메뉴 건너뛰기




Volumn 76, Issue 6, 2004, Pages 749-757

It's "juxta" potassium channel

Author keywords

Juxtaparanodes; Kv1 channels; Potassium channels

Indexed keywords

CASPR2 PROTEIN; CONNEXIN 29; CONTACTIN; CONTACTIN ASSOCIATED PROTEIN; GAP JUNCTION PROTEIN; ION CHANNEL; MEMBRANE PROTEIN; PARANODIN; PDZ PROTEIN; POTASSIUM CHANNEL; POTASSIUM ION; PROTEIN; PROTEIN 4.1B; PROTEIN NOGO A; SHAKER POTASSIUM CHANNEL; TAG 1 PROTEIN; UNCLASSIFIED DRUG;

EID: 2642534541     PISSN: 03604012     EISSN: None     Source Type: Journal    
DOI: 10.1002/jnr.20073     Document Type: Short Survey
Times cited : (73)

References (67)
  • 1
    • 0036703632 scopus 로고    scopus 로고
    • Connexin29 is uniquely distributed within myelinating glial cells of the central and peripheral nervous systems
    • Altevogt BM, Kleopa KA, Postma FR, Scherer SS, Paul DL. 2002. Connexin29 is uniquely distributed within myelinating glial cells of the central and peripheral nervous systems. J Neurosci 22:6458-6470.
    • (2002) J Neurosci , vol.22 , pp. 6458-6470
    • Altevogt, B.M.1    Kleopa, K.A.2    Postma, F.R.3    Scherer, S.S.4    Paul, D.L.5
  • 2
    • 0000094557 scopus 로고    scopus 로고
    • Myelinating Schwann cells determine the internodal localization of Kv1.1, Kv1.2, Kvbeta2, and Caspr
    • Arroyo EJ, Xu YT, Zhou L, Messing A, Peles E, Chiu SY, Scherer SS. 1999. Myelinating Schwann cells determine the internodal localization of Kv1.1, Kv1.2, Kvbeta2, and Caspr. J Neurocytol 28:333-347.
    • (1999) J Neurocytol , vol.28 , pp. 333-347
    • Arroyo, E.J.1    Xu, Y.T.2    Zhou, L.3    Messing, A.4    Peles, E.5    Chiu, S.Y.6    Scherer, S.S.7
  • 6
    • 0019391105 scopus 로고
    • The effects of 4-aminopyridine and tetraethylammonium ions on normal and demyelinated mammalian nerve fibres
    • Bostock H, Sears TA, Sherratt RM. 1981. The effects of 4-aminopyridine and tetraethylammonium ions on normal and demyelinated mammalian nerve fibres. J Physiol 313:301-315.
    • (1981) J Physiol , vol.313 , pp. 301-315
    • Bostock, H.1    Sears, T.A.2    Sherratt, R.M.3
  • 7
    • 0034993395 scopus 로고    scopus 로고
    • Contactin orchestrates assembly of the septate-like junctions at the paranode in myelinated peripheral nerve
    • Boyle ME, Berglund EO, Murai KK, Weber L, Peles E, Ranscht B. 2001. Contactin orchestrates assembly of the septate-like junctions at the paranode in myelinated peripheral nerve. Neuron 30:385-397.
    • (2001) Neuron , vol.30 , pp. 385-397
    • Boyle, M.E.1    Berglund, E.O.2    Murai, K.K.3    Weber, L.4    Peles, E.5    Ranscht, B.6
  • 9
    • 0018827024 scopus 로고
    • Potassium channels in nodal and internodal axonal membrane of mammalian myelinated fibres
    • Chiu SY, Ritchie JM. 1980. Potassium channels in nodal and internodal axonal membrane of mammalian myelinated fibres. Nature 284:170-171.
    • (1980) Nature , vol.284 , pp. 170-171
    • Chiu, S.Y.1    Ritchie, J.M.2
  • 10
    • 0033506758 scopus 로고    scopus 로고
    • Analysis of potassium channel functions in mammalian axons by gene knockouts
    • Chiu SY, Zhou L, Zhang CL, Messing A. 1999. Analysis of potassium channel functions in mammalian axons by gene knockouts. J Neurocytol 28:349-364.
