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Volumn 49, Issue 3, 2011, Pages 174-183

Early disruption of the actin cytoskeleton in cultured cerebellar granule neurons exposed to 3-morpholinosydnonimine-oxidative stress is linked to alterations of the cytosolic calcium concentration

Author keywords

Actin cytoskeleton; Cerebellar granule neurons; Cytosolic calcium; Fluorescence microscopy; L type voltage operated calcium channels; Peroxynitrite

Indexed keywords

4 (2 BENZYLBENZOYL) 2,5 DIMETHYL 1H PYRROLE 3 CARBOXYLIC ACID METHYL ESTER; ACTIN; CALCIUM CHANNEL L TYPE; CALCIUM ION; CYTOCHALASIN D; F ACTIN; G ACTIN; JASPAMIDE; LATRUNCULIN B; LINSIDOMINE; NIFEDIPINE; PEROXYNITRITE;

EID: 79952454326     PISSN: 01434160     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ceca.2011.01.009     Document Type: Article
Times cited : (16)

References (65)
  • 1
    • 0029805172 scopus 로고    scopus 로고
    • Nitric oxide, superoxide, and peroxynitrite: the good, the bad, and ugly
    • Beckman J.S., Koppenol W.H. Nitric oxide, superoxide, and peroxynitrite: the good, the bad, and ugly. Am. J. Physiol. 1996, 271:C1424-C1437.
    • (1996) Am. J. Physiol. , vol.271
    • Beckman, J.S.1    Koppenol, W.H.2
  • 3
    • 0031020172 scopus 로고    scopus 로고
    • Bright and dark sides of nitric oxide in ischemic brain injury
    • Iadecola C. Bright and dark sides of nitric oxide in ischemic brain injury. Trends Neurosci. 1997, 20:132-139.
    • (1997) Trends Neurosci. , vol.20 , pp. 132-139
    • Iadecola, C.1
  • 4
    • 0030787471 scopus 로고    scopus 로고
    • Extensive peroxynitrite activity during progressive stages of central nervous system inflammation
    • van der Veen R.C., Hinton D.R., Incardonna F., Hofman F.M. Extensive peroxynitrite activity during progressive stages of central nervous system inflammation. J. Neuroimmunol. 1997, 77:1-7.
    • (1997) J. Neuroimmunol. , vol.77 , pp. 1-7
    • van der Veen, R.C.1    Hinton, D.R.2    Incardonna, F.3    Hofman, F.M.4
  • 5
    • 0038233014 scopus 로고    scopus 로고
    • Nitric oxide-mediated mitochondrial damage in the brain: mechanisms and implications for neurodegenerative diseases
    • Bolanos J.P., Almeida A., Stewart V., Peuchen S., Land J.M., Clark J.B., Heales S.J. Nitric oxide-mediated mitochondrial damage in the brain: mechanisms and implications for neurodegenerative diseases. J. Neurochem. 1997, 68:2227-2240.
    • (1997) J. Neurochem. , vol.68 , pp. 2227-2240
    • Bolanos, J.P.1    Almeida, A.2    Stewart, V.3    Peuchen, S.4    Land, J.M.5    Clark, J.B.6    Heales, S.J.7
  • 8
    • 0029153913 scopus 로고
    • Apoptosis and necrosis: two distinct events induced, respectively, by mild and intense insults with N-methyl-D-aspartate or nitric oxide/superoxide in cortical cell cultures
    • Bonfoco E., Krainc D., Ankarcrona M., Nicotera P., Lipton S.A. Apoptosis and necrosis: two distinct events induced, respectively, by mild and intense insults with N-methyl-D-aspartate or nitric oxide/superoxide in cortical cell cultures. Proc. Natl. Acad. Sci. U.S.A. 1995, 92:7162-7166.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 7162-7166
    • Bonfoco, E.1    Krainc, D.2    Ankarcrona, M.3    Nicotera, P.4    Lipton, S.A.5
  • 10
    • 0029072217 scopus 로고
    • Colchicine induces apoptosis in cerebellar granule cells
    • Bonfoco E., Ceccatelli S., Manzo L., Nicotera P. Colchicine induces apoptosis in cerebellar granule cells. Exp. Cell Res. 1995, 218:189-200.
