Ask about this productRelated genes to: SCLY antibody
- Gene:
- SCLY NIH gene
- Name:
- selenocysteine lyase
- Previous symbol:
- -
- Synonyms:
- SCL
- Chromosome:
- 2q37.3
- Locus Type:
- gene with protein product
- Date approved:
- 2004-02-03
- Date modifiied:
- 2016-07-29
Related products to: SCLY antibody
Related articles to: SCLY antibody
- The altered expression of transposon element (TE)-derived genes that regulate immune responses implied the involvement of previous viral infections in the onset of Fragile X disorders (FXD), often bearing sustained inflammation. Here, we discovered that hypoxia greatly modifies the expression of TE-derived genes that act as oxygen-free radical scavengers, resulting in an alkylating environment under normoxia in FXD. Molybdenum cofactor synthesis 3 (MOCS3) and selenocysteine lyase (SCLY) stabilize the association of Kelch-like ECH-associated protein 1 (KEAP1) with PGAM family member 5 (PGAM5). This rewires connections between the oxidative stress response, cysteine-sulfur and selenium metabolism, and oxidoreductases. Desensitized tRNA thiolation against hypoxia in FXD suggests that the rewired radical scavenging system induces resistance to ROS in FXD. - Source: PubMed
Publication date: 2026/02/04
Suganuma TamakiHassan HuzaifaSwanson Selene KLaxman SunilWorkman Jerry L - Renal ischemia-reperfusion (IR) injury is a major cause of acute kidney injury (AKI), with limited specific therapies. Recombinant human brain natriuretic peptide (rhBNP) shows potential renal protective effects, but its role and mechanism in IR-induced AKI is unclear. The present study showed rhBNP improved renal function recovery and reduced AKI progression in ICU patients. In rat IR models, rhBNP alleviated tubular injury and enhanced kidney function. Selenocysteine lyase (SCLY), an enzyme critical for selenium recycling and selenoprotein synthesis, was identified as the hub gene associated with rhBNP treatment by transcriptome sequencing. rhBNP treatment markedly upregulated the expression of SCLY in rat kidneys with elevated selenium levels. rhBNP also inhibited ferroptosis and apoptosis in the kidney, which was significantly reversed by the knockdown of SCLY. SCLY silencing blocked the protective effect of rhBNP on human HK2 cells subjected to CCCP-R (carbonyl cyanide 3-chlorophenylhydrazone induced ATP depletion-repletion), while SCLY overexpression enhanced it. rhBNP modulated SCLY expression likely through inhibiting the binding of active GTPase RhoA to SCLY protein. In conclusion, rhBNP prevented IR-induced AKI through inhibiting ferroptosis by upregulating SCLY level and promoting selenium recycling, presenting a potentially new target for AKI treatment. - Source: PubMed
Publication date: 2025/12/31
Huang MeiyingWang LuhaoWang MinghuiYuan XiLi MengLong LuoshaWu XinyanXu LongZhao XiaoduoLiang BaienGuan XiangdongWang WeidongLi ChunlingWu Jianfeng - The enzyme selenocysteine (Sec) lyase (SCLY) decomposes Sec, releasing selenide for the synthesis of selenoproteins, which contain Sec in their primary structure and participate in strong redox reactions, maintaining redox balance. We previously showed that global disruption of the gene (Scly KO) in mice leads to obesity. Targeted deletion of in agouti-related peptide neurons enhances energy expenditure and brown adipose tissue (BAT) activation, augmenting leanness. We hypothesized that Scly KO mice develop obesity due to failure of BAT-controlled mechanisms of energy expenditure due to redirection of Sec to an alternative pathway. We analyzed BAT from male Scly KO mice on selenium (Se)-adequate [0.25 parts per million (ppm)] and Se-deficient (0.08 ppm) diets for morphology, Se content, selenoprotein expression, thyroid hormones, and additional Sec-using pathways. We found that the BAT of Scly KO mice was enlarged, with lower Se levels, and substantial whitening on a Se-adequate diet. This phenotype worsened on low Se and coincided with a mild impairment in adapting to cold exposure. BAT whitening coincided with an increase in triglycerides and reduced 3-hydroxy-3-methylglutaryl coenzyme A and cholesterol. BAT selenoproteins regulating energy metabolism, type 2 iodothyronine deiodinase (DIO2), glutathione peroxidase 1 (GPX1), and glutathione peroxidase 1 (GPX4), were significantly decreased. DIO2 reduction corresponded with an increase in thyroxine and thyroid-stimulating hormone and a reduction in heat-producing uncoupling protein 1. Downregulation of GPX4 did not affect ferroptosis in the BAT. Therefore, the whitened BAT of the KO mouse is a multifactorial process involving the disruption of BAT function through changes to selenoproteins involved in energy metabolism. Global loss of the selenocysteine-decomposing enzyme selenocysteine lyase in mice leads to lipid accumulation and whitening of the brown adipose tissue, with consequent obesity development. Selenocysteine lyase modulates selenium levels and selenoprotein expression, specifically GPX1, GPX4, and DIO2, in brown adipocytes. Selenocysteine metabolic fate hinges on the actions of selenocysteine lyase. - Source: PubMed
