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Volumn 102, Issue 5, 2007, Pages 1548-1560

Role of matrix metalloproteinase and tissue inhibitor of MMP in methamphetamine-induced behavioral sensitization and reward: Implications for dopamine receptor down-regulation and dopamine release

Author keywords

Dopamine; Dopamine receptor; Matrix metalloproteinase; Methamphetamine; Tissue inhibitor of matrix metalloproteinase

Indexed keywords

DOPAMINE; DOPAMINE 2 RECEPTOR STIMULATING AGENT; DOPAMINE RECEPTOR; DOPAMINE RECEPTOR STIMULATING AGENT; GELATINASE A; GELATINASE B; GELATINASE INHIBITOR; GUANOSINE 5' O (3 THIOTRIPHOSPHATE); MATRIX METALLOPROTEINASE; METHAMPHETAMINE; OLIGONUCLEOTIDE; SULFUR 35; TISSUE INHIBITOR OF METALLOPROTEINASE; TISSUE INHIBITOR OF METALLOPROTEINASE 2;

EID: 34547909242     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2007.04623.x     Document Type: Article
Times cited : (66)

References (46)
  • 1
    • 0035478029 scopus 로고    scopus 로고
    • Effects of matrix metalloproteinases-9 gene knock-out on the proteolysis of blood-brain barrier and white matter components after cerebral ischemia
    • Asahi M., Wang X., Mori T., Sumii T., Jung J. C., Moskowitz M. A., Fini M. E. Lo E. H. (2001) Effects of matrix metalloproteinases-9 gene knock-out on the proteolysis of blood-brain barrier and white matter components after cerebral ischemia. J. Neurosci. 21, 7724 7732.
    • (2001) J. Neurosci. , vol.21 , pp. 7724-7732
    • Asahi, M.1    Wang, X.2    Mori, T.3    Sumii, T.4    Jung, J.C.5    Moskowitz, M.A.6    Fini, M.E.7    Lo, E.H.8
  • 2
    • 0033695676 scopus 로고    scopus 로고
    • Addiction, dopamine, and the molecular mechanisms of memory
    • Berke J. Hyman S. T. (2000) Addiction, dopamine, and the molecular mechanisms of memory. Neuron 25, 515 532.
    • (2000) Neuron , vol.25 , pp. 515-532
    • Berke, J.1    Hyman, S.T.2
  • 3
    • 0036262316 scopus 로고    scopus 로고
    • Cocaine sensitization: Modulation by dopamine D2 receptors
    • Beyer C. E. Steketee J. (2002) Cocaine sensitization: modulation by dopamine D2 receptors. Cereb. Cortex 12, 526 535.
    • (2002) Cereb. Cortex , vol.12 , pp. 526-535
    • Beyer, C.E.1    Steketee, J.2
  • 4
    • 33644937491 scopus 로고    scopus 로고
    • Matrix metalloproteinase-7 disrupts dendritic spines in hippocampal neurons through NMDA receptor activation
    • Bilousova T. V., Rusakov D. A., Ethell D. W. Ethell I. M. (2006) Matrix metalloproteinase-7 disrupts dendritic spines in hippocampal neurons through NMDA receptor activation. J. Neurochem. 97, 44 56.
    • (2006) J. Neurochem. , vol.97 , pp. 44-56
    • Bilousova, T.V.1    Rusakov, D.A.2    Ethell, D.W.3    Ethell, I.M.4
  • 5
    • 0028170989 scopus 로고
    • 2+ influx and neurite growth in response to purified N-cadherin and laminin
    • 2+ influx and neurite growth in response to purified N-cadherin and laminin. J. Cell Biol. 127, 1461 1475.
    • (1994) J. Cell Biol. , vol.127 , pp. 1461-1475
    • Bixby, J.L.1    Grunwald, G.B.2    Bookman, R.J.3
  • 7
    • 0023240780 scopus 로고
    • 2+-evoked release of [3H]-dopamine from striatal synaptosomes by dopamine (D2) agonists and antagonists
    • 2+-evoked release of [3H]-dopamine from striatal synaptosomes by dopamine (D2) agonists and antagonists. J. Pharmacol. Exp. Ther. 241, 27 33.
