메뉴 건너뛰기




Volumn 134, Issue 3, 2008, Pages 285-292

Mevalonate sensitizes the nociceptive transmission in the mouse spinal cord

Author keywords

Antinociception; Geranylgeranylation; Mevalonate; RhoA; Spinal cord; Translocation

Indexed keywords

4 (1 AMINOETHYL) N (4 PYRIDYL)CYCLOHEXANECARBOXAMIDE; ENZYME INHIBITOR; FORMALDEHYDE; GGTI 2133; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE; MEVALONIC ACID; N [[5 [(2 AMINO 3 MERCAPTOPROPYL)AMINO][1,1' BIPHENYL] 2 YL]CARBONYL]METHIONINE METHYL ESTER; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN; SIMVASTATIN; UNCLASSIFIED DRUG;

EID: 37849030255     PISSN: 03043959     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pain.2007.04.031     Document Type: Article
Times cited : (18)

References (36)
  • 1
    • 0019887744 scopus 로고
    • Phase separation of integral membrane proteins in Triton X-114 solution
    • Bordier C. Phase separation of integral membrane proteins in Triton X-114 solution. J Biol Chem 256 (1981) 1604-1607
    • (1981) J Biol Chem , vol.256 , pp. 1604-1607
    • Bordier, C.1
  • 2
    • 0035913909 scopus 로고    scopus 로고
    • Regulating axon branch stability: the role of p190 RhoGAP in repressing a retraction signaling pathway
    • Billuart P., Winter C.G., Maresh A., Zhao X., and Liqun L. Regulating axon branch stability: the role of p190 RhoGAP in repressing a retraction signaling pathway. Cell 107 (2001) 195-207
    • (2001) Cell , vol.107 , pp. 195-207
    • Billuart, P.1    Winter, C.G.2    Maresh, A.3    Zhao, X.4    Liqun, L.5
  • 3
    • 0029966304 scopus 로고    scopus 로고
    • Protein prenyltransferases
    • Casey P.J., and Seabra M.C. Protein prenyltransferases. J Biol Chem 271 (1996) 5289-5292
    • (1996) J Biol Chem , vol.271 , pp. 5289-5292
    • Casey, P.J.1    Seabra, M.C.2
  • 5
    • 0025120211 scopus 로고
    • Regulation of the mevalonate pathway
    • Goldstein J.L., and Brown M.S. Regulation of the mevalonate pathway. Nature 343 (1990) 425-430
    • (1990) Nature , vol.343 , pp. 425-430
    • Goldstein, J.L.1    Brown, M.S.2
  • 6
    • 0024465343 scopus 로고
    • Post-translational processing of p21ras is two-step and involves carboxyl-methylation and carboxy-terminal proteolysis
    • Gutierrez L., Magee A.I., Marshall C.J., and Hancock J.F. Post-translational processing of p21ras is two-step and involves carboxyl-methylation and carboxy-terminal proteolysis. EMBO J 8 (1989) 1093-1098
    • (1989) EMBO J , vol.8 , pp. 1093-1098
    • Gutierrez, L.1    Magee, A.I.2    Marshall, C.J.3    Hancock, J.F.4
  • 8
    • 0023223448 scopus 로고
    • The formalin test in mice: dissociation between inflammatory and non-inflammatory pain
    • Hunskarr S., and Hole K. The formalin test in mice: dissociation between inflammatory and non-inflammatory pain. Pain 30 (1987) 103-114
    • (1987) Pain , vol.30 , pp. 103-114
    • Hunskarr, S.1    Hole, K.2
  • 9
    • 0018956018 scopus 로고
    • Intrathecal morphine in mice: a new technique
    • Hylden J.L., and Wilcox G.L. Intrathecal morphine in mice: a new technique. Eur J Pharmacol 67 (1980) 313-316
    • (1980) Eur J Pharmacol , vol.67 , pp. 313-316
    • Hylden, J.L.1    Wilcox, G.L.2
  • 10
    • 0036077667 scopus 로고    scopus 로고
    • Inhibition of rho-kinase-induced myristoylated alanine-rich C kinase substrate (MARCKS) phosphorylation in human neuronal cells by H-1152, a novel and specific Rho-kinase inhibitor
    • Ikenoya M., Hidaka H., Hosoya T., Suzuki M., Yamamoto N., and Sasaki Y. Inhibition of rho-kinase-induced myristoylated alanine-rich C kinase substrate (MARCKS) phosphorylation in human neuronal cells by H-1152, a novel and specific Rho-kinase inhibitor. J Neurochem 81 (2002) 9-16