    • (1995) Exp. Cell Res. , vol.218 , pp. 189-200
    • Bonfoco, E.1    Ceccatelli, S.2    Manzo, L.3    Nicotera, P.4
  • 11
    • 0029848750 scopus 로고    scopus 로고
    • Cytoskeletal breakdown and apoptosis elicited by NO donors in cerebellar granule cells require NMDA receptor activation
    • Bonfoco E., Leist M., Zhivotovsky B., Orrenius S., Lipton S.A., Nicotera P. Cytoskeletal breakdown and apoptosis elicited by NO donors in cerebellar granule cells require NMDA receptor activation. J. Neurochem. 1996, 67:2484-2493.
    • (1996) J. Neurochem. , vol.67 , pp. 2484-2493
    • Bonfoco, E.1    Leist, M.2    Zhivotovsky, B.3    Orrenius, S.4    Lipton, S.A.5    Nicotera, P.6
  • 12
    • 0035893961 scopus 로고    scopus 로고
    • The actin cytoskeleton response to oxidants: from small heat shock protein phosphorylation to changes in the redox state of actin itself
    • Dalle-Donne I., Rossi R., Milzani A., Di Simplicio P., Colombo R. The actin cytoskeleton response to oxidants: from small heat shock protein phosphorylation to changes in the redox state of actin itself. Free Radic. Biol. Med. 2001, 31:1624-1632.
    • (2001) Free Radic. Biol. Med. , vol.31 , pp. 1624-1632
    • Dalle-Donne, I.1    Rossi, R.2    Milzani, A.3    Di Simplicio, P.4    Colombo, R.5
  • 13
    • 1642307513 scopus 로고    scopus 로고
    • A comparative study of the effect of oxidative stress on the cytoskeleton in human cortical neurons
    • Allani P.K., Sum T., Bhansali S.G., Mukherjee S.K., Sonee M. A comparative study of the effect of oxidative stress on the cytoskeleton in human cortical neurons. Toxicol. Appl. Pharmacol. 2004, 196:29-36.
    • (2004) Toxicol. Appl. Pharmacol. , vol.196 , pp. 29-36
    • Allani, P.K.1    Sum, T.2    Bhansali, S.G.3    Mukherjee, S.K.4    Sonee, M.5
  • 18
    • 0032583203 scopus 로고    scopus 로고
    • SAPK2/p38-dependent F-actin reorganization regulates early membrane blebbing during stress-induced apoptosis
    • Huot J., Houle F., Rousseau S., Deschesnes R.G., Shah G.M., Landry J. SAPK2/p38-dependent F-actin reorganization regulates early membrane blebbing during stress-induced apoptosis. J. Cell Biol. 1998, 143:1361-1373.
    • (1998) J. Cell Biol. , vol.143 , pp. 1361-1373
    • Huot, J.1    Houle, F.2    Rousseau, S.3    Deschesnes, R.G.4    Shah, G.M.5    Landry, J.6
  • 19
    • 2442502511 scopus 로고    scopus 로고
    • Phosphorylation of p38 MAPK induced by oxidative stress is linked to activation of both caspase-8- and -9-mediated apoptotic pathways in dopaminergic neurons
    • Choi W.S., Eom D.S., Han B.S., Kim W.K., Han B.H., Choi E.J., Oh T.H., Markelonis G.J., Cho J.W., Oh Y.J. Phosphorylation of p38 MAPK induced by oxidative stress is linked to activation of both caspase-8- and -9-mediated apoptotic pathways in dopaminergic neurons. J. Biol. Chem. 2004, 279:20451-20460.
    • (2004) J. Biol. Chem. , vol.279 , pp. 20451-20460
    • Choi, W.S.1    Eom, D.S.2    Han, B.S.3    Kim, W.K.4    Han, B.H.5    Choi, E.J.6    Oh, T.H.7    Markelonis, G.J.8    Cho, J.W.9    Oh, Y.J.10
  • 20
    • 24944546733 scopus 로고    scopus 로고
    • Hydrogen peroxide alters membrane and cytoskeleton properties and increases intercellular connections in astrocytes
    • Zhu D., Tan K.S., Zhang X., Sun A.Y., Sun G.Y., Lee J.C. Hydrogen peroxide alters membrane and cytoskeleton properties and increases intercellular connections in astrocytes. J. Cell Sci. 2005, 118:3695-3703.