    • (1987) J. Pharmacol. Exp. Ther. , vol.241 , pp. 27-33
    • Bowyer, J.F.1    Weiner, N.2
  • 9
    • 4944230997 scopus 로고    scopus 로고
    • Extracellular matrix modulates β2-adrenergic receptor signaling in human airway smooth muscle cells
    • Freyer A. M., Bilington C. K., Penn R. B. Hall I. P. (2004) Extracellular matrix modulates β2-adrenergic receptor signaling in human airway smooth muscle cells. Am. J. Respir. Cell Mol. Biol. 31, 440 445.
    • (2004) Am. J. Respir. Cell Mol. Biol. , vol.31 , pp. 440-445
    • Freyer, A.M.1    Bilington, C.K.2    Penn, R.B.3    Hall, I.P.4
  • 10
    • 0036787356 scopus 로고    scopus 로고
    • Drug addiction and its underlying neurobiological basis: Neuroimaging evidence for the involvement of the frontal cortex
    • Goldstein R. Z. Volkow N. D. (2002) Drug addiction and its underlying neurobiological basis: neuroimaging evidence for the involvement of the frontal cortex. Am. J. Psychiatry 159, 1642 1652.
    • (2002) Am. J. Psychiatry , vol.159 , pp. 1642-1652
    • Goldstein, R.Z.1    Volkow, N.D.2
  • 12
    • 0030884231 scopus 로고    scopus 로고
    • Unaltered secretion of β-amyloid precursor protein in gelatinase a (matrix metalloproteinases 2)-deficient mice
    • Itoh T., Ikeda T., Gomi H., Nakao S., Suzuki T. Itohara S. (1997) Unaltered secretion of β-amyloid precursor protein in gelatinase A (matrix metalloproteinases 2)-deficient mice. J. Biol Chem. 272, 22389 22392.
    • (1997) J. Biol Chem. , vol.272 , pp. 22389-22392
    • Itoh, T.1    Ikeda, T.2    Gomi, H.3    Nakao, S.4    Suzuki, T.5    Itohara, S.6
  • 13
    • 0037121996 scopus 로고    scopus 로고
    • Matrix metalloproteinases in the adult brain physiology: A link between c-Fos, AP-1 and remodeling of neuronal connections?
    • Kaczmarek L., Lapinska-Dzwonek J. Szymczak S. (2002) Matrix metalloproteinases in the adult brain physiology: a link between c-Fos, AP-1 and remodeling of neuronal connections? EMBO J. 21, 6643 6648.
    • (2002) EMBO J. , vol.21 , pp. 6643-6648
    • Kaczmarek, L.1    Lapinska-Dzwonek, J.2    Szymczak, S.3
  • 15
    • 0024593647 scopus 로고
    • Antisense RNA-induced reduction in murine TIMP levels confers oncogenicity on Swiss 3T3 cells
    • Khokha R., Waterhouse P., Yagel S., Lala P. K., Overall C. M., Norton G. Denhardt D. T. (1989) Antisense RNA-induced reduction in murine TIMP levels confers oncogenicity on Swiss 3T3 cells. Science 243, 947 950.
    • (1989) Science , vol.243 , pp. 947-950
    • Khokha, R.1    Waterhouse, P.2    Yagel, S.3    Lala, P.K.4    Overall, C.M.5    Norton, G.6    Denhardt, D.T.7
  • 16
    • 0032842567 scopus 로고    scopus 로고
    • Tumor targeting with a selective gelatinase inhibitor
    • Koivunen E., Arap W., Valtanen H. et al. (1999) Tumor targeting with a selective gelatinase inhibitor. Nat. Biotechnol. 17, 768 774.
    • (1999) Nat. Biotechnol. , vol.17 , pp. 768-774
    • Koivunen, E.1    Arap, W.2    Valtanen, H.3
  • 17
    • 0842327251 scopus 로고    scopus 로고
    • Role of matrix metalloproteinases in delayed neuronal damage after transient global cerebral ischemia
    • Lee S. R., Tsuji K., Lee S. R. Lo E. H. (2004) Role of matrix metalloproteinases in delayed neuronal damage after transient global cerebral ischemia. J. Neurosci. 24, 671 678.
    • (2004) J. Neurosci. , vol.24 , pp. 671-678
    • Lee, S.R.1    Tsuji, K.2    Lee, S.R.3    Lo, E.H.4
  • 18
    • 0035117366 scopus 로고    scopus 로고
    • Dopamine D2 receptors regulate tyrosine hydroxylase activity and phosphorylation at Ser40 in rat striatum
    • Lindgren N., Xu Z-Q., Herrera-M M., Haycock J., Hokfelt T. Fisone G. (2001) Dopamine D2 receptors regulate tyrosine hydroxylase activity and phosphorylation at Ser40 in rat striatum. Eur. J. Neurosci. 13, 773 780.
