PMID- 15056698
OWN - NLM
STAT- MEDLINE
DCOM- 20040618
LR  - 20231213
IS  - 1529-2401 (Electronic)
IS  - 0270-6474 (Print)
IS  - 0270-6474 (Linking)
VI  - 24
IP  - 13
DP  - 2004 Mar 31
TI  - Connexin32-containing gap junctions in Schwann cells at the internodal zone of 
      partial myelin compaction and in Schmidt-Lanterman incisures.
PG  - 3186-98
AB  - In vertebrate peripheral nerves, the insulating myelin sheath is formed by 
      Schwann cells, which generate flattened membrane processes that spiral around 
      axons and form compact myelin by extrusion of cytoplasm and adhesion of apposed 
      intracellular and extracellular membrane surfaces. Cytoplasm remains within the 
      innermost and outermost tongues, in the paranodal loops bordering nodes of 
      Ranvier and in Schmidt-Lanterman incisures. By immunocytochemistry, connexin32 
      (Cx32) protein has been demonstrated at paranodal loops and Schmidt-Lanterman 
      incisures, and it is widely assumed that gap junctions are present in these 
      locations, thereby providing a direct radial route for transport of ions and 
      metabolites between cytoplasmic myelin layers. This study used freeze-fracture 
      replica immunogold labeling to detect Cx32 in ultrastructurally defined gap 
      junctions in Schmidt-Lanterman incisures, as well as in a novel location, between 
      the outer two layers of internodal myelin, approximately every micrometer along 
      the entire length of myelin, at the zone between compact myelin and noncompact 
      myelin. Thus, these gap junctions link the partially compacted second layer of 
      myelin to the noncompact outer tongue. Although these gap junctions are unusually 
      small (average, 11 connexon channels), their relative abundance and regular 
      distribution along the zone that is structurally intermediate between compact and 
      noncompact myelin demonstrates the existence of multiple sites for unidirectional 
      or bidirectional transport of water, ions, and small molecules between these two 
      distinct cytoplasmic compartments, possibly to regulate or facilitate myelin 
      compaction or to maintain the transition zone between noncompact and compact 
      myelin.
FAU - Meier, Carola
AU  - Meier C
AD  - Department of Neuroanatomy and Molecular Brain Research, Ruhr-University Bochum, 
      44801 Bochum, Germany. carola.meier@ruhr-uni-bochum.de
FAU - Dermietzel, Rolf
AU  - Dermietzel R
FAU - Davidson, Kimberly G V
AU  - Davidson KG
FAU - Yasumura, Thomas
AU  - Yasumura T
FAU - Rash, John E
AU  - Rash JE
LA  - eng
GR  - R01 NS038121/NS/NINDS NIH HHS/United States
GR  - R01 NS044395/NS/NINDS NIH HHS/United States
GR  - R01 NS044010/NS/NINDS NIH HHS/United States
GR  - NS38121/NS/NINDS NIH HHS/United States
GR  - NS-44010/NS/NINDS NIH HHS/United States
GR  - NS-39040/NS/NINDS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Neurosci
JT  - The Journal of neuroscience : the official journal of the Society for 
      Neuroscience
JID - 8102140
RN  - 0 (Connexins)
SB  - IM
MH  - Animals
MH  - Connexins/*biosynthesis
MH  - Female
MH  - Freeze Fracturing
MH  - Gap Junctions/*metabolism/*ultrastructure
MH  - Immunohistochemistry
MH  - Male
MH  - Mice
MH  - Mice, Inbred C57BL
MH  - Mice, Knockout
MH  - Myelin Sheath/metabolism/*ultrastructure
MH  - Ranvier's Nodes/metabolism/*ultrastructure
MH  - Schwann Cells/*cytology/metabolism/ultrastructure
MH  - Sciatic Nerve/metabolism/ultrastructure
MH  - Gap Junction beta-1 Protein
PMC - PMC1803337
MID - NIHMS17737
EDAT- 2004/04/02 05:00
MHDA- 2004/06/24 05:00
PMCR- 2004/09/30
CRDT- 2004/04/02 05:00
PHST- 2004/04/02 05:00 [pubmed]
PHST- 2004/06/24 05:00 [medline]
PHST- 2004/04/02 05:00 [entrez]
PHST- 2004/09/30 00:00 [pmc-release]
AID - 24/13/3186 [pii]
AID - 10.1523/JNEUROSCI.5146-03.2004 [doi]
PST - ppublish
SO  - J Neurosci. 2004 Mar 31;24(13):3186-98. doi: 10.1523/JNEUROSCI.5146-03.2004.