    • (2005) J. Cell Sci. , vol.118 , pp. 3695-3703
    • Zhu, D.1    Tan, K.S.2    Zhang, X.3    Sun, A.Y.4    Sun, G.Y.5    Lee, J.C.6
  • 22
    • 0036320954 scopus 로고    scopus 로고
    • Inhibition of oxidative stress produced by plasma membrane NADH oxidase delays low-potassium-induced apoptosis of cerebellar granule cells
    • Martin-Romero F.J., Garcia-Martin E., Gutierrez-Merino C. Inhibition of oxidative stress produced by plasma membrane NADH oxidase delays low-potassium-induced apoptosis of cerebellar granule cells. J. Neurochem. 2002, 82:705-715.
    • (2002) J. Neurochem. , vol.82 , pp. 705-715
    • Martin-Romero, F.J.1    Garcia-Martin, E.2    Gutierrez-Merino, C.3
  • 23
    • 2942596005 scopus 로고    scopus 로고
    • Kaempferol blocks oxidative stress in cerebellar granule cells and reveals a key role for reactive oxygen species production at the plasma membrane in the commitment to apoptosis
    • Samhan-Arias A.K., Martin-Romero F.J., Gutierrez-Merino C. Kaempferol blocks oxidative stress in cerebellar granule cells and reveals a key role for reactive oxygen species production at the plasma membrane in the commitment to apoptosis. Free Radic. Biol. Med. 2004, 37:48-61.
    • (2004) Free Radic. Biol. Med. , vol.37 , pp. 48-61
    • Samhan-Arias, A.K.1    Martin-Romero, F.J.2    Gutierrez-Merino, C.3
  • 24
    • 57149125691 scopus 로고    scopus 로고
    • Clustering of plasma membrane-bound cytochrome b5 reductase within 'lipid raft' microdomains of the neuronal plasma membrane
    • Samhan-Arias A.K., Garcia-Bereguiain M.A., Martin-Romero F.J., Gutierrez-Merino C. Clustering of plasma membrane-bound cytochrome b5 reductase within 'lipid raft' microdomains of the neuronal plasma membrane. Mol. Cell Neurosci. 2009, 40:14-26.
    • (2009) Mol. Cell Neurosci. , vol.40 , pp. 14-26
    • Samhan-Arias, A.K.1    Garcia-Bereguiain, M.A.2    Martin-Romero, F.J.3    Gutierrez-Merino, C.4
  • 25
    • 0030857117 scopus 로고    scopus 로고
    • N-methyl-D-aspartate evokes rapid net depolymerization of filamentous actin in cultured rat cerebellar granule cells
    • Shorte S.L. N-methyl-D-aspartate evokes rapid net depolymerization of filamentous actin in cultured rat cerebellar granule cells. J. Neurophysiol. 1997, 78:1135-1143.
    • (1997) J. Neurophysiol. , vol.78 , pp. 1135-1143
    • Shorte, S.L.1
  • 27
    • 0026774583 scopus 로고
    • Simultaneous localization and quantification of relative G and F actin content: optimization of fluorescence labeling methods
    • Knowles G.C., McCulloch C.A. Simultaneous localization and quantification of relative G and F actin content: optimization of fluorescence labeling methods. J. Histochem. Cytochem. 1992, 40:1605-1612.
    • (1992) J. Histochem. Cytochem. , vol.40 , pp. 1605-1612
    • Knowles, G.C.1    McCulloch, C.A.2
  • 29
    • 0036152486 scopus 로고    scopus 로고
    • Use of fluorescently labelled deoxyribonuclease I to spatially measure G-actin levels in migrating and non-migrating cells
    • Cramer L.P., Briggs L.J., Dawe H.R. Use of fluorescently labelled deoxyribonuclease I to spatially measure G-actin levels in migrating and non-migrating cells. Cell Motil. Cytoskeleton 2002, 51:27-38.