    • (2001) Eur. J. Neurosci. , vol.13 , pp. 773-780
    • Lindgren, N.1    Xu, Z.-Q.2    Herrera-M, M.3    Haycock, J.4    Hokfelt, T.5    Fisone, G.6
  • 19
    • 0035175984 scopus 로고    scopus 로고
    • Tissue inhibitors of metalloproteinases and programmed cell death: Conundrums, controversies and potential implications
    • Mannello F. Gazzanelli G. (2001) Tissue inhibitors of metalloproteinases and programmed cell death: conundrums, controversies and potential implications. Apoptosis 6, 479 482.
    • (2001) Apoptosis , vol.6 , pp. 479-482
    • Mannello, F.1    Gazzanelli, G.2
  • 20
    • 2142655891 scopus 로고    scopus 로고
    • Regulations of methamphetamine reward by extracellular signal-regulated kinase 1/2/ets-like gene-1 signaling pathway via the activation of dopamine receptors
    • Mizoguchi H., Yamada K., Mizuno M., Mizuno T., Nitta A., Noda Y. Nabeshima T. (2004) Regulations of methamphetamine reward by extracellular signal-regulated kinase 1/2/ets-like gene-1 signaling pathway via the activation of dopamine receptors. Mol. Pharmacol. 65, 1293 1301.
    • (2004) Mol. Pharmacol. , vol.65 , pp. 1293-1301
    • Mizoguchi, H.1    Yamada, K.2    Mizuno, M.3    Mizuno, T.4    Nitta, A.5    Noda, Y.6    Nabeshima, T.7
  • 25
    • 0028282875 scopus 로고
    • Production of matrix metalloproteinases and tissue inhibitor of metalloproteinases-1 by human brain tumors
    • Nakagawa T., Kubota T., Kabut M., Sato K., Kawano H., Hayakawa T. Okada Y. (1994) Production of matrix metalloproteinases and tissue inhibitor of metalloproteinases-1 by human brain tumors. J. Neurosurg. 81, 69 77.
    • (1994) J. Neurosurg. , vol.81 , pp. 69-77
    • Nakagawa, T.1    Kubota, T.2    Kabut, M.3    Sato, K.4    Kawano, H.5    Hayakawa, T.6    Okada, Y.7
  • 26
    • 12144290272 scopus 로고    scopus 로고
    • Role of tumor necrosis factor-alpha in methamphetamine-induced drug dependence and neurotoxicity
    • Nakajima A., Yamada K., Nagai T. et al. (2004) Role of tumor necrosis factor-alpha in methamphetamine-induced drug dependence and neurotoxicity. J. Neurosci. 24, 2212 2225.
    • (2004) J. Neurosci. , vol.24 , pp. 2212-2225
    • Nakajima, A.1    Yamada, K.2    Nagai, T.3
  • 27
    • 0035260641 scopus 로고    scopus 로고
    • Molecular basis of long-term plasticity underlying addiction
    • Nestler E. J. (2001) Molecular basis of long-term plasticity underlying addiction. Nat. Rev. Neurosci. 2, 119 128.
    • (2001) Nat. Rev. Neurosci. , vol.2 , pp. 119-128
    • Nestler, E.J.1
  • 29
    • 0344824684 scopus 로고    scopus 로고
    • Matrix metalloproteinases inhibition alters functional and structural correlates of deafferentation-induced sprouting in the dentate gyrus
    • Reeves T., Prins M. L., Zhu J. P., Povlishock J. T. Phillips L. L. (2003) Matrix metalloproteinases inhibition alters functional and structural correlates of deafferentation-induced sprouting in the dentate gyrus. J. Neurosci. 12, 10182 10189.
    • (2003) J. Neurosci. , vol.12 , pp. 10182-10189
    • Reeves, T.1    Prins, M.L.2    Zhu, J.P.3    Povlishock, J.T.4    Phillips, L.L.5
  • 30
    • 0030916121 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinases-1 (TIMP-1) is differentially induced in neurons and astrocytes after seizures: Evidence for developmental, immediate early gene, and lesion response
    • Rivera S., Tremblay E., Timsit S., Canals O., Ben-Ari Y. Khrestchatisky M. (1997) Tissue inhibitor of metalloproteinases-1 (TIMP-1) is differentially induced in neurons and astrocytes after seizures: evidence for developmental, immediate early gene, and lesion response. J. Neurosci. 17, 4223 4235.
