Ask about this productRelated genes to: SCNN1G antibody
- Gene:
- SCNN1G NIH gene
- Name:
- sodium channel epithelial 1 gamma subunit
- Previous symbol:
- -
- Synonyms:
- ENaCgamma, SCNEG
- Chromosome:
- 16p12.2
- Locus Type:
- gene with protein product
- Date approved:
- 1995-05-10
- Date modifiied:
- 2018-03-02
Related products to: SCNN1G antibody
Related articles to: SCNN1G antibody
- Aldosterone synthase deficiency (ASD), which is caused by a genetic defect in CYP11B2, involves a deficiency in aldosterone alone. Newborn and early childhood ASD patients can present with salt-wasting symptoms. In severe cases, this can lead to shock and be life-threatening. ASD must also be differentiated from another disease, pseudohypoaldosteronism type 1 (PHA1), which involves resistance to aldosterone. PHA1 can be classified into PHA1a, PHA1b, and secondary PHA1. PHA1a is caused by a heterozygous defect in NR3C2, which encodes the mineralocorticoid receptor. PHA1b is an autosomal recessive disorder caused by defects in the 3 epithelial sodium channel subunits α, β, and γ, encoded by SCNN1A, SCNN1B, and SCNN1G. Since ASD is a very rare disorder, the "The Intractable Adrenal Disorders Research by the Ministry of Health, Labour, and Welfare" developed the "Diagnostic criteria and severity classification for aldosterone synthase deficiency" to better understand the disorder. The criteria are as follows: Clinical symptoms: patient meets criteria 1 and 2. 1) Presents with salt-wasting symptoms (poor feeding, vomiting, dehydration, poor weight gain). 2) No skin pigmentation. Laboratory findings: patient meets criteria 1 through 3. 1) Low serum sodium and high serum potassium. 2) Low to normal plasma aldosterone and high plasma renin activity or high plasma active renin concentration. 3) No low blood cortisol level. Diagnoses of exclusion include PHA1, 21-hydroxylase deficiency, congenital lipoid adrenal hyperplasia, and congenital adrenal hypoplasia. We believe that the diagnostic criteria of ASD will enable clinicians and researchers to better understand congenital aldosterone deficiency. - Source: PubMed
Publication date: 2026/03/27
Tajima ToshihiroAmano NaokoIshii TomohiroOtuski MichioKatabami TakuyukiKashimada KenichiHasegawa TomonobuMukai TokuoYoshida YuichiShibata Hirotaka - The epithelial sodium channel (ENaC) is essential for sodium reabsorption and potassium homeostasis in the distal nephron, where its activity is controlled by mineralocorticoid signaling and downstream proteolytic processing of channel subunits. Although cleavage of the γ-ENaC subunit has been implicated in aldosterone-mediated sodium transport, the identity of mineralocorticoid receptor (MR)-regulated proteases responsible for this process remains uncertain. Here, we investigated the role of kallikrein-1 (encoded by ), a serine protease expressed in the connecting tubule and cortical collecting duct (CNT/CCD), as a mediator of ENaC activation. Using CRISPR/Cas9, we generated a conditional -floxed allele and established mice with CNT/CCD-specific deletion of by crossing with -Cre (CNT-). On a low-sodium, high-potassium diet, CNT-mice exhibited ∼85% less renal kallikrein-1 expression, yet maintained normal serum electrolytes, urinary potassium excretion, and aldosterone responses. Western blot analysis revealed significantly less cleavage of γ-ENaC and α-ENaC in CNT- kidneys, accompanied by more total NCC abundance. Despite impaired ENaC proteolysis, amiloride-sensitive sodium excretion was preserved, indicating intact ENaC function. These findings identify renal kallikrein-1 as a protease that contributes to ENaC subunit processing in vivo. However, the absence of overt sodium or potassium handling defects in CNT- mice suggests that kallikrein-1 deficiency is not sufficient to disrupt overall ENaC function, likely due to compensatory mechanisms from redundant proteolytic or nonproteolytic pathways. Together, our results refine the role of kallikrein-1 as a modulator, rather than a sole determinant, of ENaC activation and highlight the complexity of aldosterone-dependent sodium transport in the distal nephron. Using a novel connecting tubule/cortical collecting duct specific kallikrein-1 knockout model, we show that γ- and α-ENaC cleavage is impaired by loss of renal kallikrein-1, without major disturbances in sodium or potassium handling. These findings highlight redundancy among ENaC regulatory pathways and suggest that proteolytic cleavage of ENaC, although useful as an indicator of ENaC-mediated transport under physiological conditions, may not, in and of itself, play a major role in ENaC function. - Source: PubMed
Publication date: 2026/02/11
Curry Joshua NSu Xiao-TongWu QiMaeoka YujiroYang Chao-LingDelpire EricFenton Robert AWelling Paul AEllison David H - Asthma is characterised by a chronic inflammation and airway remodelling. The functionality of the asthma airway epithelium is altered, suggesting a central role in the pathophysiology. Cilia-associated abnormalities have been reported in the airway epithelium of asthmatic patients, but the mechanisms remain elusive. This study investigated cilia-associated dysregulations in cohorts of patients with severe asthma to identify and characterize key molecular drivers of epithelial airway remodelling. - Source: PubMed
