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Nickerson, A.

Publications and source records attributed to Nickerson, A..

2 recordsLinked to original sources

A pain-reducing Kv6.4 variant spares other Kv6 channels, offering a target for uterine pain

Uterine pain conditions such as dysmenorrhea and endometriosis are highly prevalent, poorly managed, and associated with long-term impacts on womens health. The identification of a rare KCNG4 variant (rs140124801; p.Val419Met) previously linked to reduced labor pain suggests Kv6.4 (encoded by KCNG4) may play a role in visceral nociception and offer a new target for non-opioid uterine pain relief. We analyzed UK Biobank data to evaluate clinical phenotypes associated with rare single nucleotide polymorphisms (SNPs) in the conserved TVGYG selectivity filter motif of the Kv6 family wherein p.Val419Met is located. Functional consequences of these variants were assessed using immunofluorescence in SHSY5Y cells to examine membrane trafficking, co-immunoprecipitation to investigate interactions between Kv6 subunits and Kv2.1, and single-cell RNA sequencing to determine expression patterns in mouse sensory neurons. Our genetic analysis identified 5,816 individuals heterozygous and 28 homozygous for the p.Val419Met variant, as well as 292 heterozygous carriers of the p.Thr418Met variant, all located in the Kv6.4 subunit. Neither variant was associated with increased risk for general, neurological, or pain-related disorders, even in homozygous p.Val419Met carriers, supporting a favorable safety profile. Kv6.4Val419Met has a dominant negative effect on wild type Kv6.4. However, this effect is specific to Kv6.4 as, in SHSY5Y cells, co-expression of Kv6.4Val419Met along with Kv6.1, Kv6.2 or Kv6.3, showed no effects on the efficient membrane localization of Kv6.1-3. In contrast, Kv6.4Thr418Met does not interfere with Kv6.4 trafficking or its heteromerization with Kv2.1. Additionally, In SHSY5Y cells, the equivalent p.Val419Met substitution, when introduced into Kv6.1, Kv6.2 and Kv6.3, disrupts their membrane localization, noting that these variants have never been reported. Co-immunoprecipitation shows that Kv6.4 does not interact with other Kv6 subunits and transcriptomic analysis shows that Kv6.4 is expressed in a distinct subset of mouse lumbar dorsal root ganglion neurons innervating pelvic organs. Our findings show that the Kv6.4Val419Met variant selectively disrupts Kv6.4 function without affecting other family members and is not linked to adverse phenotypes. This finding supports Kv6.4 as a highly selective and functionally distinct Kv6 subunit with no widespread deleterious effects on other Kv6 subunits, making it an attractive candidate for therapeutic targeting for uterine pain.

genetics↗

Proteolytic Cleavage of the ENaC gamma Subunit: Impact Upon Na+ and K+ Handling

The ENaC gamma subunit is essential for homeostasis of Na+, K+, and body fluid. Dual subunit cleavage before and after a short inhibitory tract allows dissociation of this tract, increasing channel open probability (PO), in vitro. Cleavage proximal to the tract occurs at a furin recognition sequence (143RKRR146 in mouse). Loss of furin-mediated cleavage prevents in vitro activation of the channel by proteolysis at distal sites. We hypothesized that 143RKRR146 mutation to 143QQQQ146 (Q4) in 129/Sv mice would reduce ENaC PO, impair flow-stimulated flux of Na+ (JNa) and K+ (JK) in perfused collecting ducts, reduce colonic amiloride-sensitive short circuit current (ISC), and impair Na+, K+, and body fluid homeostasis. Immunoblot of Q4/Q4 mouse kidney lysates confirmed loss of a band consistent in size with the furin-cleaved proteolytic fragment. However, Q4/Q4 male mice on a low Na+ diet did not exhibit altered ENaC PO or flow-induced JNa, though flow-induced JK modestly decreased. Colonic amiloride-sensitive ISC in Q4/Q4 mice was not altered. Q4/Q4 males, but not females, exhibited mildly impaired fluid volume conservation when challenged with a low Na+ diet. Blood Na+ and K+ were unchanged on a regular, low Na+, or high K+ diet. These findings suggest that biochemical evidence of gamma subunit cleavage should not be used in isolation to evaluate ENaC activity. Further, factors independent of gamma subunit cleavage modulate channel PO and the influence of ENaC on Na+, K+, and fluid volume homeostasis in 129/Sv mice, in vivo.

physiology↗