    • (1999) J Neurocytol , vol.28 , pp. 349-364
    • Chiu, S.Y.1    Zhou, L.2    Zhang, C.L.3    Messing, A.4
  • 11
    • 0028819829 scopus 로고
    • Electrical and morphological factors influencing the depolarizing afterpotential in rat and lizard myelinated axons
    • David G, Modney B, Scappaticci KA, Barrett JN, Barrett EF. 1995. Electrical and morphological factors influencing the depolarizing afterpotential in rat and lizard myelinated axons. J Physiol 489:141-157.
    • (1995) J Physiol , vol.489 , pp. 141-157
    • David, G.1    Modney, B.2    Scappaticci, K.A.3    Barrett, J.N.4    Barrett, E.F.5
  • 15
    • 84944496608 scopus 로고
    • Membrane currents in isolated frog nerve fibre under voltage clamp conditions
    • Dodge FA, Frankenhaeuser B. 1958. Membrane currents in isolated frog nerve fibre under voltage clamp conditions. J Physiol 143:76-90.
    • (1958) J Physiol , vol.143 , pp. 76-90
    • Dodge, F.A.1    Frankenhaeuser, B.2
  • 16
    • 0032031635 scopus 로고    scopus 로고
    • Myelin galactolipids are essential for proper node of Ranvier formation in the CNS
    • Dupree JL, Coetzee T, Blight A, Suzuki K, Popko B. 1998. Myelin galactolipids are essential for proper node of Ranvier formation in the CNS. J Neurosci 18:1642-1649.
    • (1998) J Neurosci , vol.18 , pp. 1642-1649
    • Dupree, J.L.1    Coetzee, T.2    Blight, A.3    Suzuki, K.4    Popko, B.5
  • 17
    • 0033552610 scopus 로고    scopus 로고
    • Axo-glial interactions regulate the localization of axonal paranodal proteins
    • Dupree JL, Girault J-A, Popko B. 1999. Axo-glial interactions regulate the localization of axonal paranodal proteins. J Cell Biol 147:1145-1151.
    • (1999) J Cell Biol , vol.147 , pp. 1145-1151
    • Dupree, J.L.1    Girault, J.-A.2    Popko, B.3
  • 18
    • 0031453392 scopus 로고    scopus 로고
    • The axonal membrane protein Caspr, a homologue of neurexin IV, is a component of the septate-like paranodal junctions that assemble during myelination
    • Einheber S, Zanazzi G, Ching W, Scherer S, Milner TA, Peles E, Salzer JL. 1997. The axonal membrane protein Caspr, a homologue of neurexin IV, is a component of the septate-like paranodal junctions that assemble during myelination. J Cell Biol 139:1495-1506.
    • (1997) J Cell Biol , vol.139 , pp. 1495-1506
    • Einheber, S.1    Zanazzi, G.2    Ching, W.3    Scherer, S.4    Milner, T.A.5    Peles, E.6    Salzer, J.L.7
  • 19
    • 0025237057 scopus 로고
    • The axonal glycoprotein TAG-1 is an immunoglobulin superfamily member with neurite outgrowth-promoting activity
    • Furley AJ, Morton SB, Manalo D, Karagogeos D, Dodd J, Jessell TM. 1990. The axonal glycoprotein TAG-1 is an immunoglobulin superfamily member with neurite outgrowth-promoting activity. Cell 61:157-170.
    • (1990) Cell , vol.61 , pp. 157-170
    • Furley, A.J.1    Morton, S.B.2    Manalo, D.3    Karagogeos, D.4    Dodd, J.5    Jessell, T.M.6
  • 20
    • 0023921366 scopus 로고
    • Evidence for the presence of two types of potassium channels in the rat optic nerve
    • Gordon TR, Kocsis JD, Waxman SG. 1988. Evidence for the presence of two types of potassium channels in the rat optic nerve. Brain Res 447:1-9.
