Linked Life Data

1322979

Source:http://linkedlifedata.com/resource/pubmed/id/1322979

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
1992-9-4
pubmed:abstractText
We have characterized voltage-dependent sodium channels in growth cones (GCPs) isolated from fetal rat brain using saxitoxin and TTX binding as well as recordings from channels reconstituted into lipid bilayer membranes. Both high- and low-affinity binding sites are present in GCP membranes. However, the two binding sites are segregated largely or completely, with the high-affinity binding sites in the plasmalemma, and the low-affinity sites in an internal membrane compartment. Plasmalemmal insertion of these internal sites can be triggered by high-potassium depolarization and depends on a metalloendoprotease-requiring mechanism. These observations indicate that a precursor-product relationship exists between the internal and external sodium channels of the growth cone, and therefore suggest that channel externalization causes conversion of low-affinity to high-affinity saxitoxin receptors. This conversion may represent a step of channel capacitation.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0270-6474
pubmed:author
pubmed:issnType
Print
pubmed:volume
12
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2948-59
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Plasmalemmal insertion and modification of sodium channels at the nerve growth cone.
pubmed:affiliation
Department of Cellular and Structural Biology, University of Colorado School of Medicine, Denver 80262.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.