Ask about this productRelated genes to: SMPDL3B antibody
- Gene:
- SMPDL3B NIH gene
- Name:
- sphingomyelin phosphodiesterase acid like 3B
- Previous symbol:
- -
- Synonyms:
- ASML3B
- Chromosome:
- 1p35.3
- Locus Type:
- gene with protein product
- Date approved:
- 2004-04-20
- Date modifiied:
- 2016-01-25
Related products to: SMPDL3B antibody
Related articles to: SMPDL3B antibody
- Sirtuin 1 (Sirt1), a member of the sirtuin family, is integral to the regulation of energy homeostasis, cellular metabolism, and stress responses. While Sirt1 has been intensively studied in mammals, studies on this gene in aquatic animals, especially turbot, is relatively limited. In this study, the sirt1 gene was cloned. The open reading frame (ORF) of the Sirt1 consists of 2187 base pairs, encoding a 728-amino-acid protein that contains a SIR2 domain. Compared with the siRNA-NC group, Sirt1 knockdown resulted in a significant downregulation of mRNA expression levels of the tight junction proteins occludin, tricellulin, claudin3, and zo1, as well as protein levels of Occludin and ZO1, within the intestinal tissue of turbot. Concurrently, it markedly inhibited the expression of genes associated with ceramide synthesis (sptlc2, kdsr, cers1, cers2, cers3, smpdl3a, smpdl3b, neu1, glb1, gba1, and sgpp2) and ceramide catabolism (sgms1a, ugcg, b4galt, and sphk1) in the same tissue. Conversely, compared to the pcDNA3.1 group, Sirt1 overexpression significantly enhanced the mRNA expression levels of occludin, tricellulin, claudin3, claudin7, and zo1, along with the protein level of Occludin. Furthermore, Sirt1 overexpression significantly elevated the expression of genes involved in ceramide synthesis (cers2, cers3, smpd3, smpdl3b, neu1, glb1, gba1, sgpp2) and ceramide catabolism (sgms1a, galt, b4galt, and sphk1). These results suggest that Sirt1 may influence the intestinal mechanical barrier by acting on the metabolic balance of ceramide and altering the expression of intestinal tight junction proteins, thus playing a crucial role in maintaining the intestinal health of turbot. - Source: PubMed
Publication date: 2026/03/18
Ma XiuhuaLiu QianhuiMai KangsenZhang Yanjiao - Kidney toxicity remains a major dose-limiting complication of radiation therapy and platinum-based chemotherapy, yet the molecular determinants of renal susceptibility and resilience to these genotoxic treatments are incompletely understood. Podocytes are particularly vulnerable to such insults, and emerging evidence implicates lipid dysregulation in podocyte injury. This study investigated the role of sphingomyelin phosphodiesterase acid-like 3B (SMPDL3B), a podocyte-enriched lipid-modulating enzyme, in radiation- and cisplatin-induced nephrotoxicity. Using a doxycycline-inducible, podocyte-specific SMPDL3B transgenic mouse model, renal injury was assessed following focal kidney irradiation, cisplatin administration, or their combination through functional assays, histopathology, ultrastructural analysis, immunofluorescence, and targeted lipidomics. Combined radiation and cisplatin exposure markedly reduced podocyte SMPDL3B expression, accompanied by podocyte depletion, glomerular basement membrane remodeling, proteinuria, and impaired renal function. These structural and functional abnormalities were associated with the selective accumulation of long-chain ceramide-1-phosphate species. In contrast, podocyte-specific induction of SMPDL3B preserved glomerular architecture, maintained renal function, and prevented pathological ceramide-1-phosphate elevation. Collectively, these findings identify SMPDL3B as a key regulator of podocyte stability and lipid homeostasis during chemoradiation stress. Enhancing SMPDL3B activity may represent a mechanistically grounded strategy to mitigate treatment-induced kidney injury while preserving anticancer efficacy. - Source: PubMed
Publication date: 2026/01/22
Ahmad AnisMallela Shamroop KumarAnsari SabaAlnukhali MohammedMerscher SandraMitrofanova AllaZeidan Youssef HPollack AlanFornoni AlessiaMarples Brian - - Source: PubMed
Publication date: 2026/01/16
Rostami-Afshari BitaElremaly WesamFranco AnitaMoreau Alain - - Source: PubMed
Publication date: 2025/11/21
Wang ZhimengHou YanfeiLiu PeiyuanWu RuinanYang JiamingFan ShilongPeng ZexuHan XiaoxuSu BinZhang Conggang - - Source: PubMed
Publication date: 2025/11/20
Chen JieYan Lina