CIDE-A Antibody
- Known as:
- CIDE-A Antibody
- Catalog number:
- 2085
- Product Quantity:
- 0.1 mg
- Category:
- -
- Supplier:
- Prosci
- Gene target:
- CIDE- Antibody
Related genes to: CIDE-A Antibody
- Gene:
- CIDEA NIH gene
- Name:
- cell death inducing DFFA like effector a
- Previous symbol:
- -
- Synonyms:
- CIDE-A
- Chromosome:
- 18p11.21
- Locus Type:
- gene with protein product
- Date approved:
- 1998-07-15
- Date modifiied:
- 2018-10-08
- Gene:
- CIDEC NIH gene
- Name:
- cell death inducing DFFA like effector c
- Previous symbol:
- -
- Synonyms:
- CIDE-3, FLJ20871, Fsp27
- Chromosome:
- 3p25.3
- Locus Type:
- gene with protein product
- Date approved:
- 2004-07-26
- Date modifiied:
- 2016-10-05
- Gene:
- CIDECP1 NIH gene
- Name:
- cell death inducing DFFA like effector c pseudogene 1
- Previous symbol:
- CIDECP
- Synonyms:
- CICE
- Chromosome:
- 3p25.3
- Locus Type:
- pseudogene
- Date approved:
- 2007-07-26
- Date modifiied:
- 2018-10-08
Related products to: CIDE-A Antibody
Related articles to: CIDE-A Antibody
- Hepatitis C virus (HCV) depends on host lipid metabolism and lipid droplets (LDs) for genome replication, assembly, and particle production, yet how LD structure and lipid utilization change over the course of infection remains incompletely understood. Here, we investigated the temporal remodeling of LD-associated metabolic pathways during HCV JFH-1 infection of human hepatoma Huh7 cells. HCV infection transiently increased LD fluorescence intensity at 24 hours post-infection (hpi), followed by normalization or relative loss of LD signal at later time points. Concomitantly, LDs became progressively clustered and enlargement during late infection, despite reduced protein levels of the canonical LD fusion proteins CIDEA, CIDEB, and CIDEC, suggesting that HCV-induced LD enlargement occurs through CIDE-independent mechanisms. Transcriptomic, RT-qPCR, and immunoblot analyses revealed time-dependent regulation of genes and proteins involved in LD structure, triglyceride synthesis, lipolysis, lipid uptake, and mitochondrial fatty acid utilization. Subcellular fractionation demonstrated preferential accumulation of fatty acids in mitochondrial fractions at 24-72 hpi. This redistribution was accompanied by increased oxygen consumption rate, elevated extracellular acidification, and progressive reactive oxygen species accumulation, indicating infection-associated metabolic activation and oxidative stress. Pharmacological inhibition of DGAT1-dependent LD biogenesis, LIPA-dependent lysosomal lipid hydrolysis, LIPE/HSL-dependent lipolysis, or CPT1-dependent mitochondrial fatty acid transport markedly reduced mitochondrial fatty acid accumulation and suppressed HCV-induced respiratory activity. Inhibition of LIPA or LIPE/HSL reduced both HCV RNA and core protein levels, whereas inhibition of CPT1 or DGAT1 had more pronounced effects on core protein than on viral RNA. Together, these findings support a model in which HCV dynamically remodels LDs, mobilizes LD-associated fatty acids, and redirects them toward mitochondria to support infection-associated metabolism and downstream stages of the viral life cycle. Lipid hydrolysis and mitochondrial fatty acid trafficking therefore represent potential host-directed targets for limiting HCV infection. - Source: PubMed
Publication date: 2026/07/10
Muhammad ImaanCraft KaciPei ShaokaiConte KaiaLi JunyanTeng ShaoleiCruz-Cosme RuthYang ShaominZhang YanjinTang Qiyi - Aneurysm progression is associated with complex molecular alterations that are insufficiently studied at transcriptomics level. An aneurysm is characterized as a bulge or a weak spot in a blood artery's wall that causes the vessel to abnormally enlarge or balloon, exceeding 50% of its normal diameter. In the present study aneurysm RNA sequencing (RNA-Seq) dataset involving 14 samples, which include 7 controls and 7 treatments was selected for the analysis. Pathway analysis showed the involvement of key genes in major shifts within lipid metabolism pathways. The protein-protein interaction (PPI) network analysis using the STRING database identified key hub genes that were significantly differentially expressed, including LIPE, SREBF1, SCARB2, LPL, PNPLA2, UCP1, CIDEC, DGAT2, CIDEA and FABP4. These key gene-encoded proteins may be prominent drug targets for future interventions aimed at treating aneurysms. - Source: PubMed
