Disease relevance of Kcna2

• In contrast, neuromyotonia sera bound more strongly to Kv1.2 subunits than to Kv1.1 or Kv1 [1].
• Ribonuclease protection, RNA blotting, and primer extension revealed that MK2-type RNA was the major MK RNA in retinoic acid-treated embryonal carcinoma cells [2].
• Hypoxia (PO(2)= approximately 30 mm Hg) reversibly inhibited Kv1.2 and Kv2.1 currents only at potentials more positive than 30 mV [3].

Psychiatry related information on Kcna2

• In chronic electroconvulsive shock-treated rats, Kv1.2 messenger RNA abundance showed similar changes to those in acute electroconvulsive shock: it was reduced 6 h after the last shock and had recovered after 24 h [4].

High impact information on Kcna2

• A family of three closely related potassium channel genes (MK1, MK2, and MK3) that are encoded at distinct genomic loci has been isolated [5].
• Currents expressed in naive CD4(+) lymphocytes are consistent with Kv1.1, Kv1.2, Kv1.3, and Kv1 [6].
• These structural changes were accompanied by a marked reduction of contactin-associated protein/paranodin, neurofascin 155 (NF155), and the potassium channel Kv1.2, whereas nodal clusters of sodium channels were unaltered [7].
• We characterized heteromultimeric channel complexes that consist of either Kv1.5 and Kv1.2 or Kv1.5 and Kv1 [8].
• 4. In postnatal day 4 (P4) sciatic nerve, most of the Kv1.2 channel subunits are involved in heteromultimeric association with Kv1 [8].

Biological context of Kcna2

• The protein levels of other Kv alpha subunits, Kv1.2 and Kv2.1, in contrast, are not affected by the expression of the Kv4.2W362F transgene [9].
• Moreover, normal glycosylation patterns are observed for Kv1.1 and Kv1.2 in whole brain lysates [10].
• The sPi4 was also found to compete with 125I-labeled apamin for binding to small-conductance Ca(2+)-activated K+ (SK) channels from rat brain synaptosomes (IC50 value of 0.5 microm). sPi4 is a high affinity blocker of the Kv1.2 channel [11].
• Kv1.1, Kv1.2, and Caspr2 all have PDZ binding sites and likely interact with the same PDZ binding protein [12].
• Moreover, hypoxia reversibly inhibited Kv1.2/Kv1.5 current activated at physiologically relevant membrane potentials ( approximately 65% at -40 mV) [3].

Anatomical context of Kcna2

• The greatest concentration of Kv1.2 was found in the basket cell axon plexus and terminal regions around the Purkinje cells [13].
• Unlike myelinated axons in the peripheral nervous system, there was no internodal strand of Kv1.1, Kv1.2, Kvbeta2, or Caspr2 [14].
• Localization of Kv1.1 and Kv1.2, two K channel proteins, to synaptic terminals, somata, and dendrites in the mouse brain [15].
• These results provide evidence that the neurological deficits associated with myelin deficiency reflect the altered distribution and expression of the K+ channel subunits Kv1.l and Kv1.2 along the internodes of spinal cord axons associated with the biophysical consequences caused by alterations in the myelin sheaths [16].
• In acute electroconvulsive shock experiments, Kv1.2 and Kv4.2 messenger RNA abundance in the dentate gyrus were reduced 6 h following the shock and returned to control levels after 24 h [4].

Associations of Kcna2 with chemical compounds

• The "fast" K+ channel blocker 4-aminopyridine, the toxin DTX-I, which targets the Kv1.1 and Kv1.2, but not DTX- K, which has higher selectivity for Kv1.1, increased the amplitude and area of CAPs of shiverer mice spinal cord axons but had insignificant effects in wild-type mice [16].

Other interactions of Kcna2

• The IKL remaining in -/- neurons was blocked by DTX, suggesting the underlying channels contained subunits Kv1.2 and/or Kv1.6 (also DTX-sensitive) [17].
• 1, Kv1.2 and their beta2 subunit are localized to the juxtaparanode [18].
• Coimmunoprecipitation experiments showed that Kv1.2 and Kvbeta1.1 interact in these tissues [19].
• Kv beta1.1/Kv beta2 double knockouts had significantly increased mortality compared with either single knockout but still maintained surface expression of Kv1.2, indicating that trafficking of this alpha subunit does not require either Kv beta subunit [20].
• Cx29 displayed a striking coincidence with Kv1.2 K(+) channels, which are localized in the axonal membrane [21].

Analytical, diagnostic and therapeutic context of Kcna2

• RT PCR on mRNA from enzymatically dissociated, isolated bipolar cells showed that these neurons express the Shaker-like K+ channels Kv1.1, Kv1.2, and Kv1 [22].
• Confocal immunohistochemistry showed that, unlike wild-type mice, which have a precise juxtaparanodal localization of the Kv1.l and Kv1.2 K+ channel subunits, shiverer mouse axons displayed a dispersed distribution of these subunits along the internodes [16].
• PS/2, R1-2, or MK2 significantly inhibited the recruitment of eosinophils and lymphocytes into the bronchoalveolar lavage (BAL) fluid and decreased inflammation in the lung tissues [23].

References