    • (1988) Brain Res , vol.447 , pp. 1-9
    • Gordon, T.R.1    Kocsis, J.D.2    Waxman, S.G.3
  • 21
    • 0024456844 scopus 로고
    • Pharmacological sensitivities of two afterhyperpolarizations in rat optic nerve
    • Gordon TR, Kocsis JD, Waxman SG. 1989. Pharmacological sensitivities of two afterhyperpolarizations in rat optic nerve. Brain Res 502:252-257.
    • (1989) Brain Res , vol.502 , pp. 252-257
    • Gordon, T.R.1    Kocsis, J.D.2    Waxman, S.G.3
  • 24
    • 0028000933 scopus 로고
    • + currents expressed in Xenopus oocytes by mKv1.1, mKv1.2 and their heteromultimers as revealed by mutagenesis of the dendrotoxin-binding site in mKv1.1
    • + currents expressed in Xenopus oocytes by mKv1.1, mKv1.2 and their heteromultimers as revealed by mutagenesis of the dendrotoxin-binding site in mKv1.1. Pflugers Arch Eur J Physiol 428:382-390.
    • (1994) Pflugers Arch Eur J Physiol , vol.428 , pp. 382-390
    • Hopkins, W.F.1    Allen, M.L.2    Houamed, K.M.3    Tempel, B.L.4
  • 25
    • 0025362581 scopus 로고
    • Evidence for the formation of heteromultimeric potassium channels in Xenopus oocytes
    • Isacoff EY, Jan YN, Jan LY. 1990. Evidence for the formation of heteromultimeric potassium channels in Xenopus oocytes. Nature 345:530-534.
    • (1990) Nature , vol.345 , pp. 530-534
    • Isacoff, E.Y.1    Jan, Y.N.2    Jan, L.Y.3
  • 26
    • 0036703477 scopus 로고    scopus 로고
    • A myelin galactolipid, sulfatide, is essential for maintenance of ion channels on myelinated axon but not essential for initial cluster formation
    • Ishibashi T, Dupree JL, Ikenaka K, Hirahara Y, Honke K, Peles E, Popko B, Suzuki K, Nishino H, Baba H. 2002. A myelin galactolipid, sulfatide, is essential for maintenance of ion channels on myelinated axon but not essential for initial cluster formation. J Neurosci 22:6507-6514.
    • (2002) J Neurosci , vol.22 , pp. 6507-6514
    • Ishibashi, T.1    Dupree, J.L.2    Ikenaka, K.3    Hirahara, Y.4    Honke, K.5    Peles, E.6    Popko, B.7    Suzuki, K.8    Nishino, H.9    Baba, H.10
  • 28
    • 0034703004 scopus 로고    scopus 로고
    • Subunit composition determines Kv1 potassium channel surface expression
    • Manganas LN, Trimmer JS. 2000. Subunit composition determines Kv1 potassium channel surface expression. J Biol Chem 275:29685-29693.
    • (2000) J Biol Chem , vol.275 , pp. 29685-29693
    • Manganas, L.N.1    Trimmer, J.S.2
  • 32
    • 0345255951 scopus 로고    scopus 로고
    • The myelin-axolemmal complex: Biochemical dissection and the role of galactosphingolipids
    • Menon K, Rasband MN, Taylor CM, Brophy PJ, Bansal R, Pfeiffer SE. 2003. The myelin-axolemmal complex: biochemical dissection and the role of galactosphingolipids. J Neurochem 87:995-1009.
    • (2003) J Neurochem , vol.87 , pp. 995-1009
    • Menon, K.1    Rasband, M.N.2    Taylor, C.M.3    Brophy, P.J.4    Bansal, R.5    Pfeiffer, S.E.6
  • 34
    • 0034727892 scopus 로고    scopus 로고
    • Type II brain 4.1 (4.1B/K1AA0987), a member of the protein 4.1 family, is localized to neuronal paranodes
    • Ohara R, Yamakawa H, Nakayama M, Ohara O. 2000. Type II brain 4.1 (4.1B/K1AA0987), a member of the protein 4.1 family, is localized to neuronal paranodes. Brain Res Mol Brain Res 85:41-52.
