Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
19
pubmed:dateCreated
2001-9-21
pubmed:abstractText
Contactin (also known as F3, F11) is a surface glycoprotein that has significant homology with the beta2 subunit of voltage-gated Na(+) channels. Contactin and Na(+) channels can be reciprocally coimmunoprecipitated from brain homogenates, indicating association within a complex. Cells cotransfected with Na(+) channel Na(v)1.2alpha and beta1 subunits and contactin have threefold to fourfold higher peak Na(+) currents than cells with Na(v)1.2alpha alone, Na(v)1.2/beta1, Na(v)1.2/contactin, or Na(v)1.2/beta1/beta2. These cells also have a correspondingly higher saxitoxin binding, suggesting an increased Na(+) channel surface membrane density. Coimmunoprecipitation of different subunits from cell lines shows that contactin interacts specifically with the beta1 subunit. In the PNS, immunocytochemical studies show a transient colocalization of contactin and Na(+) channels at new nodes of Ranvier forming during remyelination. In the CNS, there is a particularly high level of colocalization of Na(+) channels and contactin at nodes both during development and in the adult. Contactin may thus significantly influence the functional expression and distribution of Na(+) channels in neurons.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1529-2401
pubmed:author
pubmed:issnType
Electronic
pubmed:day
1
pubmed:volume
21
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7517-25
pubmed:dateRevised
2011-7-22
pubmed:meshHeading
pubmed-meshheading:11567041-Animals, pubmed-meshheading:11567041-Axons, pubmed-meshheading:11567041-Binding, Competitive, pubmed-meshheading:11567041-Brain Chemistry, pubmed-meshheading:11567041-CHO Cells, pubmed-meshheading:11567041-Cell Adhesion Molecules, Neuronal, pubmed-meshheading:11567041-Cell Line, pubmed-meshheading:11567041-Cell Membrane, pubmed-meshheading:11567041-Contactins, pubmed-meshheading:11567041-Cricetinae, pubmed-meshheading:11567041-Demyelinating Diseases, pubmed-meshheading:11567041-Female, pubmed-meshheading:11567041-Gene Expression, pubmed-meshheading:11567041-Lysophosphatidylcholines, pubmed-meshheading:11567041-Nerve Tissue Proteins, pubmed-meshheading:11567041-Patch-Clamp Techniques, pubmed-meshheading:11567041-Precipitin Tests, pubmed-meshheading:11567041-Protein Subunits, pubmed-meshheading:11567041-Ranvier's Nodes, pubmed-meshheading:11567041-Rats, pubmed-meshheading:11567041-Saxitoxin, pubmed-meshheading:11567041-Sciatic Nerve, pubmed-meshheading:11567041-Sodium, pubmed-meshheading:11567041-Sodium Channel Blockers, pubmed-meshheading:11567041-Sodium Channels, pubmed-meshheading:11567041-Tetrodotoxin, pubmed-meshheading:11567041-Transfection
pubmed:year
2001
pubmed:articleTitle
Contactin associates with Na+ channels and increases their functional expression.
pubmed:affiliation
Departments of Neurobiology/Anatomy and Biochemistry/Biophysics, University of Rochester Medical Center, Rochester, New York 14642, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.