메뉴 건너뛰기




Volumn 75, Issue 2, 2014, Pages 255-265

Abnormal junctions and permeability of myelin in PMP22-deficient nerves

Author keywords

[No Author keywords available]

Indexed keywords

IMMUNOGLOBULIN; JUNCTIONAL ADHESION MOLECULE C; MYELIN ASSOCIATED GLYCOPROTEIN; PERIPHERAL MYELIN PROTEIN 22; TIGHT JUNCTION PROTEIN;

EID: 84896547826     PISSN: 03645134     EISSN: 15318249     Source Type: Journal    
DOI: 10.1002/ana.24086     Document Type: Article
Times cited : (53)

References (32)
  • 1
    • 0033940488 scopus 로고    scopus 로고
    • Activity-dependent conduction block in multifocal motor neuropathy
    • Kaji, R, Bostock, H, Kohara, N, et al. Activity-dependent conduction block in multifocal motor neuropathy. Brain 2000; 123 (pt 8): 1602-1611.
    • (2000) Brain , vol.123 , Issue.PART 8 , pp. 1602-1611
    • Kaji, R.1    Bostock, H.2    Kohara, N.3
  • 2
    • 33845907921 scopus 로고    scopus 로고
    • Rapid conduction and the evolution of giant axons and myelinated fibers
    • Hartline DK, Colman DR,. Rapid conduction and the evolution of giant axons and myelinated fibers. Curr Biol 2007; 17: R29-R35.
    • (2007) Curr Biol , vol.17
    • Hartline, D.K.1    Colman, D.R.2
  • 3
    • 84883137706 scopus 로고    scopus 로고
    • The PMP22 gene and its related diseases
    • Li J, Parker B, Martyn C, et al. The PMP22 gene and its related diseases. Mol Neurobiol 2013; 47: 673-698.
    • (2013) Mol Neurobiol , vol.47 , pp. 673-698
    • Li, J.1    Parker, B.2    Martyn, C.3
  • 4
    • 0842304504 scopus 로고    scopus 로고
    • Loss-of-function phenotype of hereditary neuropathy with liability to pressure palsies
    • Li J, Krajewski K, Lewis RA, et al. Loss-of-function phenotype of hereditary neuropathy with liability to pressure palsies. Muscle Nerve 2004; 29: 205-210.
    • (2004) Muscle Nerve , vol.29 , pp. 205-210
    • Li, J.1    Krajewski, K.2    Lewis, R.A.3
  • 5
    • 0030048699 scopus 로고    scopus 로고
    • Deletions of chromosome 17p11.2 in multifocal neuropathies
    • Tyson J, Malcolm S, Thomas PK, et al. Deletions of chromosome 17p11.2 in multifocal neuropathies. Ann Neurol 1996; 39: 180-186.
    • (1996) Ann Neurol , vol.39 , pp. 180-186
    • Tyson, J.1    Malcolm, S.2    Thomas, P.K.3
  • 6
    • 0028784820 scopus 로고
    • Hypermyelination and demyelinating peripheral neuropathy in Pmp22-deficient mice
    • Adlkofer K, Martini R, Aguzzi A, et al. Hypermyelination and demyelinating peripheral neuropathy in Pmp22-deficient mice. Nat Genet 1995; 11: 274-280.
    • (1995) Nat Genet , vol.11 , pp. 274-280
    • Adlkofer, K.1    Martini, R.2    Aguzzi, A.3
  • 7
    • 0030994297 scopus 로고    scopus 로고
    • Heterozygous peripheral myelin protein 22-deficient mice are affected by a progressive demyelinating tomaculous neuropathy
    • Adlkofer K, Frei R, Neuberg DH, et al. Heterozygous peripheral myelin protein 22-deficient mice are affected by a progressive demyelinating tomaculous neuropathy. J Neurosci 1997; 17: 4662-4671.
    • (1997) J Neurosci , vol.17 , pp. 4662-4671
    • Adlkofer, K.1    Frei, R.2    Neuberg, D.H.3
  • 8
    • 74949099450 scopus 로고    scopus 로고
    • Conduction block in PMP22 deficiency
    • Bai Y, Zhang X, Katona I, et al. Conduction block in PMP22 deficiency. J Neurosci 2010; 30: 600-608.
    • (2010) J Neurosci , vol.30 , pp. 600-608
    • Bai, Y.1    Zhang, X.2    Katona, I.3
  • 9
    • 49449098975 scopus 로고    scopus 로고
    • Mutation of FIG4 causes a rapidly progressive, asymmetric neuronal degeneration