Publication date: 2026/03/31
Lois G ShirleyMurugan ShanmugapriyaJaganathan Mohana ShanmugamS Dhanush KumarJ Jino Blessy - Early and complete weaning has been shown to induce steatohepatitis in mice fed a standard diet (Adachi et al., Am J Physiol Endocrinol Metab. 2025;329:E455-E462). However, whether subsequent high-fat high-sucrose (HF/HS) diet intake exacerbates this pathology, and how endoplasmic reticulum (ER) stress-related transcription factors and epigenetic regulation contribute to this process remain unclear. - Source: PubMed
Publication date: 2026/03/17
Adachi HarukaIshiyama ShioriYoshimura KentaroKasai HirotakeMochizuki Kazuki - Obesity poses a significant risk for metabolic disorders, such as insulin resistance and metabolic-associated fatty liver disease (MAFLD), yet effective treatments remain limited. Cell Death-Inducing DNA Fragmentation Factor-α-Like Effector C (CIDEC), a lipid droplet membrane protein, facilitates lipid droplet fusion and is crucial for adipose tissue expansion, making it a key target for obesity and related metabolic diseases. However, previous research revealed that complete genetic deletion of Cidec in adipose tissues, while reducing fat accumulation, induced severe insulin resistance in high-fat diet (HFD)-fed mice, potentially due to ectopic fat storage in the liver. Given that complete knockout is an extreme approach, partial inhibition holds greater clinical relevance. Therefore, this study aimed to investigate the effects of partial inhibition of CIDEC in adipose tissues on fat accumulation and insulin sensitivity in mice. Using the Cre-LoxP system, we generated adipose Cidec haploinsufficient mice. Under a standard diet, these mice exhibited normal body weight, fat accumulation, and insulin sensitivity. Notably, under HFD conditions, mice with partial Cidec deficiency showed reduced fat accumulation in adipose tissues while hepatic fat accumulation remained unchanged, accompanied by improved insulin sensitivity and increased energy expenditure. Mechanistically, we found partial Cidec deficiency activated thermogenic program in adipocytes in vivo and in vitro through the ATGL-PPARα pathway. In conclusion, adipose CIDEC partial inhibition attenuates HFD-induced obesity and insulin resistance by enhancing ATGL-PPARα-mediated energy expenditure, establishing this approach as a promising therapeutic strategy for obesity and related metabolic diseases. - Source: PubMed
Publication date: 2025/07/07
Fu QinghuaWang PengLi WeilinCai ZhenhuaZhao ShijiLing WeidongLi MingxunTang XiaochuanSong Ziyi - The cell death-inducing DFF45-like effector (CIDE) family comprises CIDEA, CIDEB, and CIDEC (fat-specific protein of 27 kDa), all of which are lipid droplet-associated proteins and contribute to fat storage and energy homeostasis. However, the relative impacts of these isoforms on fat storage in adipose tissue and obesity in humans have been unclear. We here examined the expression of CIDE family genes in visceral adipose tissue (VAT) of obese individuals who underwent laparoscopic sleeve gastrectomy and explored its relation to adiposity-related parameters. RNA-sequencing analysis revealed that and were highly expressed in VAT, whereas was expressed at a substantially lower level. and expression levels were positively correlated with body fat mass and subcutaneous adipose tissue (SAT) area, whereas expression was negatively correlated with these markers. In addition, and expression levels showed positive and negative correlations, respectively, with BMI. Multivariable regression analysis showed that only expression was significantly associated with body fat mass. Stratification of the subjects according to tertiles of expression revealed that BMI, body fat mass, and SAT area were significantly greater in the highest expression group than in the other two groups. Our findings thus suggest that, among CIDE isoforms, CIDEC is the most closely associated with fat storage in human adipose tissue. - Source: PubMed
Publication date: 2025/04/08
Iwahashi YasuyukiNishikage SeijiHosokawa YuseiYamada TomokoNakagawa YasushiHirota YushiSakaguchi KazuhikoNishimoto YukiNakajima ShinsukeKitahama SeiichiYamamoto YasuyoshiMukai TomoichiroOgawa WataruTamori Yoshikazu