    • (2002) J Neurochem , vol.81 , pp. 9-16
    • Ikenoya, M.1    Hidaka, H.2    Hosoya, T.3    Suzuki, M.4    Yamamoto, N.5    Sasaki, Y.6
  • 11
    • 3142685946 scopus 로고    scopus 로고
    • Initiation of neuropathic pain requires lysophosphatidic acid receptor signaling
    • Inoue M., Rashid M.H., Fujita R., Contos J.J.A., Chun J., and Ueda H. Initiation of neuropathic pain requires lysophosphatidic acid receptor signaling. Nat Med 10 (2004) 712-718
    • (2004) Nat Med , vol.10 , pp. 712-718
    • Inoue, M.1    Rashid, M.H.2    Fujita, R.3    Contos, J.J.A.4    Chun, J.5    Ueda, H.6
  • 12
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 13
    • 0028973293 scopus 로고
    • Ras CAAX peptidomimetic FTI-277 selectively blocks oncogenic ras signaling by inducing cytoplasmic accumulation of inactive ras-raf complexes
    • Lerner E.C., Quan Y., Blaskovich M.A., Fossum R.D., Vogt A., Sun J., et al. Ras CAAX peptidomimetic FTI-277 selectively blocks oncogenic ras signaling by inducing cytoplasmic accumulation of inactive ras-raf complexes. J Biol Chem 270 (1995) 26802-26806
    • (1995) J Biol Chem , vol.270 , pp. 26802-26806
    • Lerner, E.C.1    Quan, Y.2    Blaskovich, M.A.3    Fossum, R.D.4    Vogt, A.5    Sun, J.6
  • 14
    • 0034006173 scopus 로고    scopus 로고
    • Rho GTPases regulate distinct aspects of dendritic arbor growth in Xenopus central neurons in vivo
    • Li Z., Van Aelst L., and Cline H.T. Rho GTPases regulate distinct aspects of dendritic arbor growth in Xenopus central neurons in vivo. Nat Neurosci 3 (2000) 217-225
    • (2000) Nat Neurosci , vol.3 , pp. 217-225
    • Li, Z.1    Van Aelst, L.2    Cline, H.T.3
  • 15
    • 0030026182 scopus 로고    scopus 로고
    • Differential effects of the Rac GTPase on Purkinje cell axons and dendritic trunks and spines
    • Luo L., Hensch T.K., Ackerman L., Barbel S., Jan L.Y., and Jan Y.N. Differential effects of the Rac GTPase on Purkinje cell axons and dendritic trunks and spines. Nature 379 (1996) 837-840
    • (1996) Nature , vol.379 , pp. 837-840
    • Luo, L.1    Hensch, T.K.2    Ackerman, L.3    Barbel, S.4    Jan, L.Y.5    Jan, Y.N.6
  • 16
    • 0242489166 scopus 로고    scopus 로고
    • Implication of geranylgeranyltransferase I in synapse formation
    • Luo Z.G., Je H.S., Wang Q., Yang F., Dobbins G.C., Yang Z.H., et al. Implication of geranylgeranyltransferase I in synapse formation. Neuron 40 (2003) 703-717
    • (2003) Neuron , vol.40 , pp. 703-717
    • Luo, Z.G.1    Je, H.S.2    Wang, Q.3    Yang, F.4    Dobbins, G.C.5    Yang, Z.H.6
  • 17
    • 0034661746 scopus 로고    scopus 로고
    • Small GTPases Rac and Rho in the maintenance of dendritic spines and branches in hippocampal pyramidal neurons
    • Nakayama A.Y., Harms M.B., and Luo L. Small GTPases Rac and Rho in the maintenance of dendritic spines and branches in hippocampal pyramidal neurons. J Neurosci 20 (2000) 5329-5338
    • (2000) J Neurosci , vol.20 , pp. 5329-5338
    • Nakayama, A.Y.1    Harms, M.B.2    Luo, L.3
  • 18
    • 20144370412 scopus 로고    scopus 로고
    • Thrombin-induced rapid geranylgeranylation of RhoA as an essential process for RhoA activation in endothelial cells
    • Ohkawara H., Ishibashi T., Sakamoto T., Sugimoto K., Nagata K., Yokoyama K., et al. Thrombin-induced rapid geranylgeranylation of RhoA as an essential process for RhoA activation in endothelial cells. J Biol Chem 280 (2005) 10182-10188
    • (2005) J Biol Chem , vol.280 , pp. 10182-10188
    • Ohkawara, H.1    Ishibashi, T.2    Sakamoto, T.3    Sugimoto, K.4    Nagata, K.5    Yokoyama, K.6
  • 19
    • 0036842877 scopus 로고    scopus 로고
    • Modulation of nociceptive transmission by pituitary adenylate cyclase activating polypeptide in the spinal cord of the mouse
