Ecopipet spare part and service kit
- Known as:
- Ecopipet spare service reagent
- Catalog number:
- SKE-01
- Category:
- -
- Supplier:
- Capp
- Gene target:
- Ecopipet spare part and service kit
Related genes to: Ecopipet spare part and service kit
- Gene:
- SPRTN NIH gene
- Name:
- SprT-like N-terminal domain
- Previous symbol:
- C1orf124
- Synonyms:
- DKFZP547N043, Spartan, DVC1
- Chromosome:
- 1q42.2
- Locus Type:
- gene with protein product
- Date approved:
- 2005-06-23
- Date modifiied:
- 2016-10-18
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- The IVS4+919G>A founder variant causes a late-onset, cardiac-predominant form of Fabry disease, yet the severity of cardiac remodeling varies markedly among affected men. We studied 167 unrelated male carriers. Genome-wide association analyses included 81 men aged ≥50 years for left ventricular hypertrophy (LVH; left ventricular mass index [LVMI] ≥ 51 g/m) and septal hypertrophy (interventricular septal thickness at end-diastole [IVSd] ≥ 1.2 cm), and 149 men with plasma globotriaosylsphingosine (lyso-Gb3) measurements. Genotyping was performed with the Axiom Genome-Wide TPM 2.0 Array. Mean LVMI increased from 34.6 ± 11.3 g/m at 20-39 years to 75.1 ± 34.0 g/m at ≥60 years, although substantial variability persisted within each age stratum. rs1435166 and rs2572260, located in the adjacent / region, showed identical associations with LVH (both = 4.14 × 10) and concordant genotypes in all 81 participants (dosage r = 1.00; D' = 1.00), indicating a single regional association signal. The association remained evident in exact testing, Firth logistic regression, and an age-adjusted continuous-LVMI analysis yielded concordant results. In the age-adjusted analysis, each rs1435166 T allele was associated with a 12.8 g/m lower LVMI. Two intergenic variants met the exploratory threshold for septal hypertrophy, whereas no variant reached genome-wide significance for lyso-Gb3. These findings support the hypothesis that inherited genetic background contributes to variation in cardiac remodeling severity among carriers of the same pathogenic GLA variant. Independent replication, regional fine-mapping, and functional validation are required. - Source: PubMed
Publication date: 2026/08/20
Sung Kuo-TzuHsu Chih-YenLu Yung-HsiuHung Chung-LiehNiu Dau-Ming - Glyoxal (GO) is a small, highly reactive molecule that is produced naturally in cells during normal metabolism and can also come from processed foods and oxidative stress. Because of its high reactivity, glyoxal can modify DNA and proteins to form harmful products called advanced glycation end-products (AGEs), which have been linked to diseases such as diabetes, cancer, and aging. Although glyoxal is known to modify DNA and proteins, it is not well understood whether it can form DNA-protein crosslinks (DPCs), a type of DNA damage in which proteins become permanently attached to DNA. In this study, we investigated glyoxal induced DPC formation in HeLa cells using biochemical assays and mass spectrometry-based proteomics experiments. We observed that glyoxal exposure elevated cellular DPC formation in a concentration- and time-dependent manner. Cells with reduced SPRTN expression accumulated higher levels of DPCs, suggesting that SPRTN plays an important role in repairing glyoxal induced DNA damage. Proteomics experiments revealed 469 proteins exhibited elevated DNA association in glyoxal-treated samples, including histones and other proteins involved in chromatin organization, DNA replication, DNA repair, and gene expression. experiments confirmed that glyoxal can directly crosslink DNA with histone proteins. Overall, this study provides the first evidence that glyoxal forms DNA-protein crosslinks in human cells. These findings provide a foundation for future studies on the chemical structure, biological effects and repair of glyoxal induced DNA-protein crosslinks and their possible role in human disease. - Source: PubMed
Publication date: 2026/07/31
