Model of pregnant woman examination, 1 part
- Known as:
- Model pregnant woman examination, 1 part
- Catalog number:
- KMC033
- Product Quantity:
- Set
- Category:
- -
- Supplier:
- Kemaj
- Gene target:
- Model pregnant woman examination 1 part
Related genes to: Model of pregnant woman examination, 1 part
- 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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- DNA-protein cross-links (DPCs) represent a prevalent form of DNA damage that forms when cellular proteins become covalently trapped to DNA strands upon exposure to various endogenous and exogenous agents. Methylglyoxal is an endogenous metabolite that reacts with guanine and adenine bases in DNA and RNA, as well as cysteine, arginine, and lysine residues in proteins, generating advanced glycation end-products (AGEs), including DPCs. These modifications have been linked to human disease, including cancer, liver disease, diabetes, and neurodegenerative disorders. Herein, we present a mass spectrometry method for quantifying MGO-induced DNA-protein cross-links (DPCs) in human cells. We prepared an isotope NC-dG-MGO-Lys internal standard and developed a quantitative liquid chromatography-tandem mass spectrometry (LC-MS/MS) method for detecting and quantifying the formation and repair of dG-MGO-Lys DPCs in cells. Genomic DNA was extracted, subjected to sequential protease and nuclease digestion, purified by offline high-performance liquid chromatography (HPLC), and analyzed by LC-MS/MS. The method's standard curve showed a strong linear relationship across a concentration range of 10-1000 fmol ( = 0.9994). The method achieved limits of detection (LOD) and quantification (LOQ) of 10 and 20 fmol, respectively. Inhibition of proteasome and SPRTN activity revealed that SPRTN functions as a predominant proteolytic enzyme in MGO DPC repair. Overall, this analytical approach can offer valuable insights into the relevance of DPCs in diseases linked to elevated MGO levels. - Source: PubMed
Publication date: 2026/04/17
Omondi Reinner OBarnes Elijah MGurajala Krishna CFisette GabrielleChaudray Ibaad AErber Luke - Oxidative DNA damage caused by endogenous reactive oxygen species (ROS) is a key driver of mutagenesis, cellular dysfunction, and aging, contributing to diseases like cancer, neurodegeneration, rheumatoid arthritis, cardiovascular disorders, and diabetes. Although more than 20 oxidative base lesions have been identified, ROS-induced DNA-protein crosslinks (DPCs) are poorly characterized. ROS-DPCs are unusually bulky and highly toxic lesions that accumulate in metabolically active tissues with age, but their identities, biological consequences, and repair in living cells have remained elusive. In the present work, we characterized ROS-DPCs in human fibrosarcoma (HT1080) cells treated with hydrogen peroxide (HO) and elucidated the mechanisms of their removal. Mass spectrometry-based proteomics has identified over 100 cellular proteins that participated in DPC formation, most of which are involved in DNA metabolism. Our data further reveal that DNA replication and transcription facilitate DPC detection and identify a critical role of the ubiquitin-proteasomal system (UPS), replication-coupled activity of SPRTN metalloprotease, and nucleotide excision repair (NER) in removing ROS-induced DPCs. ROS-DPC formation was blocked by pretreatment with metabolically stable and cell-permeable glutathione (GSH) analog (Ψ-GSH), suggesting a possible therapeutic strategy for preventing diseases associated with increased ROS levels. - Source: PubMed
Publication date: 2026/03/13
Cyuzuzo Cesar IKruk MonicaZhang QiAlshareef DuhaHarmon JamesMachida Yuichi JVanKoten Harrison WMore Swati SCampbell ColinTretyakova Natalia Y - DNA-protein cross-links (DPCs) are highly toxic DNA lesions that block replication and transcription, but their impact on organismal physiology is unclear. We identified a role for the metalloprotease SPRTN in preventing DPC-driven immunity and its pathological consequences. Loss of SPRTN activity during replication and mitosis lead to unresolved DNA damage, chromosome segregation errors, micronuclei formation, and cytosolic DNA release that activates the cyclic GMP-AMP synthase (cGAS)-stimulator of interferon genes (STING) pathway. In a knock-in mouse model of Ruijs-Aalfs progeria syndrome, chronic cGas-Sting signaling caused embryonic lethality through inflammation and innate immune responses. Surviving mice displayed aging phenotypes beginning in embryogenesis, which persisted into adulthood. Genetic or pharmacological inhibition of cGas-Sting rescued embryonic lethality and alleviated progeroid phenotypes. - Source: PubMed
Publication date: 2026/01/29
Tomaskovic InesPrieto-Garcia CristianBoskovic MariaGlumac MateoTsai Tsung-LinMosler ThorstenKazi RubinaRathore RajeshwariAndrade JorgeHoffmann MarinaGiuliani GiulioJacomin Anne-ClairePereira Raquel SKnop EliasWachsmuth LaurensBeli PetraHusnjak KoraljkaPasparakis ManolisAblasser AndreaKrause Daniela SPotente MichaelPapathanasiou StamatisTerzic JanosDikic Ivan - - Source: PubMed
Publication date: 2026/01/16
Dzhaubermezov Murat AEkomasova Natalia VAkhmetshin Askar AAtabiev Biyaslan KhChagarov Ongar SGabidullina Liliya RSufyanova Zemfira RFedorova Yuliya YuNurgalieva Alfiia KhProkofyeva Darya SMiziev Ismail AChekanov Nikolay NKhusnutdinova Elza K - DNA-protein crosslinks (DPCs) are toxic DNA lesions formed by the covalent attachment of proteins to DNA. Failure to resolve DPCs leads to genomic instability, premature aging, and cancer predisposition. Although multiple proteases and the 26S proteasome degrade DPCs, how these lesions are detected and marked for proteolysis remains unclear. Here, we show that poly-(ADP-ribose) polymerases (PARP1/2) sense DPCs and modify them with poly(ADP-ribose) (PAR) to promote repair via a SPRTN-Tdp1 axis. We discovered a Nudix homology domain (NHD) in SPRTN that mediates direct non-covalent PAR binding and is important for DPC repair. Loss of PARP1/2 activity or mutation of the SPRTN NHD leads to sustained DPCs. Single-molecule analysis revealed that SPRTN does not bind efficiently to the DPC, however after the addition of PARP1 in the presence of NAD , SPRTN binding to the DPC was significantly increased. Our findings establish PARP1/2 enzymes as immediate DPC sensors, reveal PARylation as a signal marking DPCs for SPRTN-dependent degradation, and identify SPRTN as the first PARP-directed protease. - Source: PubMed
Publication date: 2026/01/09
Hurley KatelynLeary Liam PGarcia MartinRahman AyeshaSchaich Matthew AKloet Max SKumi-Ansah FrederickBlade Elizabeth GLiu QiangRhiner AndrewLe MeganSimonson QuinceeFilippov Dmitri Vvan der Heden van Noort Gerbrand JMcLellan Jason SVan Houten BennettLopez-Mosqueda Jaime