    • Ohsawa M., Brailoiu G.C., Shiraki M., Dun N.J., Paul K., and Tseng L.F. Modulation of nociceptive transmission by pituitary adenylate cyclase activating polypeptide in the spinal cord of the mouse. Pain 100 (2002) 27-34
    • (2002) Pain , vol.100 , pp. 27-34
    • Ohsawa, M.1    Brailoiu, G.C.2    Shiraki, M.3    Dun, N.J.4    Paul, K.5    Tseng, L.F.6
  • 20
    • 0034617489 scopus 로고    scopus 로고
    • Decrease of hindpaw withdrawal latency by cocaine- and amphetamine-regulated transcript peptide to the mouse spinal cord
    • Ohsawa M., Dun S.L., Tseng L.F., Chang J.K., and Dun N.J. Decrease of hindpaw withdrawal latency by cocaine- and amphetamine-regulated transcript peptide to the mouse spinal cord. Eur J Pharmacol 399 (2000) 165-169
    • (2000) Eur J Pharmacol , vol.399 , pp. 165-169
    • Ohsawa, M.1    Dun, S.L.2    Tseng, L.F.3    Chang, J.K.4    Dun, N.J.5
  • 21
    • 0032563718 scopus 로고    scopus 로고
    • Modulation of the formalin-induced nociceptive response by diabetes: possible involvement of protein kinase C
    • Ohsawa M., Kashiwazaki T., and Kamei J. Modulation of the formalin-induced nociceptive response by diabetes: possible involvement of protein kinase C. Brain Res 803 (1998) 198-203
    • (1998) Brain Res , vol.803 , pp. 198-203
    • Ohsawa, M.1    Kashiwazaki, T.2    Kamei, J.3
  • 22
    • 0036829011 scopus 로고    scopus 로고
    • Can we conquer pain?
    • Scholz J., and Woolf C.J. Can we conquer pain?. Nat Neurosci 5 (2002) 1062-1067
    • (2002) Nat Neurosci , vol.5 , pp. 1062-1067
    • Scholz, J.1    Woolf, C.J.2
  • 23
    • 0034722890 scopus 로고    scopus 로고
    • Farnesyltransferase and geranylgeranyltransferase I inhibitors and cancer therapy: Lessons from mechanism and bench-to-bedside translational studies
    • Sebti S.M., and Hamilton A.D. Farnesyltransferase and geranylgeranyltransferase I inhibitors and cancer therapy: Lessons from mechanism and bench-to-bedside translational studies. Oncogene 19 (2000) 6584-6593
    • (2000) Oncogene , vol.19 , pp. 6584-6593
    • Sebti, S.M.1    Hamilton, A.D.2
  • 24
    • 0034630098 scopus 로고    scopus 로고
    • Recent advances in the study of prenylated proteins
    • Sinensky M. Recent advances in the study of prenylated proteins. Biochem Biophys Acta 1484 (2000) 93-106
    • (2000) Biochem Biophys Acta , vol.1484 , pp. 93-106
    • Sinensky, M.1
  • 26
    • 0033807686 scopus 로고    scopus 로고
    • Regulation of dendritic spine morphology by the Rho family of small GTPases: antagonistic roles of Rac and Rho
    • Tashiro A., Minden A., and Yuste R. Regulation of dendritic spine morphology by the Rho family of small GTPases: antagonistic roles of Rac and Rho. Cereb Cortex 10 (2000) 927-938
    • (2000) Cereb Cortex , vol.10 , pp. 927-938
    • Tashiro, A.1    Minden, A.2    Yuste, R.3
  • 27
    • 13544263311 scopus 로고    scopus 로고
    • Involvement of Rho-kinase in inflammatory and neuropathic pain through phosphorylation of myristoylated alanine-rich C-kinase substrate (MARCKS)
    • Tatsumi S., Mabuchi T., Katano T., Matsumura S., Abe T., Hidaka H., et al. Involvement of Rho-kinase in inflammatory and neuropathic pain through phosphorylation of myristoylated alanine-rich C-kinase substrate (MARCKS). Neuroscience 131 (2005) 491-498
    • (2005) Neuroscience , vol.131 , pp. 491-498
    • Tatsumi, S.1    Mabuchi, T.2    Katano, T.3    Matsumura, S.4    Abe, T.5    Hidaka, H.6
  • 28
    • 0030982564 scopus 로고    scopus 로고
    • Regulation of dendritic growth and remodeling by Rho, Rac, and Cdc42
    • Threadgill R., Bobb K., and Ghosh A. Regulation of dendritic growth and remodeling by Rho, Rac, and Cdc42. Neuron 19 (1997) 625-634
