Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
24
pubmed:dateCreated
1985-2-21
pubmed:abstractText
Neuron-glia cell adhesion molecule (Ng-CAM) has previously been shown to be present exclusively on neurons and to mediate adhesion between neuronal membranes and glial cells. In the present study, its chain structure, binding functions, and relation to N-CAM (the other known CAM on neurons) were investigated further. Three polypeptide components of chicken Ng-CAM (Mr 200,000, 135,000, and 80,000) have been isolated. By using specific antisera against each component, the Mr 135,000 and Mr 80,000 components were found to cross-react antigenically with the Mr 200,000 component but not with each other. The conclusion that the Mr 135,000 and 80,000 components are structurally related to different regions of the Mr 200,000 component was further supported by the finding that 32P could be incorporated in vitro into the Mr 200,000 and 80,000 components but not into the Mr 135,000 component. Ng-CAM appears to be involved in both neuron-glia adhesion and neuron-neuron adhesion by distinguishable mechanisms that appear to involve different sites or conformations of the molecule. Polyclonal antibodies and a monoclonal antibody against Ng-CAM both inhibited adhesion between glia and neurons derived from brain, cerebellum, and retina. In contrast, antibodies against N-CAM (which inhibit neuron-neuron adhesion) did not inhibit neuron-glia adhesion. These findings confirm the proposed function of Ng-CAM in neuron-glia adhesion. In addition, however, Ng-CAM was found to be involved directly or indirectly in neuron-neuron adhesion. Non-cross-reactive polyclonal anti-Ng-CAM and anti-N-CAM antibodies each inhibited the aggregation of neurons from whole brain and cerebellum and the inhibition was greater when both antibodies were present together. In contrast, monoclonal anti-Ng-CAM antibodies were found that inhibited neuron-glia adhesion but did not inhibit neuronal cell aggregation. The amount of Ng-CAM expressed on neurons was not directly predictive of the effect of anti-Ng-CAM antibodies on their homotypic aggregation. Although Ng-CAM and N-CAM can be expressed simultaneously on individual neurons, the ratio of N-CAM to Ng-CAM ranged from 1.5 for cerebellar cells to 10.0 for retinal cells. While, as expected, retinal cell aggregation was inhibitable only by anti-N-CAM, cerebellar cells, which expressed at least as much Ng-CAM as brain cells, showed significantly less inhibition by anti-Ng-CAM antibodies. These findings raise the possibility that Ng-CAM may actually interact with N-CAM to yield non-linear effects. That Ng-CAM and N-CAM may function differently in vivo was suggested by their distribution in sections of brain regions. Within the cerebellum, for example, immunofluorescent anti-N-CAM staining was relatively uniform in all layers; in contrast anti-Ng-CAM staining was absent on dividing external granule cells and was present in greatest abundance on processes of post-mitotic migratory cells in the molecular layer. These observations are consistent with the hypothesis that Ng-CAM mediates neuron-glia adhesion and is thereby also involved in neuronal migration along radial glial cells.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/6393132-320200, http://linkedlifedata.com/resource/pubmed/commentcorrection/6393132-388439, http://linkedlifedata.com/resource/pubmed/commentcorrection/6393132-4101340, http://linkedlifedata.com/resource/pubmed/commentcorrection/6393132-4113154, http://linkedlifedata.com/resource/pubmed/commentcorrection/6393132-4160044, http://linkedlifedata.com/resource/pubmed/commentcorrection/6393132-5432063, http://linkedlifedata.com/resource/pubmed/commentcorrection/6393132-6165990, http://linkedlifedata.com/resource/pubmed/commentcorrection/6393132-6194561, http://linkedlifedata.com/resource/pubmed/commentcorrection/6393132-6201120, http://linkedlifedata.com/resource/pubmed/commentcorrection/6393132-6208560, http://linkedlifedata.com/resource/pubmed/commentcorrection/6393132-6364137, http://linkedlifedata.com/resource/pubmed/commentcorrection/6393132-6474186, http://linkedlifedata.com/resource/pubmed/commentcorrection/6393132-6576344, http://linkedlifedata.com/resource/pubmed/commentcorrection/6393132-6577452, http://linkedlifedata.com/resource/pubmed/commentcorrection/6393132-6586373, http://linkedlifedata.com/resource/pubmed/commentcorrection/6393132-6586374, http://linkedlifedata.com/resource/pubmed/commentcorrection/6393132-6725397, http://linkedlifedata.com/resource/pubmed/commentcorrection/6393132-6791580, http://linkedlifedata.com/resource/pubmed/commentcorrection/6393132-6823544, http://linkedlifedata.com/resource/pubmed/commentcorrection/6393132-6959151, http://linkedlifedata.com/resource/pubmed/commentcorrection/6393132-7085646, http://linkedlifedata.com/resource/pubmed/commentcorrection/6393132-893445
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:volume
81
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7989-93
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Polypeptide components and binding functions of neuron-glia cell adhesion molecules.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.