메뉴 건너뛰기




Volumn 401, Issue 1-2, 2006, Pages 159-164

Protein tyrosine nitration is associated with cold- and drug-resistant microtubules in neuronal-like PC12 cells

Author keywords

Cytoskeleton; Microtubules; Nitration; Nitric oxide; PC12 cells

Indexed keywords

CYTOSKELETON PROTEIN; NOCODAZOLE; TYROSINE;

EID: 33646434559     PISSN: 03043940     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.neulet.2006.03.009     Document Type: Article
Times cited : (19)

References (34)
  • 4
    • 18744399023 scopus 로고    scopus 로고
    • STOP and GO with NO: nitric oxide as a regulator of cell motility in simple brains
    • Bicker G. STOP and GO with NO: nitric oxide as a regulator of cell motility in simple brains. BioEssays 27 (2005) 495-505
    • (2005) BioEssays , vol.27 , pp. 495-505
    • Bicker, G.1
  • 5
    • 0033118430 scopus 로고    scopus 로고
    • + on the state of tubulin polymerisation in NGF-differentiated PC12 cells
    • + on the state of tubulin polymerisation in NGF-differentiated PC12 cells. J. Neurosci. Res. 56 (1999) 28-35
    • (1999) J. Neurosci. Res. , vol.56 , pp. 28-35
    • Cappelletti, G.1    Maggioni, M.G.2    Maci, R.3
  • 6
    • 0037811301 scopus 로고    scopus 로고
    • Protein tyrosine nitration is triggered by nerve growth factor during neuronal differentiation of PC12 cells
    • Cappelletti G., Maggioni M.G., Tedeschi G., and Maci R. Protein tyrosine nitration is triggered by nerve growth factor during neuronal differentiation of PC12 cells. Exp. Cell Res. 288 (2003) 9-20
    • (2003) Exp. Cell Res. , vol.288 , pp. 9-20
    • Cappelletti, G.1    Maggioni, M.G.2    Tedeschi, G.3    Maci, R.4
  • 8
    • 20144365869 scopus 로고    scopus 로고
    • Protein tyrosine nitration in rat brain is associated with raft proteins, flotillin-1 and alpha-tubulin: effect of biological aging
    • Dremina E.S., Sharov V.S., and Schoneich C. Protein tyrosine nitration in rat brain is associated with raft proteins, flotillin-1 and alpha-tubulin: effect of biological aging. J. Neurochem. 93 (2005) 1262-1271
    • (2005) J. Neurochem. , vol.93 , pp. 1262-1271
    • Dremina, E.S.1    Sharov, V.S.2    Schoneich, C.3
  • 9
    • 0033984598 scopus 로고    scopus 로고
    • Tubulin-tyrosine ligase, a long-lasting enigma
    • Erck C., Frank R., and Wehland J. Tubulin-tyrosine ligase, a long-lasting enigma. Neurochem. Res. 25 (2000) 5-10
    • (2000) Neurochem. Res. , vol.25 , pp. 5-10
    • Erck, C.1    Frank, R.2    Wehland, J.3
  • 11
    • 0032748099 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3β phosphorylation of microtubule-associated protein 1B regulates the stability of microtubules in growth cones
    • Goold R.G., Owen R., and Gordon-Weeks P.R. Glycogen synthase kinase 3β phosphorylation of microtubule-associated protein 1B regulates the stability of microtubules in growth cones. J. Cell Sci. 112 (1999) 3373-3384
    • (1999) J. Cell Sci. , vol.112 , pp. 3373-3384
    • Goold, R.G.1    Owen, R.2    Gordon-Weeks, P.R.3
  • 15
    • 0038731081 scopus 로고    scopus 로고
    • Biological selectivity and functional aspects of protein tyrosine nitration
    • Ischiropoulos H. Biological selectivity and functional aspects of protein tyrosine nitration. Biochem. Biophys. Res. Commun. 305 (2003) 776-783
    • (2003) Biochem. Biophys. Res. Commun. , vol.305 , pp. 776-783
    • Ischiropoulos, H.1
  • 16
    • 13244284790 scopus 로고    scopus 로고
    • Pathophysiological functions of nitric-oxide-mediated protein modifications