    • (1997) Neuron , vol.19 , pp. 625-634
    • Threadgill, R.1    Bobb, K.2    Ghosh, A.3
  • 29
    • 0030656619 scopus 로고    scopus 로고
    • Calcium sensitization of smooth muscle mediated by a Rho-associated protein kinase in hypertension
    • Uehata M., Ishizaki T., Satoh H., Ono T., Kawahara T., Morishita T., et al. Calcium sensitization of smooth muscle mediated by a Rho-associated protein kinase in hypertension. Nature 389 (1997) 990-994
    • (1997) Nature , vol.389 , pp. 990-994
    • Uehata, M.1    Ishizaki, T.2    Satoh, H.3    Ono, T.4    Kawahara, T.5    Morishita, T.6
  • 30
    • 0030968580 scopus 로고    scopus 로고
    • Rho GTPases and signaling networks
    • Van Aelst L., and D'Souza-Schorey C. Rho GTPases and signaling networks. Genes Dev 11 (1997) 2295-2322
    • (1997) Genes Dev , vol.11 , pp. 2295-2322
    • Van Aelst, L.1    D'Souza-Schorey, C.2
  • 31
    • 0142245593 scopus 로고    scopus 로고
    • Inhibition of protein geranylgeranylation indued apoptosis in myeloma plasma cells by reducing Mcl-1 protein levels
    • Van de Donk N.W.C., Kamphuis M.M.J., van Kessel B., Lokhorst H.M., and Bloem A.C. Inhibition of protein geranylgeranylation indued apoptosis in myeloma plasma cells by reducing Mcl-1 protein levels. Blood 102 (2003) 3354-3362
    • (2003) Blood , vol.102 , pp. 3354-3362
    • Van de Donk, N.W.C.1    Kamphuis, M.M.J.2    van Kessel, B.3    Lokhorst, H.M.4    Bloem, A.C.5
  • 32
    • 0033594336 scopus 로고    scopus 로고
    • Potent, highly selective, and non-thiol inhibitors of protein geranylgeranyltransferase-I
    • Vasudevan A., Qian Y., Vogt A., Blaskovich M.A., Ohkanda J., Sebti S.M., et al. Potent, highly selective, and non-thiol inhibitors of protein geranylgeranyltransferase-I. J Med Chem 42 (1999) 1333-1340
    • (1999) J Med Chem , vol.42 , pp. 1333-1340
    • Vasudevan, A.1    Qian, Y.2    Vogt, A.3    Blaskovich, M.A.4    Ohkanda, J.5    Sebti, S.M.6
  • 33
    • 19944432457 scopus 로고    scopus 로고
    • Presynaptic and postsynaptic roles of NO, cGK, and RhoA in long-lasting potentiation and aggregation of synaptic proteins
    • Wang H.G., Lu F.M., Jin I., Udo H., Kandel E.R., De vente J., et al. Presynaptic and postsynaptic roles of NO, cGK, and RhoA in long-lasting potentiation and aggregation of synaptic proteins. Neuron 45 (2005) 389-403
    • (2005) Neuron , vol.45 , pp. 389-403
    • Wang, H.G.1    Lu, F.M.2    Jin, I.3    Udo, H.4    Kandel, E.R.5    De vente, J.6
  • 34
    • 0034235662 scopus 로고    scopus 로고
    • Rapid dendritic eremodeling in the developing retina: dependence on enurotransmission and reciprocal regulation by Rac and Rho
    • Wong W.T., Faulkner-Jones B.E., Sanes J.R., and Wong R.O. Rapid dendritic eremodeling in the developing retina: dependence on enurotransmission and reciprocal regulation by Rac and Rho. J Neurosci 20 (2000) 5024-5036
    • (2000) J Neurosci , vol.20 , pp. 5024-5036
    • Wong, W.T.1    Faulkner-Jones, B.E.2    Sanes, J.R.3    Wong, R.O.4
  • 35
    • 0034625770 scopus 로고    scopus 로고
    • Neuronal plasticity: increasing the gain in pain
    • Woolf C.J., and Salter M.W. Neuronal plasticity: increasing the gain in pain. Science 288 (2000) 1765-1769
    • (2000) Science , vol.288 , pp. 1765-1769
    • Woolf, C.J.1    Salter, M.W.2
  • 36
    • 0029898894 scopus 로고    scopus 로고
    • Protein prenylation: molecular mechanisms and functional consequences
    • Zhang F.L., and Casey P.J. Protein prenylation: molecular mechanisms and functional consequences. Annu Rev Biochem 65 (1996) 241-269
    • (1996) Annu Rev Biochem , vol.65 , pp. 241-269
    • Zhang, F.L.1    Casey, P.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.