Publication date: 2025/12/26
Shimada Briana KOgawa-Wong Ashley NSoares Antonio GHallam Kayla ASantiago Princess J DSaelua KaitlynNakahara-Akita Kescher KTorres Daniel JBrockman John DKurokawa SuguruEwell Kris LBellinger Miyoko TToh PamelaLagatta Pamplona Remedios GabrielaAlfulaij NaghumSwanson Sydonie MSeyedali AliZavacki Ann MarieBerry Marla JSeale Lucia A - Brown adipocytes (BA), the predominant cell type in brown adipose tissue (BAT), are essential for adaptive thermogenesis in response to environmental temperature or diets that impact energy expenditure. BAT thermogenic activation is regulated by thyroid hormones (TH) and norepinephrine, with TH activation carried out by the selenoprotein class of deiodinases, making BAT reliant on the micronutrient selenium (Se). Se is utilized to synthesize selenocysteine (Sec), incorporated into selenoproteins. The enzyme Sec lyase (Scly) decomposes Sec to provide selenide for selenoprotein synthesis. Besides deiodinases, glutathione peroxidases (GPXs) are critical selenoproteins for antioxidant defense and redox balance in BAT. Whole-body Scly knockout (KO) mice exhibit obesity, glucose intolerance, fatty liver, and BAT whitening. However, the specific tissue where Scly loss drives this phenotype remains unclear. As BAT regulates energy expenditure and glucose metabolism, we hypothesized either hepatocyte or BA Scly deletion drives the observed phenotype in Scly KO mice. We generated hepatocyte-specific and BA-specific Scly KO mice and assessed metabolic and thermogenic outcomes. Hepatocyte-specific Scly KO mice showed no metabolic phenotype, suggesting hepatic Scly is dispensable. BA-specific Scly KO mice exhibited normal glucose and insulin tolerance. Under Se-deficiency, male BA-specific Scly KO mice recovered body temperature after initial cold-induced thermogenic impairment. Only male mice showed reduced expression of GPX1 and GPX4 in BAT across diets, without TH impairments. These findings demonstrate that Scly in BA supports local Se homeostasis and selenoprotein expression in a sex- and Se-dependent manner, with its loss leading to transient thermoregulatory impairment, contributing to the Scly KO phenotype. - Source: PubMed
Publication date: 2025/12/09
Santiago P J DShimada B KAlfulaij NHallam K ASoares A GYoung VSwanson S MRemedios G LToh PSeale L A - Dietary selenium (Se) deficiency elevates the risk of cardiometabolic disorders driven by excessive caloric dietary intake. A high-fat diet leads to redox imbalance and elevates lipid deposits in the heart regardless of sex. Selenium maintains redox homeostasis by regulating the levels of antioxidant selenoproteins, such as glutathione peroxidases 1 and 4 (GPX1,4) and thioredoxin reductases 1 and 2. Se-dependent tissues such as the heart have a recycling mechanism to maintain selenoprotein synthesis, especially when Se is limiting, carried out by the enzyme selenocysteine lyase (SCLY). Despite being highly reliant on Se to function properly, it remains unclear if SCLY is required to modulate Se and selenoprotein synthesis in the heart, particularly in obesity. In this study, we analyzed cardiomyocyte (CM) function and molecular modifications in the hearts of male and female whole body knockout ( KO) mice fed a Se-deficient, obesogenic diet. We found sex-specific differences demonstrating that the loss of SCLY activity is more detrimental to the hearts of female mice on an obesogenic diet than in male mice, due to reduced glutathione (GSH) peroxidase 1 and 4 expression and decreased circulating Se levels. In addition, overall GPX activity and total GSH levels in KO female hearts resulted in significantly reduced CM contractility. In summary, the loss of , coupled with Se deficiency and a high-fat diet reduces the ability of the GSH system to mitigate oxidative stress in female hearts, increasing redox imbalances that favor the establishment of cardiometabolic disorders. Global loss of selenocysteine lyase controls the glutathione system in the heart, impacting glutathione peroxidase protein levels and activity, and glutathione levels in a mouse model of obesity. Loss of selenocysteine lyase and selenomethionine deficiency impacts cardiomyocyte function and selenoproteins in a sexually dimorphic nature, with females being affected more than males when mice are on a high-fat diet. - Source: PubMed
Publication date: 2025/10/24
Shimada Briana KWatanabe MarissaApo Takayama Nadia KSoares Antonio GHallam Kayla ARivers Orion SEwell KrisSantiago Princess J DSwanson Sydonie MToh PamelaAlfulaij NaghumBerry Marla JSeale Lucia A