Ask about this productRelated genes to: LASS6 antibody
- Gene:
- CERS6 NIH gene
- Name:
- ceramide synthase 6
- Previous symbol:
- LASS6
- Synonyms:
- -
- Chromosome:
- 2q24.3
- Locus Type:
- gene with protein product
- Date approved:
- 2004-04-30
- Date modifiied:
- 2016-10-05
Related products to: LASS6 antibody
Related articles to: LASS6 antibody
- Ceramide synthases (CerS) are key enzymes in sphingolipid metabolism that regulate fundamental cellular processes, including apoptosis, cell growth, and homeostasis. Among the six known mammalian isoforms (CerS1-CerS6), CerS5 has been particularly well studied for its involvement in the synthesis of the sphingolipid C16-ceramide. However, its expression, localization, and functional significance of CerS5 in the retina remain unclear. In the present study, we investigated the presence, distribution, and functional role of CerS5 in mouse retina using CerS5 knockout (KO) mice. We performed quantitative polymerase chain reaction, X-gal staining, and immunohistochemistry to analyze the expression and localization. Electroretinography (ERG) was employed to assess the impact of CerS5 deficiency on retinal function. Our results demonstrated that CerS5 is localized to the inner nuclear layer and ganglion cell layer, co-localizing with horizontal cells and specific subsets of amacrine and ganglion cells. The retina of CerS5 KO mice showed a reduction in overall thickness, with significant thinning observed in all retinal layers except the photoreceptor, whereas the outer plexiform layer showed increased thickness. Despite these structural alterations, ERG recordings revealed no significant changes in retinal function. These findings suggest that CerS5 contributes to the maintenance of retinal structural integrity, particularly through its presence in specific retinal cell types, whereas its loss does not markedly impair retinal function in adult mice. The observed structural alterations highlight its potential role in retinal physiology and possible implications for retinal pathophysiology, warranting further investigation into compensatory mechanisms by other ceramide synthase isoforms. - Source: PubMed
Song Soo-JinKoo Jae-HyunKim Hee-YeonPark Joo-WonPaik Sun-SookKim In-BeomShin Jung-A - To investigate clinical and peripheral blood mononuclear cells (PBMCs) transcriptomic features associated with chronic brucellosis and to test the hypothesis that lipid metabolism-related transcriptomic alterations in PBMCs may be involved in chronic disease progression. - Source: PubMed
Publication date: 2026/07/02
Wang RongNiu BinZhang XinWang YinghanTian HaiyanZhang ChenmingZhang Liaoyun - Ceramides, a diverse class of bioactive sphingolipids, play a pivotal role in cellular stress response. We have previously reported a novel mechanism by which a particular member of this class, C-ceramide, activates death pathways in cancer cells. In this mechanism, C-ceramide, generated by ceramide synthase 6 (CerS6), binds directly to the tumor suppressor p53 and protects it from MDM2-mediated degradation, thereby promoting a stress response. In the present study, we investigated the mechanism by which p53 acquires ceramide, a highly hydrophobic molecule. Using bimolecular fluorescence complementation, we show that in cells under metabolic stress, p53 is recruited to the cytoplasmic surface of the ER by CerS6, the ER resident enzyme generating C-ceramide. The direct contact between the two proteins enables the transfer of C-ceramide from CerS6 to the DNA-binding domain of p53. Domain deletion experiments and pulldown assays with purified recombinant cytoplasmic fragments of CerS6 showed that the p53 physically interacts with the two large cytoplasmic loops of CerS6, forming a complex on the surface of the ER membrane. The interaction between p53 and CerS6 strictly requires the presence of C-ceramide in the catalytic site of the enzyme. Substitution of the CerS6 lumenal loop, which defines the enzyme's acyl chain specificity, with the corresponding loop of CerS2, which generates very-long-chain ceramides, abolished the interaction with p53. Our results uncover a previously unknown process, the direct C-ceramide transfer to the p53 DNA-binding domain at the ER surface, which is a mechanism regulating activation of this tumor suppressor. The findings that this mechanism is triggered upon metabolic stress induction by specific chemotherapeutics, as well as by nutrient and growth factor deprivation, highlight it as a promising target for cancer treatment. - Source: PubMed
Publication date: 2026/07/09
Childress Madeline SJeffries Kristen AHorita David AKrupenko Sergey AKrupenko Natalia I - Myopia is one of the most common eye diseases affecting children and adolescents, with its etiology often attributed to a combination of genetic and environmental factors. This study utilized single-cell RNA sequencing (scRNA-seq) technology to investigate gene expression differences between guinea pigs with spontaneous high myopia (SHM) and those with normal vision. - Source: PubMed
Publication date: 2026/07/02
Bao BoLiu JinpengXie YunxiaoXi RuofanSun YuecongYan JingzheXin JizhaoYang ZhaohuiYin XueweiGuo DadongBi Hongsheng - Diabetic kidney disease (DKD) is a critical microvascular complication of diabetes mellitus, and the current pharmacotherapies are limited by side effects. Medical and edible homology (MEH) Agents: The DKD and healthy control multi- -target active and low-toxic drugs (MEH) agents were identified based on transcriptomic data of DKD patients and healthy controls retrieved in the GEO database. - Source: PubMed
Publication date: 2026/06/30
Ning YaxianZhou XiaochunZhang LiliWang GouqinWang Jianqin