    • Zhang X, Chow CY, Sahenk Z, et al. Mutation of FIG4 causes a rapidly progressive, asymmetric neuronal degeneration. Brain 2008; 131: 1990-2001.
    • (2008) Brain , vol.131 , pp. 1990-2001
    • Zhang, X.1    Chow, C.Y.2    Sahenk, Z.3
  • 10
    • 84655163880 scopus 로고    scopus 로고
    • Fig4 expression in the rodent nervous system and its potential role in preventing abnormal lysosomal accumulation
    • Guo J, Ma YH, Yan Q, et al. Fig4 expression in the rodent nervous system and its potential role in preventing abnormal lysosomal accumulation. J Neuropathol Exp Neurol 2012; 71: 28-39.
    • (2012) J Neuropathol Exp Neurol , vol.71 , pp. 28-39
    • Guo, J.1    Ma, Y.H.2    Yan, Q.3
  • 11
    • 78649407784 scopus 로고    scopus 로고
    • Permeability of the paranodal junction of myelinated nerve fibers
    • Mierzwa A, Shroff S, Rosenbluth J,. Permeability of the paranodal junction of myelinated nerve fibers. J Neurosci 2010; 30: 15962-15968.
    • (2010) J Neurosci , vol.30 , pp. 15962-15968
    • Mierzwa, A.1    Shroff, S.2    Rosenbluth, J.3
  • 12
    • 0034448329 scopus 로고    scopus 로고
    • Ionic permeability of the frog sciatic nerve perineurium: Parallel studies of potassium and lanthanum penetration using electrophysiological and electron microscopic techniques
    • Todd BA, Inman C, Sedgwick EM, et al. Ionic permeability of the frog sciatic nerve perineurium: parallel studies of potassium and lanthanum penetration using electrophysiological and electron microscopic techniques. J Neurocytol 2000; 29: 551-567.
    • (2000) J Neurocytol , vol.29 , pp. 551-567
    • Todd, B.A.1    Inman, C.2    Sedgwick, E.M.3
  • 13
    • 0034625467 scopus 로고    scopus 로고
    • Ionic permeability of the opossum sciatic nerve perineurium, examined using electrophysiological and electron microscopic techniques
    • Todd BA, Inman C, Sedgwick EM, et al. Ionic permeability of the opossum sciatic nerve perineurium, examined using electrophysiological and electron microscopic techniques. Brain Res 2000; 867: 223-231.
    • (2000) Brain Res , vol.867 , pp. 223-231
    • Todd, B.A.1    Inman, C.2    Sedgwick, E.M.3
  • 14
    • 84863938267 scopus 로고    scopus 로고
    • Transient opening of the perineurial barrier for analgesic drug delivery
    • Hackel D, Krug SM, Sauer RS, et al. Transient opening of the perineurial barrier for analgesic drug delivery. Proc Natl Acad Sci U S A 2012; 109: E2018-E2027.
    • (2012) Proc Natl Acad Sci U S A , vol.109
    • Hackel, D.1    Krug, S.M.2    Sauer, R.S.3
  • 15
    • 0035807817 scopus 로고    scopus 로고
    • Peripheral myelin protein 22 is a constituent of intercellular junctions in epithelia
    • Notterpek L, Roux KJ, Amici SA, et al. Peripheral myelin protein 22 is a constituent of intercellular junctions in epithelia. Proc Natl Acad Sci U S A 2001; 98: 14404-14409.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 14404-14409
    • Notterpek, L.1    Roux, K.J.2    Amici, S.A.3
  • 16
    • 79951830550 scopus 로고    scopus 로고
    • LSR defines cell corners for tricellular tight junction formation in epithelial cells
    • Masuda S, Oda Y, Sasaki H, et al. LSR defines cell corners for tricellular tight junction formation in epithelial cells. J Cell Sci 2011; 124: 548-555.
    • (2011) J Cell Sci , vol.124 , pp. 548-555
    • Masuda, S.1    Oda, Y.2    Sasaki, H.3
  • 17
    • 36749083418 scopus 로고    scopus 로고
    • Expression and function of junctional adhesion molecule-C in myelinated peripheral nerves
