Linked Life Data

9067844

Source:http://linkedlifedata.com/resource/pubmed/id/9067844

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1997-6-6
pubmed:abstractText
The distribution and cellular localization of connexin32 (Cx32) in the brain and spinal cord of the mouse and rat was investigated by light microscope (LM) and electron microscope (EM) immunohistochemistry by using several different antibodies against Cx32. By double immunofluorescence staining for Cx32 and either the oligodendrocyte markers cyclic nucleotide phosphodiesterase (CNPase) or Rip, Cx32 was consistently found in oligodendrocyte cell bodies and proximal processes. Cx32 immunoreactivity was also clearly visualized along CNPase- and Rip-positive myelinated fibers. Both immunopositive cells and fibers were heterogeneously distributed and were often more intensely labeled when dispersed in or associated with regions of gray matter than when concentrated in major white matter tracts. Labeling of myelin sheaths along fibers was restricted to subpopulations of myelinated axons. In the cerebellar cortex, for example, it was selectively localized to sheaths around Purkinje cell axons. Punctate staining, distinct from that corresponding to cells or fibers, was evident in the olfactory bulb and hippocampus. By EM, oligodendrocytes exhibited cytoplasmic labeling associated with rough endoplasmic reticulum and Golgi apparatus. Their processes were intermittently stained, most intensely when surrounding myelinated fibers and occasionally in paranodal loops. Cx32-immunoreactive gap junctions with symmetric labeling (staining on both junctional membranes) were observed between oligodendrocytic somata and processes as well as between presumptive oligodendrocytic processes. Unidentifiable elements forming asymmetrically labeled gap junctions (staining only one side of junctional membranes) were less frequently encountered. Western blot analysis confirmed anti-Cx32 antibody detection of Cx32 in whole brain homogenates and an enrichment of the protein in isolated myelin fractions. These results are consistent with earlier ultrastructural studies showing the occurrence of inter-oligodendrocytic gap junctions, but indicate that these may be more prevalent than previously thought. Furthermore, the results suggest a specialized role of gap junctions composed of Cx32 along myelinated fibers belonging to subpopulations of neurons.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0021-9967
pubmed:author
pubmed:issnType
Print
pubmed:day
24
pubmed:volume
379
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
571-91
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Connexin32 in oligodendrocytes and association with myelinated fibers in mouse and rat brain.
pubmed:affiliation
Department of Physiology, University of Manitoba, Winnipeg, Canada.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't