    • (2002) Cell Motil. Cytoskeleton , vol.51 , pp. 27-38
    • Cramer, L.P.1    Briggs, L.J.2    Dawe, H.R.3
  • 30
    • 0026482631 scopus 로고
    • Suppression of programmed neuronal death by sustained elevation of cytoplasmic calcium
    • Franklin J.L., Johnson E.M. Suppression of programmed neuronal death by sustained elevation of cytoplasmic calcium. Trends Neurosci. 1992, 15:501-508.
    • (1992) Trends Neurosci. , vol.15 , pp. 501-508
    • Franklin, J.L.1    Johnson, E.M.2
  • 31
    • 0029887755 scopus 로고    scopus 로고
    • High affinity block by nimodipine of the internal calcium elevation in chronically depolarized rat cerebellar granule neurons
    • Marchetti C., Usai C. High affinity block by nimodipine of the internal calcium elevation in chronically depolarized rat cerebellar granule neurons. Neurosci. Lett. 1996, 207:77-80.
    • (1996) Neurosci. Lett. , vol.207 , pp. 77-80
    • Marchetti, C.1    Usai, C.2
  • 32
    • 0032885168 scopus 로고    scopus 로고
    • Activity of voltage-operated calcium channels in rat cerebellar granule neurons and neuronal survival
    • Toescu E.C. Activity of voltage-operated calcium channels in rat cerebellar granule neurons and neuronal survival. Neuroscience 1999, 94:561-570.
    • (1999) Neuroscience , vol.94 , pp. 561-570
    • Toescu, E.C.1
  • 34
    • 0027258451 scopus 로고
    • Calcium-induced actin depolymerization reduces NMDA channel activity
    • Rosenmund C., Westbrook G.L. Calcium-induced actin depolymerization reduces NMDA channel activity. Neuron 1993, 10:805-814.
    • (1993) Neuron , vol.10 , pp. 805-814
    • Rosenmund, C.1    Westbrook, G.L.2
  • 35
    • 0030807917 scopus 로고    scopus 로고
    • The actin-severing protein gelsolin modulates calcium channel and NMDA receptor activities and vulnerability to excitotoxicity in hippocampal neurons
    • Furukawa K., Fu W., Li Y., Witke W., Kwiatkowski D.J., Mattson M.P. The actin-severing protein gelsolin modulates calcium channel and NMDA receptor activities and vulnerability to excitotoxicity in hippocampal neurons. J. Neurosci. 1997, 17:8178-8186.
    • (1997) J. Neurosci. , vol.17 , pp. 8178-8186
    • Furukawa, K.1    Fu, W.2    Li, Y.3    Witke, W.4    Kwiatkowski, D.J.5    Mattson, M.P.6
  • 36
    • 0036678723 scopus 로고    scopus 로고
    • Endoplasmic reticulum calcium release is modulated by actin polymerization
    • Wang Y., Mattson M.P., Furukawa K. Endoplasmic reticulum calcium release is modulated by actin polymerization. J. Neurochem. 2002, 82:945-952.
    • (2002) J. Neurochem. , vol.82 , pp. 945-952
    • Wang, Y.1    Mattson, M.P.2    Furukawa, K.3
  • 38
    • 1942424905 scopus 로고    scopus 로고
    • Actin filaments regulate voltage-gated ion channels in salamander retinal ganglion cells
    • Schubert T., Akopian A. Actin filaments regulate voltage-gated ion channels in salamander retinal ganglion cells. Neuroscience 2004, 125:583-590.
    • (2004) Neuroscience , vol.125 , pp. 583-590
    • Schubert, T.1    Akopian, A.2
  • 39
    • 32344451568 scopus 로고    scopus 로고
    • 2+ influx in third-order neurons of salamander retina is regulated by the actin cytoskeleton
    • 2+ influx in third-order neurons of salamander retina is regulated by the actin cytoskeleton. Neuroscience 2006, 138:17-24.