    • Scheiermann C, Meda P, Aurrand-Lions M, et al. Expression and function of junctional adhesion molecule-C in myelinated peripheral nerves. Science 2007; 318: 1472-1475.
    • (2007) Science , vol.318 , pp. 1472-1475
    • Scheiermann, C.1    Meda, P.2    Aurrand-Lions, M.3
  • 18
    • 0032521342 scopus 로고    scopus 로고
    • Myelin-associated glycoprotein is a myelin signal that modulates the caliber of myelinated axons
    • Yin X, Crawford TO, Griffin JW, et al. Myelin-associated glycoprotein is a myelin signal that modulates the caliber of myelinated axons. J Neurosci 1998; 18: 1953-1962.
    • (1998) J Neurosci , vol.18 , pp. 1953-1962
    • Yin, X.1    Crawford, T.O.2    Griffin, J.W.3
  • 19
    • 84861917238 scopus 로고    scopus 로고
    • Genetic disruption of Pten in a novel mouse model of tomaculous neuropathy
    • Goebbels S, Oltrogge JH, Wolfer S, et al. Genetic disruption of Pten in a novel mouse model of tomaculous neuropathy. EMBO Mol Med 2012; 4: 486-499.
    • (2012) EMBO Mol Med , vol.4 , pp. 486-499
    • Goebbels, S.1    Oltrogge, J.H.2    Wolfer, S.3
  • 20
    • 0033681225 scopus 로고    scopus 로고
    • Peripheral demyelination and neuropathic pain behavior in periaxin-deficient mice
    • Gillespie CS, Sherman DL, Fleetwood-Walker SM, et al. Peripheral demyelination and neuropathic pain behavior in periaxin-deficient mice. Neuron 2000; 26: 523-531.
    • (2000) Neuron , vol.26 , pp. 523-531
    • Gillespie, C.S.1    Sherman, D.L.2    Fleetwood-Walker, S.M.3
  • 21
    • 0034623082 scopus 로고    scopus 로고
    • Junctional adhesion molecule interacts with the PDZ domain-containing proteins AF-6 and ZO-1
    • Ebnet K, Schulz CU, Meyer zu Brickwedde MK, et al. Junctional adhesion molecule interacts with the PDZ domain-containing proteins AF-6 and ZO-1. J Biol Chem 2000; 275: 27979-27988.
    • (2000) J Biol Chem , vol.275 , pp. 27979-27988
    • Ebnet, K.1    Schulz, C.U.2    Meyer Zu Brickwedde, M.K.3
  • 22
    • 33847315194 scopus 로고    scopus 로고
    • JAM-C regulates tight junctions and integrin-mediated cell adhesion and migration
    • Mandicourt G, Iden S, Ebnet K, et al. JAM-C regulates tight junctions and integrin-mediated cell adhesion and migration. J Biol Chem 2007; 282: 1830-1837.
    • (2007) J Biol Chem , vol.282 , pp. 1830-1837
    • Mandicourt, G.1    Iden, S.2    Ebnet, K.3
  • 23
    • 79951520187 scopus 로고    scopus 로고
    • Actin polymerization is essential for myelin sheath fragmentation during Wallerian degeneration
    • Jung J, Cai W, Lee HK, et al. Actin polymerization is essential for myelin sheath fragmentation during Wallerian degeneration. J Neurosci 2011; 31: 2009-2015.
    • (2011) J Neurosci , vol.31 , pp. 2009-2015
    • Jung, J.1    Cai, W.2    Lee, H.K.3
  • 24
    • 33747495972 scopus 로고    scopus 로고
    • Junctional adhesion molecules (JAMs) are differentially expressed in fibroblasts and co-localize with ZO-1 to adherens-like junctions
    • Morris AP, Tawil A, Berkova Z, et al. Junctional adhesion molecules (JAMs) are differentially expressed in fibroblasts and co-localize with ZO-1 to adherens-like junctions. Cell Commun Adhes 2006; 13: 233-247.
    • (2006) Cell Commun Adhes , vol.13 , pp. 233-247
    • Morris, A.P.1    Tawil, A.2    Berkova, Z.3
  • 25
    • 0036429180 scopus 로고    scopus 로고
    • E-cadherin is required for the correct formation of autotypic adherens junctions of the outer mesaxon but not for the integrity of myelinated fibers of peripheral nerves