    • (2000) Brain Res Mol Brain Res , vol.85 , pp. 41-52
    • Ohara, R.1    Yamakawa, H.2    Nakayama, M.3    Ohara, O.4
  • 35
    • 0031041601 scopus 로고    scopus 로고
    • Identification of a novel contactin-associated transmembrane receptor with multiple domains implicated in protein-protein interactions
    • Peles E, Nativ M, Lustig M, Grumet M, Schilling J, Martinez R, Plowman GD, Schlessinger J. 1997. Identification of a novel contactin-associated transmembrane receptor with multiple domains implicated in protein-protein interactions. EMBO J 16:978-988.
    • (1997) EMBO J , vol.16 , pp. 978-988
    • Peles, E.1    Nativ, M.2    Lustig, M.3    Grumet, M.4    Schilling, J.5    Martinez, R.6    Plowman, G.D.7    Schlessinger, J.8
  • 38
    • 0035478027 scopus 로고    scopus 로고
    • Localization of Caspr2 in myelinated nerves depends on axonglia interactions and the generation of barriers along the axon
    • Poliak S, Gollan L, Salomon D, Berglund EO, Ohara R, Ranscht B, Peles E. 2001. Localization of Caspr2 in myelinated nerves depends on axonglia interactions and the generation of barriers along the axon. J Neurosci 21:7568-7575.
    • (2001) J Neurosci , vol.21 , pp. 7568-7575
    • Poliak, S.1    Gollan, L.2    Salomon, D.3    Berglund, E.O.4    Ohara, R.5    Ranscht, B.6    Peles, E.7
  • 48
    • 0001899956 scopus 로고
    • Physiology of axons
    • Waxman SG, Kocsis JD, Stys PK, editors. New York: Oxford University Press
    • Ritchie JM. 1995. Physiology of axons. In: Waxman SG, Kocsis JD, Stys PK, editors. The axon. New York: Oxford University Press. p 68-96.
    • (1995) The Axon , pp. 68-96
    • Ritchie, J.M.1
  • 49
    • 0023899694 scopus 로고
    • Role of glial cells in the differentiation and function of myelinated axons
    • Rosenbluth J. 1988. Role of glial cells in the differentiation and function of myelinated axons. Int J Dev Neurosci 6:3-24.
    • (1988) Int J Dev Neurosci , vol.6 , pp. 3-24
    • Rosenbluth, J.1
  • 50
    • 0001851099 scopus 로고
    • Glial membranes and axoglial junctions
    • New York: Oxford University Press
    • Rosenbluth J. 1995. Glial membranes and axoglial junctions. In: Neuroglia. New York: Oxford University Press.
    • (1995) Neuroglia
    • Rosenbluth, J.1
  • 54
    • 0018840887 scopus 로고
    • Effects of 4-aminopyridine on normal and demyelinated mammalian nerve fibres
    • Sherratt RM, Bostock H, Sears TA. 1980. Effects of 4-aminopyridine on normal and demyelinated mammalian nerve fibres. Nature 283:570-572.
    • (1980) Nature , vol.283 , pp. 570-572
    • Sherratt, R.M.1    Bostock, H.2    Sears, T.A.3
  • 56
    • 0021922832 scopus 로고
    • 4-Aminopyridine leads to restoration of conduction in demyelinated rat sciatic nerve
    • Targ EF, Kocsis JD. 1985. 4-Aminopyridine leads to restoration of conduction in demyelinated rat sciatic nerve. Brain Res 328:358-361.
    • (1985) Brain Res , vol.328 , pp. 358-361
    • Targ, E.F.1    Kocsis, J.D.2
  • 57
    • 0022652854 scopus 로고
    • Action potential characteristics of demyelinated rat sciatic nerve following application of 4-aminopyridine
    • Targ EF, Kocsis JD. 1986. Action potential characteristics of demyelinated rat sciatic nerve following application of 4-aminopyridine. Brain Res 363:1-9.
