PT  - JOURNAL ARTICLE
AU  - Katie Kazarinova-Noyes
AU  - Jyoti Dhar Malhotra
AU  - Dyke P. McEwen
AU  - Laura N. Mattei
AU  - Erik O. Berglund
AU  - Barbara Ranscht
AU  - S. Rock Levinson
AU  - Melitta Schachner
AU  - Peter Shrager
AU  - Lori L. Isom
AU  - Zhi-Cheng Xiao
TI  - Contactin Associates with Na<sup>+</sup> Channels and Increases Their Functional Expression
AID  - 10.1523/JNEUROSCI.21-19-07517.2001
DP  - 2001 Oct 01
TA  - The Journal of Neuroscience
PG  - 7517--7525
VI  - 21
IP  - 19
4099  - http://www.jneurosci.org/content/21/19/7517.short
4100  - http://www.jneurosci.org/content/21/19/7517.full
SO  - J. Neurosci.2001 Oct 01; 21
AB  - Contactin (also known as F3, F11) is a surface glycoprotein that has significant homology with the β2 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 Nav1.2α and β1 subunits and contactin have threefold to fourfold higher peak Na+ currents than cells with Nav1.2α alone, Nav1.2/β1, Nav1.2/contactin, or Nav1.2/β1/β2. 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 β1 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.