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].

References