    • Young P, Boussadia O, Berger P, et al. E-cadherin is required for the correct formation of autotypic adherens junctions of the outer mesaxon but not for the integrity of myelinated fibers of peripheral nerves. Mol Cell Neurosci 2002; 21: 341-351.
    • (2002) Mol Cell Neurosci , vol.21 , pp. 341-351
    • Young, P.1    Boussadia, O.2    Berger, P.3
  • 26
    • 40949099049 scopus 로고    scopus 로고
    • Organization of multiprotein complexes at cell-cell junctions
    • Ebnet K,. Organization of multiprotein complexes at cell-cell junctions. Histochem Cell Biol 2008; 130: 1-20.
    • (2008) Histochem Cell Biol , vol.130 , pp. 1-20
    • Ebnet, K.1
  • 27
    • 74549139060 scopus 로고    scopus 로고
    • Zinc-alpha2-glycoprotein in cachexia and obesity
    • Tisdale MJ,. Zinc-alpha2-glycoprotein in cachexia and obesity. Curr Opin Support Palliat Care 2009; 3: 288-293.
    • (2009) Curr Opin Support Palliat Care , vol.3 , pp. 288-293
    • Tisdale, M.J.1
  • 28
    • 39849100440 scopus 로고    scopus 로고
    • Adherens and tight junctions: Structure, function and connections to the actin cytoskeleton
    • Hartsock A, Nelson WJ,. Adherens and tight junctions: structure, function and connections to the actin cytoskeleton. Biochim Biophys Acta 2008; 1778: 660-669.
    • (2008) Biochim Biophys Acta , vol.1778 , pp. 660-669
    • Hartsock, A.1    Nelson, W.J.2
  • 29
    • 0000325399 scopus 로고
    • The pathology of neuropathies with focal thickening of the myelin sheath (tomaculous neuropathy): Studies on the formation of the abnormal myelin sheath
    • Madrid R, Bradley G,. The pathology of neuropathies with focal thickening of the myelin sheath (tomaculous neuropathy): studies on the formation of the abnormal myelin sheath. J Neurol Sci 1975; 25: 415-448.
    • (1975) J Neurol Sci , vol.25 , pp. 415-448
    • Madrid, R.1    Bradley, G.2
  • 30
    • 21044437802 scopus 로고    scopus 로고
    • Tight junctions in Schwann cells of peripheral myelinated axons: A lesson from claudin-19-deficient mice
    • Miyamoto T, Morita K, Takemoto D, et al. Tight junctions in Schwann cells of peripheral myelinated axons: a lesson from claudin-19-deficient mice. J Cell Biol 2005; 169: 527-538.
    • (2005) J Cell Biol , vol.169 , pp. 527-538
    • Miyamoto, T.1    Morita, K.2    Takemoto, D.3
  • 31
    • 84863229734 scopus 로고    scopus 로고
    • Schwann cell-specific JAM-C-deficient mice reveal novel expression and functions for JAM-C in peripheral nerves
    • Colom B, Poitelon Y, Huang W, et al. Schwann cell-specific JAM-C-deficient mice reveal novel expression and functions for JAM-C in peripheral nerves. FASEB J 2012; 26: 1064-1076.
    • (2012) FASEB J , vol.26 , pp. 1064-1076
    • Colom, B.1    Poitelon, Y.2    Huang, W.3
  • 32
    • 0029799520 scopus 로고    scopus 로고
    • Functional dissociation of paracellular permeability and transepithelial electrical resistance and disruption of the apical-basolateral intramembrane diffusion barrier by expression of a mutant tight junction membrane protein
    • Balda MS, Whitney JA, Flores C, et al. Functional dissociation of paracellular permeability and transepithelial electrical resistance and disruption of the apical-basolateral intramembrane diffusion barrier by expression of a mutant tight junction membrane protein. J Cell Biol 1996; 134: 1031-1049.
    • (1996) J Cell Biol , vol.134 , pp. 1031-1049
    • Balda, M.S.1    Whitney, J.A.2    Flores, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.