Gurajala Krishna CBarnes Elijah MErber Luke - DNA polymerase ζ (Polζ) is essential for replication across damaged DNA, yet the mechanisms governing its regulation in mammalian cells remain incompletely understood. The catalytic subunit REV3L is nearly twice the size of its yeast counterpart owing to a large vertebrate-specific insertion, and recent studies reported that REV3L undergoes proteolytic cleavage by the endopeptidase TASP1. Here, we show that REV3L cleavage generates two stable fragments, Nter-p70 and Cter-p300, which reassociate into a long-lived heterodimeric complex with enhanced polymerase activity. This interaction is stabilized by key residues within the catalytically inactive EXO domain. The cleaved Polζ complex associates with chromatin, binds nascent DNA, and undergoes ATR-dependent phosphorylation in response to replication stress. Importantly, preventing REV3L cleavage markedly impairs Polζ activity, reduces cisplatin-induced mutagenesis, and increases RAD51 nuclear foci and sister chromatid exchange, consistent with a compensatory shift toward homologous recombination-mediated repair. Together, our findings suggest that the vertebrate-specific expansion of REV3L necessitated cleavage to restore structural organization and optimize catalytic function, representing an evolutionary adaptation in DNA damage tolerance pathways. - Source: PubMed
Publication date: 2026/06/15
Goulas JordaneGuignier BasileBen Yamin BarbaraPouvelle CarolineYurchenko AndreyDespras Emmanuellede Oliveira LucianaLaplante PierreBochaton DorianPlassard DamienYang WeiTheillet François-XavierVeaute XavierWood Richard DNikolaev SergeyCordonnier Agnès MKannouche Patricia L - Topoisomerase 1 (TOP1) is essential for relieving DNA supercoils during replication and transcription. However, its transient reaction intermediates (TOP1 cleavage complexes or TOP1-DNA covalent complexes, i.e., TOP1ccs) become highly genotoxic when stabilized. While mechanisms that resolve chemotherapy-induced TOP1ccs are well-characterized, how cells prevent their accumulation under physiological conditions for securing genomic stability has remained elusive. Here, we elucidate a novel regulatory pathway in which CHK1-mediated phosphorylation of TOP1 at Serine-320 regulates its religation activity and hence limits steady-state TOP1cc levels during unperturbed cellular metabolism. We further demonstrate a distinct mechanism of TOP1cc stabilization, which escapes recognition by proteasomal and autophagic machineries, while being susceptible to CtIP, SPRTN, and p97-mediated removal. Defective phosphorylation of TOP1 at S320 impairs replication-fork progression, leading to replication- and transcription-associated DSBs, R-loop stabilization, genomic instability, and hypersensitivity to TOP1 poisons. Overall, our study assigns a new function to CHK1 in direct regulation of human TOP1cc dynamics, with critical implications for genomic integrity and combinatorial chemotherapy. - Source: PubMed
Publication date: 2026/05/13
Guha Majumdar AnandaChauhan NitishGupta PoojaSubramanian MaheshPatro Birija Sankar - The DNA-dependent metalloprotease SPRTN has emerged as a key enzyme in the proteolysis of DNA-protein crosslinks (DPCs), thereby protecting us against genome instability, accelerated ageing, and cancer. DNA and ubiquitin chains serve as the primary activator and catalyst of SPRTN proteolysis, respectively, but how they promote SPRTN activation and activity remains incompletely understood. To address this question, we developed a highly sensitive multi-turnover fluorescence resonance energy transfer (FRET) assay to monitor SPRTN proteolysis in real time. We found that the auto-cleaved N-terminal SPRTN fragment, comprising the metalloprotease domain (MPD), zinc-binding domain (ZBD), and basic region (BR), is highly stable, enzymatically active, and retains ubiquitin-dependent activation. Interestingly, the MPD alone exhibits basal intrinsic activity that is independent of both DNA activation and ubiquitin avidity effect. We show that ZBD and MPD together exert steric regulation: ZBD maintains MPD in an autoinhibited state, while MPD largely prevents ZBD from binding to DNA. BR, together with DNA, is essential to relieve ZBD-mediated inhibition of MPD. Using a site-trapping approach, we demonstrate that the ZBD-BR- DNA trinity induces an open conformation of the SPRTN N-terminus in cis, thereby releasing autoinhibition. MPD and BR together restrict the DNA-binding stoichiometry of ZBD, enabling SPRTN to function efficiently in proximity to DNA despite its low abundance in vivo. Collectively, our work overturns the long-standing dogma that SPRTN autocleavage inactivates the enzyme and reveals how DNA-induced conformational changes in SPRTN fine-tune its protease activity, providing a prerequisite for subsequent ubiquitin activation and rapid proteolysis of DPCs. - Source: PubMed
Publication date: 2026/05/01
Song WeiNewman Joseph AZhao YichenChalk RodRedfield ChristinaElliott Paul RRamadan Kristijan