    • (1997) J. Neurosci. , vol.17 , pp. 4223-4235
    • Rivera, S.1    Tremblay, E.2    Timsit, S.3    Canals, O.4    Ben-Ari, Y.5    Khrestchatisky, M.6
  • 31
    • 0030732153 scopus 로고    scopus 로고
    • Persistent structural modifications in nucleus accumbens and prefrontal cortex neurons produced by previous experience with amphetamine
    • Robinson T. E. Kolb B. (1997) Persistent structural modifications in nucleus accumbens and prefrontal cortex neurons produced by previous experience with amphetamine. J. Neurosci. 17, 8491 8497.
    • (1997) J. Neurosci. , vol.17 , pp. 8491-8497
    • Robinson, T.E.1    Kolb, B.2
  • 33
    • 0029075885 scopus 로고
    • Sensitization to the conditioned rewarding effects of cocaine: Pharmacological and temporal characteristics
    • Shippenberg T. S. Heidbreder C. h. (1995) Sensitization to the conditioned rewarding effects of cocaine: pharmacological and temporal characteristics. J. Pharmacol. Exp. Ther. 273, 808 815.
    • (1995) J. Pharmacol. Exp. Ther. , vol.273 , pp. 808-815
    • Shippenberg, T.S.1    Heidbreder, C.H.2
  • 34
    • 0030022245 scopus 로고    scopus 로고
    • Activation of recombinant human neutrophil procollagenase in the presence of doxycycline results in fragmentation of the enzyme and loss of enzyme activity
    • Smith G. N. J., Brandt K. D. Hasty K. A. (1996) Activation of recombinant human neutrophil procollagenase in the presence of doxycycline results in fragmentation of the enzyme and loss of enzyme activity. Arthritis Rheum. 39, 235 244.
    • (1996) Arthritis Rheum. , vol.39 , pp. 235-244
    • Smith, G.N.J.1    Brandt, K.D.2    Hasty, K.A.3
  • 35
    • 0035188727 scopus 로고    scopus 로고
    • How matrix metalloproteinases regulate cell behavior
    • Sternlicht M. D. Werb Z. (2001) How matrix metalloproteinases regulate cell behavior. Annu. Rev. Cell Dev. Biol. 17, 463 516.
    • (2001) Annu. Rev. Cell Dev. Biol. , vol.17 , pp. 463-516
    • Sternlicht, M.D.1    Werb, Z.2
  • 36
    • 0028907318 scopus 로고
    • Mechanism of cell surgace activation of 72-kDa type IV collagenase Isolation of the activated form of the membrane metalloproteinases
    • Strongin A. Y., Collier I., Bannikov G., Marmer B. L., Grant G. A. Goldberg G. I. (1995) Mechanism of cell surgace activation of 72-kDa type IV collagenase Isolation of the activated form of the membrane metalloproteinases. J. Biol. Chem. 270, 5331 5338.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5331-5338
    • Strongin, A.Y.1    Collier, I.2    Bannikov, G.3    Marmer, B.L.4    Grant, G.A.5    Goldberg, G.I.6
  • 37
    • 0029032794 scopus 로고
    • Amphetamine redistributes dopamine from synaptic vesicles to the cytosol and promotes reverse transport
    • Sulzer D., Chen T. K., Lau Y. Y., Kristensen H., Rayport S. Ewing A. (1995) Amphetamine redistributes dopamine from synaptic vesicles to the cytosol and promotes reverse transport. J. Neurosci. 15, 4102 4108.
    • (1995) J. Neurosci. , vol.15 , pp. 4102-4108
    • Sulzer, D.1    Chen, T.K.2    Lau, Y.Y.3    Kristensen, H.4    Rayport, S.5    Ewing, A.6
  • 38
    • 0034143263 scopus 로고    scopus 로고
    • The presynaptic calcium channel is part of a transmembrane complex linking a synaptic laminin (α4β2γ1) with non-erythroid spectrin
    • Sunderland W. J., Son Y. J., Miner J. H., Sanes J. R. Carlson S. S. (2000) The presynaptic calcium channel is part of a transmembrane complex linking a synaptic laminin (α4β2γ1) with non-erythroid spectrin. J. Neurosci. 20, 1009 1019.