    • (2006) Neuroscience , vol.138 , pp. 17-24
    • Akopian, A.1    Szikra, T.2    Cristofanilli, M.3    Krizaj, D.4
  • 40
    • 0028929186 scopus 로고
    • Induction, effects, and quantification of sublethal oxidative stress by hydrogen peroxide on cultured human fibroblasts
    • Mocali A., Caldini R., Chevanne M., Paoletti F. Induction, effects, and quantification of sublethal oxidative stress by hydrogen peroxide on cultured human fibroblasts. Exp. Cell Res. 1995, 216:388-395.
    • (1995) Exp. Cell Res. , vol.216 , pp. 388-395
    • Mocali, A.1    Caldini, R.2    Chevanne, M.3    Paoletti, F.4
  • 41
    • 0031890098 scopus 로고    scopus 로고
    • Hydrogen peroxide-induced cytoskeletal rearrangement in cultured pulmonary endothelial cells
    • Zhao Y., Davis H.W. Hydrogen peroxide-induced cytoskeletal rearrangement in cultured pulmonary endothelial cells. J. Cell Physiol. 1998, 174:370-379.
    • (1998) J. Cell Physiol. , vol.174 , pp. 370-379
    • Zhao, Y.1    Davis, H.W.2
  • 42
    • 0032990887 scopus 로고    scopus 로고
    • Oxidative stress affects cytoskeletal structure and cell-matrix interactions in cells from an ocular tissue: the trabecular meshwork
    • Zhou L., Li Y., Yue B.Y. Oxidative stress affects cytoskeletal structure and cell-matrix interactions in cells from an ocular tissue: the trabecular meshwork. J. Cell Physiol. 1999, 180:182-189.
    • (1999) J. Cell Physiol. , vol.180 , pp. 182-189
    • Zhou, L.1    Li, Y.2    Yue, B.Y.3
  • 43
    • 0034069867 scopus 로고    scopus 로고
    • Carbonylation and disassembly of the F-actin cytoskeleton in oxidant induced barrier dysfunction and its prevention by epidermal growth factor and transforming growth factor alpha in a human colonic cell line
    • Banan A., Zhang Y., Losurdo J., Keshavarzian A. Carbonylation and disassembly of the F-actin cytoskeleton in oxidant induced barrier dysfunction and its prevention by epidermal growth factor and transforming growth factor alpha in a human colonic cell line. Gut 2000, 46:830-837.
    • (2000) Gut , vol.46 , pp. 830-837
    • Banan, A.1    Zhang, Y.2    Losurdo, J.3    Keshavarzian, A.4
  • 44
    • 0027245908 scopus 로고
    • Nitric oxide measured by a porphyrinic microsensor in rat brain after transient middle cerebral artery occlusion
    • Malinski T., Bailey F., Zhang Z.G., Chopp M. Nitric oxide measured by a porphyrinic microsensor in rat brain after transient middle cerebral artery occlusion. J. Cereb. Blood Flow Metab. 1993, 13:355-358.
    • (1993) J. Cereb. Blood Flow Metab. , vol.13 , pp. 355-358
    • Malinski, T.1    Bailey, F.2    Zhang, Z.G.3    Chopp, M.4
  • 46
    • 0036273352 scopus 로고    scopus 로고
    • Stimulation of the NADPH oxidase in activated rat microglia removes nitric oxide but induces peroxynitrite production
    • Bal-Price A., Matthias A., Brown G.C. Stimulation of the NADPH oxidase in activated rat microglia removes nitric oxide but induces peroxynitrite production. J. Neurochem. 2002, 80:73-80.
    • (2002) J. Neurochem. , vol.80 , pp. 73-80
    • Bal-Price, A.1    Matthias, A.2    Brown, G.C.3
  • 47
    • 0037049252 scopus 로고    scopus 로고
    • Peroxynitrite generated in the rat spinal cord induces neuron death and neurological deficits
    • Bao F., Liu D. Peroxynitrite generated in the rat spinal cord induces neuron death and neurological deficits. Neuroscience 2002, 115:839-849.
    • (2002) Neuroscience , vol.115 , pp. 839-849
    • Bao, F.1    Liu, D.2
  • 48
    • 0023427610 scopus 로고
    • Effects of cytochalasin and phalloidin on actin
    • Cooper J.A. Effects of cytochalasin and phalloidin on actin. J. Cell Biol. 1987, 105:1473-1478.