    • (1986) Brain Res , vol.363 , pp. 1-9
    • Targ, E.F.1    Kocsis, J.D.2
  • 58
    • 0037092443 scopus 로고    scopus 로고
    • The neuronal adhesion protein TAG-1 is expressed by Schwann cells and oligodendrocytes and is localized to the juxtaparanodal region of myelinated fibers
    • Traka M, Dupree JL, Popko B, Karagogeos D. 2002. The neuronal adhesion protein TAG-1 is expressed by Schwann cells and oligodendrocytes and is localized to the juxtaparanodal region of myelinated fibers. J Neurosci 22:3016-3024.
    • (2002) J Neurosci , vol.22 , pp. 3016-3024
    • Traka, M.1    Dupree, J.L.2    Popko, B.3    Karagogeos, D.4
  • 60
    • 0002718674 scopus 로고    scopus 로고
    • Heteromultimer formation in native K+ channels
    • New York: Kluwer Academic/Plenum Publishers
    • Trimmer JS, Rhodes KJ. 2001. Heteromultimer formation in native K+ channels. In: Potassium channels in cardiovascular biology. New York: Kluwer Academic/Plenum Publishers.
    • (2001) Potassium Channels in Cardiovascular Biology
    • Trimmer, J.S.1    Rhodes, K.J.2
  • 61
    • 0033555445 scopus 로고    scopus 로고
    • Dynamic potassium channel distributions during axonal development prevent aberrant firing patterns
    • Vabnick I, Trimmer JS, Schwarz TL, Levinson SR, Risal D, Shrager P. 1999. Dynamic potassium channel distributions during axonal development prevent aberrant firing patterns. J Neurosci 19:747-758.
    • (1999) J Neurosci , vol.19 , pp. 747-758
    • Vabnick, I.1    Trimmer, J.S.2    Schwarz, T.L.3    Levinson, S.R.4    Risal, D.5    Shrager, P.6
  • 64
    • 0032530718 scopus 로고    scopus 로고
    • Temperature-sensitive neuromuscular transmission in Kv1.1 null mice: Role of potassium channels under the myelin sheath in young nerves
    • Zhou L, Zhang CL, Messing A, Chiu SY. 1998. Temperature-sensitive neuromuscular transmission in Kv1.1 null mice: role of potassium channels under the myelin sheath in young nerves. J Neurosci 18:7200-7215.
    • (1998) J Neurosci , vol.18 , pp. 7200-7215
    • Zhou, L.1    Zhang, C.L.2    Messing, A.3    Chiu, S.Y.4
  • 65
    • 0033565421 scopus 로고    scopus 로고
    • Determinants of excitability at transition zones in Kv1.1-deficient myelinated nerves
    • Zhou L, Messing A, Chiu SY. 1999. Determinants of excitability at transition zones in Kv1.1-deficient myelinated nerves. J Neurosci 19:5768-5781.
    • (1999) J Neurosci , vol.19 , pp. 5768-5781
    • Zhou, L.1    Messing, A.2    Chiu, S.Y.3
  • 66
    • 0035914395 scopus 로고    scopus 로고
    • Determinants involved in Kv1 potassium channel folding in the endoplasmic reticulum, glycosylation in the Golgi, and cell surface expression
    • Zhu J, Watanabe I, Gomez B, Thornhill WB. 2001. Determinants involved in Kv1 potassium channel folding in the endoplasmic reticulum, glycosylation in the Golgi, and cell surface expression. J Biol Chem 276:39419-39427.
    • (2001) J Biol Chem , vol.276 , pp. 39419-39427
    • Zhu, J.1    Watanabe, I.2    Gomez, B.3    Thornhill, W.B.4
  • 67
    • 0037815216 scopus 로고    scopus 로고
    • Heteromeric Kv1 potassium channel expression: Amino acid determinants involved in processing and trafficking to the cell surface
    • Zhu J, Watanabe I, Gomez B, Thornhill WB. 2003. Heteromeric Kv1 potassium channel expression: amino acid determinants involved in processing and trafficking to the cell surface. J Biol Chem 278:25558-25567.
    • (2003) J Biol Chem , vol.278 , pp. 25558-25567
    • Zhu, J.1    Watanabe, I.2    Gomez, B.3    Thornhill, W.B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.