PMID- 10561689
OWN - NLM
STAT- MEDLINE
DCOM- 20000105
LR  - 20231213
IS  - 0360-4012 (Print)
IS  - 0360-4012 (Linking)
VI  - 58
IP  - 5
DP  - 1999 Dec 1
TI  - Altered molecular architecture of peripheral nerves in mice lacking the 
      peripheral myelin protein 22 or connexin32.
PG  - 612-23
AB  - Peripheral nerves of mutant mice deficient for peripheral myelin protein 22 
      (PMP22) or connexin32 (Cx32) display similar pathologies as observed in 
      hereditary human peripheral neuropathies. Mice lacking PMP22 develop focal 
      hypermyelination followed by myelin degeneration and axonal atrophy. 
      Cx32-deficient mice form normal myelin initially but develop demyelination and 
      remyelination at older ages. We have examined the lack of PMP22 or Cx32 on the 
      distribution of other components of the myelin sheath including myelin basic 
      protein (MBP), E-cadherin, and myelin-associated glycoprotein (MAG), as well as 
      the delayed rectifying potassium channel Kv1.1 as an intrinsic membrane protein 
      of axons. In peripheral nerves of wild-type mice, Kv1.1 is present as a pair of 
      juxtaparanodal clusters and a focal line extending longitudinally into the 
      internode, branching parallel and adjacent to Schmidt-Lanterman incisures. 
      Myelinated peripheral nerve fibers of 3-week-old PMP22(0/0) mice show tomacula 
      and abnormally short internodes of variable lengths with minor effects on the 
      localization of E-cadherin and Kv1.1. In older PMP22(0/0) mice, hypomyelinated 
      fibers contain supernumerary Schwann cells and loose focally restricted 
      E-cadherin and Kv1.1 expression. In contrast, remyelinated fibers in adult 
      Cx32(0/0) mice exhibit a correct localization of these marker proteins, except 
      that juxtaparanodal Kv1.1 clusters are aligned in abnormally short intervals of 
      regular distances accompanied by an increased number of Schwann cells. Thus, 
      different degrees of demyelination and remyelination in demyelinating mouse 
      models have variable effects on the confinement of specific proteins to 
      structural and functional internodal domains.
CI  - Copyright 1999 Wiley-Liss, Inc.
FAU - Neuberg, D H
AU  - Neuberg DH
AD  - Institute of Cell Biology, Swiss Federal Institute of Technology, ETH 
      Honggerberg, Zurich, Switzerland.
FAU - Sancho, S
AU  - Sancho S
FAU - Suter, U
AU  - Suter U
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Neurosci Res
JT  - Journal of neuroscience research
JID - 7600111
RN  - 0 (Cadherins)
RN  - 0 (Connexins)
RN  - 0 (Kcna1 protein, mouse)
RN  - 0 (Myelin Basic Protein)
RN  - 0 (Myelin Proteins)
RN  - 0 (Myelin-Associated Glycoprotein)
RN  - 0 (Pmp22 protein, mouse)
RN  - 0 (Potassium Channels)
RN  - 0 (Potassium Channels, Voltage-Gated)
RN  - 147173-20-4 (Kv1.1 Potassium Channel)
SB  - IM
MH  - Animals
MH  - Cadherins/analysis
MH  - Connexins/*genetics
MH  - Female
MH  - Genotype
MH  - Hereditary Sensory and Motor Neuropathy/*physiopathology
MH  - Immunohistochemistry
MH  - Kv1.1 Potassium Channel
MH  - Male
MH  - Mice
MH  - Mice, Knockout
MH  - Mutation
MH  - Myelin Basic Protein/analysis
MH  - Myelin Proteins/*genetics
MH  - Myelin Sheath/*chemistry/*pathology
MH  - Myelin-Associated Glycoprotein/analysis
MH  - Peripheral Nerves/*chemistry/*pathology
MH  - Potassium Channels/analysis
MH  - *Potassium Channels, Voltage-Gated
MH  - Time Factors
MH  - Gap Junction beta-1 Protein
EDAT- 1999/11/24 00:00
MHDA- 1999/11/24 00:01
CRDT- 1999/11/24 00:00
PHST- 1999/11/24 00:00 [pubmed]
PHST- 1999/11/24 00:01 [medline]
PHST- 1999/11/24 00:00 [entrez]
AID - 10.1002/(SICI)1097-4547(19991201)58:5<612::AID-JNR2>3.0.CO;2-X [pii]
AID - 10.1002/(sici)1097-4547(19991201)58:5<612::aid-jnr2>3.0.co;2-x [doi]
PST - ppublish
SO  - J Neurosci Res. 1999 Dec 1;58(5):612-23. doi: 
      10.1002/(sici)1097-4547(19991201)58:5<612::aid-jnr2>3.0.co;2-x.