    • (2000) J. Neurosci. , vol.20 , pp. 1009-1019
    • Sunderland, W.J.1    Son, Y.J.2    Miner, J.H.3    Sanes, J.R.4    Carlson, S.S.5
  • 39
    • 0036470147 scopus 로고    scopus 로고
    • Matrixmetalloproteinase-9 undergoes expression and activation during dendritic remodeling in adult hippocampus
    • Szklarczyk A., Lapinska J., Rylski M., Mckay R. D. Kaczmarek L. (2002) Matrixmetalloproteinase-9 undergoes expression and activation during dendritic remodeling in adult hippocampus. J. Neurosci. 22, 920 930.
    • (2002) J. Neurosci. , vol.22 , pp. 920-930
    • Szklarczyk, A.1    Lapinska, J.2    Rylski, M.3    McKay, R.D.4    Kaczmarek, L.5
  • 40
    • 0028659774 scopus 로고
    • Doxycycline and chemically modified tetracyclines inhibit gelatinase a (MMP-2) gene expression in human skin keratinocytes
    • Uitto V. J., Firth J., Nip L. Golub L. (1994) Doxycycline and chemically modified tetracyclines inhibit gelatinase A (MMP-2) gene expression in human skin keratinocytes. Ann. NY Acad. Sci. 732, 140 151.
    • (1994) Ann. NY Acad. Sci. , vol.732 , pp. 140-151
    • Uitto, V.J.1    Firth, J.2    Nip, L.3    Golub, L.4
  • 41
    • 0026769035 scopus 로고    scopus 로고
    • Neurexins: Synaptic cell surface proteins related to the alpha-latrotoxin receptor and laminin
    • Ushkaryov Y. A., Petrenko A. G., Geppert M. Sudhof T. C. (2002) Neurexins: synaptic cell surface proteins related to the alpha-latrotoxin receptor and laminin. Science 257, 50 56.
    • (2002) Science , vol.257 , pp. 50-56
    • Ushkaryov, Y.A.1    Petrenko, A.G.2    Geppert, M.3    Sudhof, T.C.4
  • 42
    • 0033564779 scopus 로고    scopus 로고
    • Spatiotemporal expression patterns of metalloproteinases and their inhibitors in the postnatal developing rat cerebellum
    • Vaillant C., Didier-Bazes M., Hurter A., Bein M. F. Thomasset N. (1999) Spatiotemporal expression patterns of metalloproteinases and their inhibitors in the postnatal developing rat cerebellum. J. Neurosci. 19, 4994 5004.
    • (1999) J. Neurosci. , vol.19 , pp. 4994-5004
    • Vaillant, C.1    Didier-Bazes, M.2    Hurter, A.3    Bein, M.F.4    Thomasset, N.5
  • 44
    • 15744398881 scopus 로고    scopus 로고
    • Drug dependence, synaptic plasticity, and tissue plasminogen activator
    • Yamada K., Nagai T. Nabeshima T. (2005) Drug dependence, synaptic plasticity, and tissue plasminogen activator. J. Pharmacol. Sci. 97, 157 161.
    • (2005) J. Pharmacol. Sci. , vol.97 , pp. 157-161
    • Yamada, K.1    Nagai, T.2    Nabeshima, T.3
  • 45
    • 0035405886 scopus 로고    scopus 로고
    • Metalloproteinases in biology and pathology of the nervous system
    • Yong V. W., Power C., Forsyth P. Edwards D. R. (2001) Metalloproteinases in biology and pathology of the nervous system. Nat. Rev. Neurosci. 2, 502 511.
    • (2001) Nat. Rev. Neurosci. , vol.2 , pp. 502-511
    • Yong, V.W.1    Power, C.2    Forsyth, P.3    Edwards, D.R.4
  • 46
    • 0030824185 scopus 로고    scopus 로고
    • Zymographic measurement of gelatinase activiy in brain tissue after detergent extrqaction and affinity-support purification
    • Zhang J. W. Gottschall P. E. (1997) Zymographic measurement of gelatinase activiy in brain tissue after detergent extrqaction and affinity-support purification. J. Neurosci. Methods 76, 15 20.
    • (1997) J. Neurosci. Methods , vol.76 , pp. 15-20
    • Zhang, J.W.1    Gottschall, P.E.2


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