    • Ischiropoulos H., and Gow A. Pathophysiological functions of nitric-oxide-mediated protein modifications. Toxicology 208 (2005) 299-303
    • (2005) Toxicology , vol.208 , pp. 299-303
    • Ischiropoulos, H.1    Gow, A.2
  • 18
    • 0035371473 scopus 로고    scopus 로고
    • Disruption of retinogeniculate pattern formation by inhibition of soluble guanylyl cyclase
    • Leamy C.A., Ho-Pao C.L., and Sur M. Disruption of retinogeniculate pattern formation by inhibition of soluble guanylyl cyclase. J. Neurosci. 21 (2001) 3871-3880
    • (2001) J. Neurosci. , vol.21 , pp. 3871-3880
    • Leamy, C.A.1    Ho-Pao, C.L.2    Sur, M.3
  • 19
    • 0030049998 scopus 로고    scopus 로고
    • Microtubule assembly and turnover in growing axons
    • Li Y., and Black M.M. Microtubule assembly and turnover in growing axons. J. Neurosci. 16 (1996) 531-534
    • (1996) J. Neurosci. , vol.16 , pp. 531-534
    • Li, Y.1    Black, M.M.2
  • 20
    • 0028945057 scopus 로고
    • Microtubules and microtubule-associated proteins
    • Mandelkow E., and Mandelkow E.M. Microtubules and microtubule-associated proteins. Curr. Opin. Cell Biol. 7 (1995) 72-81
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 72-81
    • Mandelkow, E.1    Mandelkow, E.M.2
  • 22
    • 0024109183 scopus 로고
    • Cytoskeleton dynamics and nerve growth
    • Mitchison T., and Kirschner M. Cytoskeleton dynamics and nerve growth. Neuron 1 (1988) 761-772
    • (1988) Neuron , vol.1 , pp. 761-772
    • Mitchison, T.1    Kirschner, M.2
  • 23
    • 0036073066 scopus 로고    scopus 로고
    • NMDA receptor stimulation induces temporary alpha-tubulin degradation signaled by nitric oxide-mediated tyrosine nitration in the nervous system of Sepia officinalis
    • Palumbo A., Fiore G., Di Cristo C., Di Cosmo A., and d'Ischia M. NMDA receptor stimulation induces temporary alpha-tubulin degradation signaled by nitric oxide-mediated tyrosine nitration in the nervous system of Sepia officinalis. Biochem. Biophys. Res. Commun. 293 (2002) 1536-1543
    • (2002) Biochem. Biophys. Res. Commun. , vol.293 , pp. 1536-1543
    • Palumbo, A.1    Fiore, G.2    Di Cristo, C.3    Di Cosmo, A.4    d'Ischia, M.5
  • 24
    • 0028283568 scopus 로고
    • Accumulation of delta-2-tubulin, a major tubulin variant that cannot be tyrosinated in neuronal tissues and in stable microtubule assemblies
    • Paturle-Lafanechère L., Manier M., Trigault N., Pirollet F., Mazarguil H., and Job D. Accumulation of delta-2-tubulin, a major tubulin variant that cannot be tyrosinated in neuronal tissues and in stable microtubule assemblies. J. Cell Sci. 107 (1994) 1529-1543
    • (1994) J. Cell Sci. , vol.107 , pp. 1529-1543
    • Paturle-Lafanechère, L.1    Manier, M.2    Trigault, N.3    Pirollet, F.4    Mazarguil, H.5    Job, D.6
  • 25
    • 0029057332 scopus 로고
    • Nitric oxide triggers a switch to growth arrest during differentiation of neuronal cells
    • Peunova N., and Enikolopov G. Nitric oxide triggers a switch to growth arrest during differentiation of neuronal cells. Nature 375 (1995) 68-73
    • (1995) Nature , vol.375 , pp. 68-73
    • Peunova, N.1    Enikolopov, G.2
  • 26
    • 0035890074 scopus 로고    scopus 로고
    • Nitric oxide is an essential negative regulator of cell proliferation in Xenopus brain
    • Peunova N., Scheinker V., Cline H., and Enikolopov G. Nitric oxide is an essential negative regulator of cell proliferation in Xenopus brain. J. Neurosci. 21 (2001) 8809-8818
    • (2001) J. Neurosci. , vol.21 , pp. 8809-8818