Publication date: 2026/02/09
Devilliers Maëva ASaber Cherif LyndaBrisebarre AudreyChouquet RubyBralet LudivineAncel JulienVivien AlexandreLuczka-Majérus EmilieBonnomet ArnaudLalun NathalieTaillé CamilleDubernard XavierMérol Jean-ClaudeRuaux ChristophePolette MyriamDeslée GaëtanPerotin Jeanne-MarieDormoy Valérian - This study investigated the molecular regulation of uterine calcium ion (Ca²⁺) transport during the oviposition cycle in Guizhou Sansui ducks. Uterine tissues were collected at 0, 2, 5, and 16 h after oviposition to determine Ca²⁺ concentrations and quantify the mRNA levels of ten Ca²⁺ transport-related genes, including transient receptor potential vanilloid 6 (TRPV6), inositol 1,4,5-trisphosphate receptor type 1 (IP3R1), inositol 1,4,5-trisphosphate receptor type 2 (IP3R2), inositol 1,4,5-trisphosphate receptor type 3 (IP3R3), solute carrier family 4 member 4 (SLC4A4), solute carrier family 4 member 9 (SLC4A9), potassium inwardly-rectifying channel subfamily J member 15 (KCNJ15), sodium channel epithelial subunit gamma (SCNN1G), adenosyl homocysteinase-like 1 (AHCYL1), and protein kinase C alpha (PRKCA). In addition, the expression profiles of these ten genes were assessed across 12 tissues (heart, liver, spleen, lung, kidney, large intestine, small intestine, duodenum, pancreas, proventriculus, gizzard, and pectoral muscle) at the four oviposition time points. The results showed that the Ca²⁺ concentration in the uterine tissue was relatively low at 0 h, increased at 2 h and 5 h (P < 0.01), and reached its peak at 16 h (P < 0.01). The expression of the ten genes showed an overall upward trend, with TRPV6 slightly decreasing initially and then continuously increasing. Correlation analysis revealed that at 0 h, uterine Ca²⁺ concentration was negatively correlated with IP3R2 and KCNJ15 (P < 0.05), while IP3R2 was positively correlated with KCNJ15 (P < 0.05). At 2 h, TRPV6 expression was negatively correlated with both Ca²⁺ concentration and KCNJ15 (P < 0.05). At 16 h, Ca²⁺ concentration was negatively correlated with SCNN1G but positively correlated with SLC4A9 (P < 0.05). All ten genes were expressed across 12 tissues, showing distinct temporal and spatial patterns. These results suggest that TRPV6, IP3Rs (IP3R1, IP3R2, and IP3R3), SLC4A4/9, KCNJ15, SCNN1G, AHCYL1, and PRKCA may cooperatively regulate uterine Ca²⁺ absorption, intracellular release, and local homeostasis, while their tissue-specific expression reflects systemic regulation of calcium metabolism. - Source: PubMed
Publication date: 2026/01/09
Zhao YongLiao ChaomeiFu HongmeiDing YijieGuo XingchenZhang Yiyu - This study employed primary uterine epithelial cells from Sansui ducks (Anas platyrhynchos) at the peak of lay as an in vitro model. Using shRNA-mediated interference, we generated single knockdowns of inositol 1,4,5-trisphosphate receptor type 1 (IP3R1), inositol 1,4,5-trisphosphate receptor type 2 (IP3R2), and inositol 1,4,5-trisphosphate receptor type 3 (IP3R3), as well as dual knockdowns of IP3R1+IP3R2, IP3R1+IP3R3, and IP3R2+IP3R3, and a triple knockdown targeting all three IP3R isoforms. These treatments were designed to elucidate the regulatory effects of IP3R expression on intracellular calcium ion (Ca²⁺) concentrations and the expression of genes related to ion transport. After 48 h of transfection, fluorescence labeling with the Fluo-3/AM probe showed that intracellular Ca²⁺ concentrations were significantly higher in all treatment groups compared with the control group (P < 0.01). The real-time qPCR (RT-qPCR) analysis of ten ion transport-related genes revealed that the expression of transient receptor potential cation channel subfamily V member 6 (TRPV6), ORAI calcium release-activated calcium modulator 1 (ORAI1), epithelial sodium channel gamma subunit (SCNN1G), solute carrier family 8 member A1 (SLC8A1), ATPase plasma membrane Ca²⁺-transporting 1 (ATP2B1), and ATPase sarcoplasmic/endoplasmic reticulum Ca²⁺-transporting 2 (ATP2A2) was significantly downregulated in multiple IP3R knockdown groups compared with the NC group (P < 0.05). The expression levels of these genes also showed significant correlations with intracellular Ca²⁺ levels (P < 0.05), including both positive and negative correlations. In the IP3R1 knockdown group, TRPV6, ORAI1, and SCNN1G were negatively correlated with Ca²⁺ concentration (P < 0.05). In contrast, ATP2B1 exhibited a positive correlation with Ca²⁺ in the IP3R2 knockdown group (P < 0.01), whereas SLC8A1 expression was positively correlated with Ca²⁺ in the IP3R1 + IP3R3 dual knockdowns group (P < 0.05). Collectively, the knockdown of IP3Rs not only reduced intracellular calcium ion (Ca²⁺) release but also altered the expression of ion channel-related genes, thereby affecting Ca²⁺ homeostasis. These findings provide new molecular evidence for the regulatory role of IP₃Rs in ion transport networks and Ca²⁺ balance in uterine epithelial cells of laying ducks. - Source: PubMed
Publication date: 2026/01/11
Zhao YongYou MinfangDing YijieFu HongmeiGuo XingchenZhang Yiyu