    • (1987) J. Cell Biol. , vol.105 , pp. 1473-1478
    • Cooper, J.A.1
  • 49
    • 0023142377 scopus 로고
    • Inhibition of actin polymerization by latrunculin A
    • Coue M., Brenner S.L., Spector I., Korn E.D. Inhibition of actin polymerization by latrunculin A. FEBS Lett. 1987, 213:316-318.
    • (1987) FEBS Lett. , vol.213 , pp. 316-318
    • Coue, M.1    Brenner, S.L.2    Spector, I.3    Korn, E.D.4
  • 50
    • 0024360298 scopus 로고
    • Latrunculins-novel marine macrolides that disrupt microfilament organization and affect cell growth. I. Comparison with cytochalasin D
    • Spector I., Shochet N.R., Blasberger D., Kashman Y. Latrunculins-novel marine macrolides that disrupt microfilament organization and affect cell growth. I. Comparison with cytochalasin D. Cell Motil. Cytoskeleton 1989, 13:127-144.
    • (1989) Cell Motil. Cytoskeleton , vol.13 , pp. 127-144
    • Spector, I.1    Shochet, N.R.2    Blasberger, D.3    Kashman, Y.4
  • 51
    • 0035065418 scopus 로고    scopus 로고
    • Effects of cytochalasin D and latrunculin B on mechanical properties of cells
    • Wakatsuki T., Schwab B., Thompson N.C., Elson E.L. Effects of cytochalasin D and latrunculin B on mechanical properties of cells. J. Cell Sci. 2001, 114:1025-1036.
    • (2001) J. Cell Sci. , vol.114 , pp. 1025-1036
    • Wakatsuki, T.1    Schwab, B.2    Thompson, N.C.3    Elson, E.L.4
  • 52
    • 2942576910 scopus 로고    scopus 로고
    • Fluorescence measurements of steady state peroxynitrite production upon SIN-1 decomposition: NADH versus dihydrodichlorofluorescein and dihydrorhodamine 123
    • Martin-Romero F.J., Gutierrez-Martin Y., Henao F., Gutierrez-Merino C. Fluorescence measurements of steady state peroxynitrite production upon SIN-1 decomposition: NADH versus dihydrodichlorofluorescein and dihydrorhodamine 123. J. Fluoresc. 2004, 14:17-23.
    • (2004) J. Fluoresc. , vol.14 , pp. 17-23
    • Martin-Romero, F.J.1    Gutierrez-Martin, Y.2    Henao, F.3    Gutierrez-Merino, C.4
  • 54
    • 16244372090 scopus 로고    scopus 로고
    • Calcium regulation of actin dynamics in dendritic spines
    • Oertner T.G., Matus A. Calcium regulation of actin dynamics in dendritic spines. Cell Calcium 2005, 37:477-482.
    • (2005) Cell Calcium , vol.37 , pp. 477-482
    • Oertner, T.G.1    Matus, A.2
  • 55
    • 0032517822 scopus 로고    scopus 로고
    • Calcium and protein kinase c regulate the actin cytoskeleton in the synaptic terminal of retinal bipolar cells
    • Job C., Lagnado L. Calcium and protein kinase c regulate the actin cytoskeleton in the synaptic terminal of retinal bipolar cells. J. Cell Biol. 1998, 143:1661-1672.
    • (1998) J. Cell Biol. , vol.143 , pp. 1661-1672
    • Job, C.1    Lagnado, L.2
  • 56
    • 0023778390 scopus 로고
    • Multiple types of neuronal calcium channels and their selective modulation
    • Tsien R.W., Lipscombe D., Madison D.V., Bley K.R., Fox A.P. Multiple types of neuronal calcium channels and their selective modulation. Trends Neurosci. 1988, 11:431-438.
    • (1988) Trends Neurosci. , vol.11 , pp. 431-438
    • Tsien, R.W.1    Lipscombe, D.2    Madison, D.V.3    Bley, K.R.4    Fox, A.P.5
  • 57
    • 77953124127 scopus 로고    scopus 로고
    • L-type calcium channels and cytochrome b5 reductase are components of protein complexes tightly associated with lipid rafts microdomains of the neuronal plasma membrane
    • Marques-da-Silva D., Samhan-Arias A.K., Tiago T., Gutierrez-Merino C. L-type calcium channels and cytochrome b5 reductase are components of protein complexes tightly associated with lipid rafts microdomains of the neuronal plasma membrane. J. Proteomics 2010, 73:1502-1510.
