J.H., Gelasco A.K., and Raymond J.R. Calmodulin interacts with the third intracellular loop of the serotonin 5-hydroxytryptamine1A receptor at two distinct sites: putative role in receptor phosphorylation by protein kinase C. J. Biol. Chem. 279 (2004) 17027-17037
    • (2004) J. Biol. Chem. , vol.279 , pp. 17027-17037
    • Turner, J.H.1    Gelasco, A.K.2    Raymond, J.R.3
  • 51
    • 0032431164 scopus 로고    scopus 로고
    • The neurotrophic activity of PACAP on rat cerebellar granule cells is associated with activation of the protein kinase A pathway and c-fos gene expression
    • Vaudry D., Basille M., Anouar Y., Fournier A., Vaudry H., and Gonzalez B.J. The neurotrophic activity of PACAP on rat cerebellar granule cells is associated with activation of the protein kinase A pathway and c-fos gene expression. Ann. NY Acad. Sci. 865 (1998) 92-99
    • (1998) Ann. NY Acad. Sci. , vol.865 , pp. 92-99
    • Vaudry, D.1    Basille, M.2    Anouar, Y.3    Fournier, A.4    Vaudry, H.5    Gonzalez, B.J.6
  • 52
    • 0034048147 scopus 로고    scopus 로고
    • Pituitary adenylate cyclase-activating polypeptide and its receptors: from structure to functions
    • Vaudry D., Gonzalez B.J., Basille M., Yon L., Fournier A., and Vaudry H. Pituitary adenylate cyclase-activating polypeptide and its receptors: from structure to functions. Pharmacol. Rev. 52 (2000) 269-324
    • (2000) Pharmacol. Rev. , vol.52 , pp. 269-324
    • Vaudry, D.1    Gonzalez, B.J.2    Basille, M.3    Yon, L.4    Fournier, A.5    Vaudry, H.6
  • 53
    • 0029861717 scopus 로고    scopus 로고
    • VIP and pituitary adenylate cyclase activating polypeptide (PACAP) have an antiproliferative effect on the T98G human glioblastoma cell line through interaction with VIP2 receptor
    • Vertongen P., Camby I., Darro F., Kiss R., and Robberecht P. VIP and pituitary adenylate cyclase activating polypeptide (PACAP) have an antiproliferative effect on the T98G human glioblastoma cell line through interaction with VIP2 receptor. Neuropeptides 30 (1996) 491-496
    • (1996) Neuropeptides , vol.30 , pp. 491-496
    • Vertongen, P.1    Camby, I.2    Darro, F.3    Kiss, R.4    Robberecht, P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.