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Gene Review

Scn2a  -  sodium channel, voltage-gated, type II,...

Rattus norvegicus

Synonyms: NachII, Nav1.2, RII/RIIA, RNSCPIIR, SCN, ...
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High impact information on Scn2a1

  • Recent studies have shown that glutathione S-transferase fusion proteins containing portions of Nav1.2 intracellular domains interact directly with ankyrinG [1].
  • Single-cell RT-PCR reveals that several alpha-subunit isoforms of the Na+ channels are co-expressed within a single hair cell, with a major expression of Nav1.2 and Nav1.6 subunits [2].
  • Various types of Na+ channel alpha-subunits, i.e., Nav1.1, Nav1.2, and Nav1.6, have been described in rodent Purkinje cells [3].
  • Comparison of the effects of four Na+ channel analgesics on TTX-resistant Na+ currents in rat sensory neurons and recombinant Nav1.2 channels [4].
  • Ambroxol blocked resting TTX-r channels more potently than Nav1.2, the opposite was the case for lidocaine, mexiletine and benzocaine [4].

Anatomical context of Scn2a1

  • SWDs increased with age in WAG/Rij rats. mRNA levels for sodium channels Nav1.1 and Nav1.6, but not Nav1.2, were found to be up-regulated selectively within the facial somatosensory cortex (at AP +0.0, ML +6.0 mm) [5].

Associations of Scn2a1 with chemical compounds

  • Nimodipine treatment caused a moderate reduction (approximately 30%) of the mRNA for Nav1.2 and a marked reduction (approximately 70%) of the mRNA for Nav1.3, whereas treatment with Bay K 8644 produced 90-130% increases in these same mRNAs [6].

Analytical, diagnostic and therapeutic context of Scn2a1

  • As evidenced by RT-PCR and immunocytochemical analysis, morphologically differentiated CG cells expressed Nav1.2 and Nav1.6, though both subunits appeared to be differentially regulated [7].
  • In this study, the effects of four Na(+) channel blockers on rat tetrodotoxin-resistant (TTX-r) Na(+) channels (representing mostly Nav1.8) in sensory neurons were investigated using the patch-clamp technique in the voltage-clamp configuration, and compared with those on cells heterologously expressing Nav1.2 alpha subunits [4].


  1. Sodium channel beta1 subunit-mediated modulation of Nav1.2 currents and cell surface density is dependent on interactions with contactin and ankyrin. McEwen, D.P., Meadows, L.S., Chen, C., Thyagarajan, V., Isom, L.L. J. Biol. Chem. (2004) [Pubmed]
  2. Voltage-gated Na+ channel activation induces both action potentials in utricular hair cells and brain-derived neurotrophic factor release in the rat utricle during a restricted period of development. Chabbert, C., Mechaly, I., Sieso, V., Giraud, P., Brugeaud, A., Lehouelleur, J., Couraud, F., Valmier, J., Sans, A. J. Physiol. (Lond.) (2003) [Pubmed]
  3. Voltage-gated sodium channels in cerebellar Purkinje cells of mormyrid fish. de Ruiter, M.M., De Zeeuw, C.I., Hansel, C. J. Neurophysiol. (2006) [Pubmed]
  4. Comparison of the effects of four Na+ channel analgesics on TTX-resistant Na+ currents in rat sensory neurons and recombinant Nav1.2 channels. Weiser, T. Neurosci. Lett. (2006) [Pubmed]
  5. Dysregulation of sodium channel expression in cortical neurons in a rodent model of absence epilepsy. Klein, J.P., Khera, D.S., Nersesyan, H., Kimchi, E.Y., Waxman, S.G., Blumenfeld, H. Brain Res. (2004) [Pubmed]
  6. L-type calcium channel activation up-regulates the mRNAs for two different sodium channel alpha subunits (Nav1.2 and Nav1.3) in rat pituitary GH3 cells. Vega, A.V., Espinosa, J.L., López-Domínguez, A.M., López-Santiago, L.F., Navarrete, A., Cota, G. Brain Res. Mol. Brain Res. (2003) [Pubmed]
  7. Differential targeting and functional specialization of sodium channels in cultured cerebellar granule cells. Osorio, N., Alcaraz, G., Padilla, F., Couraud, F., Delmas, P., Crest, M. J. Physiol. (Lond.) (2005) [Pubmed]
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