    • (2010) J. Proteomics , vol.73 , pp. 1502-1510
    • Marques-da-Silva, D.1    Samhan-Arias, A.K.2    Tiago, T.3    Gutierrez-Merino, C.4
  • 58
    • 1542508954 scopus 로고    scopus 로고
    • Localization of ion channels to lipid Raft domains within the cardiovascular system
    • O'Connell K.M., Martens J.R., Tamkun M.M. Localization of ion channels to lipid Raft domains within the cardiovascular system. Trends Cardiovasc. Med. 2004, 14:37-42.
    • (2004) Trends Cardiovasc. Med. , vol.14 , pp. 37-42
    • O'Connell, K.M.1    Martens, J.R.2    Tamkun, M.M.3
  • 60
    • 33747667539 scopus 로고    scopus 로고
    • Calcium channel and glutamate receptor activities regulate actin organization in salamander retinal neurons
    • Cristofanilli M., Akopian A. Calcium channel and glutamate receptor activities regulate actin organization in salamander retinal neurons. J. Physiol. 2006, 575:543-554.
    • (2006) J. Physiol. , vol.575 , pp. 543-554
    • Cristofanilli, M.1    Akopian, A.2
  • 61
    • 0032403433 scopus 로고    scopus 로고
    • Regulation of F-actin stability in dendritic spines by glutamate receptors and calcineurin
    • Halpain S., Hipolito A., Saffer L. Regulation of F-actin stability in dendritic spines by glutamate receptors and calcineurin. J. Neurosci. 1998, 18:9835-9844.
    • (1998) J. Neurosci. , vol.18 , pp. 9835-9844
    • Halpain, S.1    Hipolito, A.2    Saffer, L.3
  • 62
    • 34548394571 scopus 로고    scopus 로고
    • Disruption of actin cytoskeleton causes internalization of Ca(v)1.3 (alpha 1D) L-type calcium channels in salamander retinal neurons
    • Cristofanilli M., Mizuno F., Akopian A. Disruption of actin cytoskeleton causes internalization of Ca(v)1.3 (alpha 1D) L-type calcium channels in salamander retinal neurons. Mol. Vis. 2007, 13:1496-1507.
    • (2007) Mol. Vis. , vol.13 , pp. 1496-1507
    • Cristofanilli, M.1    Mizuno, F.2    Akopian, A.3
  • 63
    • 77951706007 scopus 로고    scopus 로고
    • Glutamate-induced internalization of Ca(v)1.3 L-type Ca(2+) channels protects retinal neurons against excitotoxicity
    • Mizuno F., Barabas P., Krizaj D., Akopian A. Glutamate-induced internalization of Ca(v)1.3 L-type Ca(2+) channels protects retinal neurons against excitotoxicity. J. Physiol. 2010, 588:953-966.
    • (2010) J. Physiol. , vol.588 , pp. 953-966
    • Mizuno, F.1    Barabas, P.2    Krizaj, D.3    Akopian, A.4
  • 64
    • 0037423394 scopus 로고    scopus 로고
    • Nitric oxide-dependent generation of reactive species in sickle cell disease. Actin tyrosine induces defective cytoskeletal polymerization
    • Aslan M., Ryan T.M., Townes T.M., Coward L., Kirk M.C., Barnes S., Alexander C.B., Rosenfeld S.S., Freeman B.A. Nitric oxide-dependent generation of reactive species in sickle cell disease. Actin tyrosine induces defective cytoskeletal polymerization. J. Biol. Chem. 2003, 278:4194-4204.
    • (2003) J. Biol. Chem. , vol.278 , pp. 4194-4204
    • Aslan, M.1    Ryan, T.M.2    Townes, T.M.3    Coward, L.4    Kirk, M.C.5    Barnes, S.6    Alexander, C.B.7    Rosenfeld, S.S.8    Freeman, B.A.9
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.