    • Peunova, N.1    Scheinker, V.2    Cline, H.3    Enikolopov, G.4
  • 27
    • 0030861630 scopus 로고    scopus 로고
    • A novel, nerve growth factor-activated pathway involving nitric oxide, p53, and p21AWF1 regulates neuronal differentiation of PC12 cells
    • Poluha W., Schonhoff C., Harrington K., Lachyankar M., Crosbie N., Bulseco D., and Ross A. A novel, nerve growth factor-activated pathway involving nitric oxide, p53, and p21AWF1 regulates neuronal differentiation of PC12 cells. J. Biol. Chem. 272 (1997) 24002-24007
    • (1997) J. Biol. Chem. , vol.272 , pp. 24002-24007
    • Poluha, W.1    Schonhoff, C.2    Harrington, K.3    Lachyankar, M.4    Crosbie, N.5    Bulseco, D.6    Ross, A.7
  • 29
    • 0036324619 scopus 로고    scopus 로고
    • Nitric oxide affects the phosphorylation state of microtubule-associated protein 2 (MAP-2) and neurofilament: an immunocytochemical study in the brain of rats and neuronal nitric oxide synthase (nNOS)-knockouts
    • Rothe F., Possel H., and Wolf G. Nitric oxide affects the phosphorylation state of microtubule-associated protein 2 (MAP-2) and neurofilament: an immunocytochemical study in the brain of rats and neuronal nitric oxide synthase (nNOS)-knockouts. Nitric Oxide 6 (2002) 9-17
    • (2002) Nitric Oxide , vol.6 , pp. 9-17
    • Rothe, F.1    Possel, H.2    Wolf, G.3
  • 30
    • 0027284439 scopus 로고
    • The nitric oxide and cGMP signal transduction system: regulation and mechanism of action
    • Schmidt H.H., Lohmann S.M., and Walter U. The nitric oxide and cGMP signal transduction system: regulation and mechanism of action. Biochim. Biophys. Acta 1178 (1993) 153-175
    • (1993) Biochim. Biophys. Acta , vol.1178 , pp. 153-175
    • Schmidt, H.H.1    Lohmann, S.M.2    Walter, U.3
  • 31
    • 0033709834 scopus 로고    scopus 로고
    • Nitric oxide and cGMP influence axonogenesis of antennal pioneer neurons
    • Seidel C., and Bicker G. Nitric oxide and cGMP influence axonogenesis of antennal pioneer neurons. Development 127 (2000) 4541-4549
    • (2000) Development , vol.127 , pp. 4541-4549
    • Seidel, C.1    Bicker, G.2
  • 32
    • 0035929149 scopus 로고    scopus 로고
    • Nitrosylation: the prototypic redox-based signaling mechanism
    • Stamler J.S., Lamas S., and Fang F.C. Nitrosylation: the prototypic redox-based signaling mechanism. Cell 106 (2001) 675-683
    • (2001) Cell , vol.106 , pp. 675-683
    • Stamler, J.S.1    Lamas, S.2    Fang, F.C.3
  • 33
    • 20644445194 scopus 로고    scopus 로고
    • Characterization of nitroproteome in neuron-like PC12 cells differentiated with nerve growth factor: identification of two nitration sites in alpha-tubulin
    • Tedeschi G., Cappelletti G., Negri A., Pagliato L., Maggioni M.G., Maci R., and Ronchi S. Characterization of nitroproteome in neuron-like PC12 cells differentiated with nerve growth factor: identification of two nitration sites in alpha-tubulin. Proteomics 5 (2005) 2422-2432
    • (2005) Proteomics , vol.5 , pp. 2422-2432
    • Tedeschi, G.1    Cappelletti, G.2    Negri, A.3    Pagliato, L.4    Maggioni, M.G.5    Maci, R.6    Ronchi, S.7
  • 34
    • 0345169048 scopus 로고    scopus 로고
    • Post-translational modifications regulate microtubule function
    • Westermann S., and Weber K. Post-translational modifications regulate microtubule function. Nat. Rev. Mol. Cell Biol. 4 (2003) 938-948
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 938-948
    • Westermann, S.1    Weber, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.