Ask about this productRelated genes to: SERPINC1 antibody
- Gene:
- SERPINC1 NIH gene
- Name:
- serpin family C member 1
- Previous symbol:
- AT3
- Synonyms:
- ATIII, MGC22579
- Chromosome:
- 1q25.1
- Locus Type:
- gene with protein product
- Date approved:
- 1986-01-01
- Date modifiied:
- 2019-04-23
Related products to: SERPINC1 antibody
Related articles to: SERPINC1 antibody
- To establish a rapid whole-genome sequencing (rWGS) workflow applicable to the neonatal intensive care unit (NICU) setting and evaluate its diagnostic utility and clinical feasibility. Twenty critically ill neonates with suspected genetic disorders were included in this study. A workflow for rWGS encompassing neonate enrollment through to the return of genetic diagnosis results was established. A trio-based rWGS data analysis was performed using DRAGEN-GATK-Hail, with results reviewed and reported by a multidisciplinary team. The average turnaround time for the 20 NICU neonates was 5.5 working days. Genetic diagnoses were achieved in ten cases, resulting in a diagnostic yield of 50%, based on the clinical database and variant pathogenicity assessments. The identified diagnostic variants were located across nine genes, including AGT, ANK1, NSD1, SERPINC1, OTC (in two cases), INS, PKHD1, SAMD9, and LZTR1. The clinical implications were confirmed in all ten diagnosed neonates, with 'genetic counseling and recurrence risk management', 'early therapeutic decision-making' and 'enhancement of clinical outcomes and survival rates'. Notably, neonate rWGS-03 demonstrated the highest impact, as rWGS enabled the early identification of renal tubular dysgenesis before symptom onset. This study demonstrates the feasibility of rWGS for critically ill neonates with suspected genetic disorders admitted to the NICU. As the first implementation of neonatologist-driven rWGS in Korea, it highlights the meaningful clinical benefits of timely and accurate diagnosis. Our findings underscore its clinical value and support the integration of rWGS into routine clinical care, as well as the development of future studies within public healthcare systems. - Source: PubMed
Publication date: 2026/05/15
Cho Hye-WonKim Jeong-MinPark Sung HyeonKim HyeseonShin Dong MunYu Ho-YeongYang MisunAhn So YoonSung Se InKim Bong-JoPark Mi-HyunJang Mi-AeChang Yun SilPark Hyun-Young - Arginine residues in antithrombin are essential for heparin binding and for the activation of this key anticoagulant serpin. Mutations affecting these residues may cause antithrombin deficiency, specifically Type II heparin-binding site (HBS) defects, and increase the risk of thrombosis. However, previous alanine-scanning mutagenesis and crystallographic studies have yielded conflicting results regarding the specific residues involved in heparin binding. Our aim was to characterize natural variants affecting arginine residues in antithrombin. Genetic, biochemical, and functional characterization of antithrombin was done in 663 unrelated patients, most with antithrombin deficiency. Recombinant expression of the variants was performed in two different N-glycosylation backgrounds. We identified nine missense variants affecting eight arginine residues located at or near the HBS, four of them novel. Two variants, the most distant from the HBS (p.R291H and p.R177C), were found to be benign. In contrast, p.R45W, p.R56C, p.R79C, p.R79H, and p.R161Q caused Type II HBS deficiency. p.R78Q, causing a mild Type II HBS defect, was identified in a patient with compound heterozygosity with other HBS mutations. N-glycosylation at N167 modulated heparin affinity and influenced the clinical severity of mutations affecting arginine residues involved in heparin interaction. Finally, p.R89S caused Type I deficiency by creating a novel N-glycosylation motif, leading to hyperglycosylation and intracellular retention. Natural variants provide valuable insights into the functional contribution of arginine residues to antithrombin-heparin interaction. Our findings highlight the biochemical, functional, and clinical heterogeneity of these mutations and underscore the importance of comprehensive characterization for accurate diagnosis and prognosis in affected individuals. - Source: PubMed
Publication date: 2026/04/22
Cifuentes-Riquelme Rosade la Morena-Barrio María EugeniaMiñano AntoniaGarrido-Rodríguez PedroVelasco FranciscoRojo-Carrillo Juan JoséLópez-Correas PalomaZaragoza-Huesca DavidPadilla JoséLozano María LuisaBravo-Pérez CarlosCorral Javier - Diagnosis of antithrombin deficiency (ATD), the most severe inherited thrombophilia, commonly relies on functional assays despite their uncertain sensitivity. Moreover, routine characterization of ATD remains uncommon due to limited supporting clinical data. - Source: PubMed
Publication date: 2026/04/20
Rojnik TamaraŠket RobertSlapnik BarbaraVrhovšek BlažMavri AlenkaDebeljak MarušaBožič Mijovski Mojca - Recurrent pregnancy loss (RPL) remains a devastating outcome for many women, with up to 40–60% of cases classified as unexplained despite extensive clinical workup. During pregnancy, extracellular vesicles (EVs) from the placenta enters into maternal circulation and plays a vital role in completion of a successful pregnancy. Profiling of EVs cargo proteins offers a promising avenue for the pathophysiology of RPL, with the potential to revolutionize diagnosis, prognosis, and treatment strategies. Blood samples were collected from 5 pregnant women with history of RPL and 5 gestational aged-matched healthy pregnant controls. EVs were extracted from plasma and characterized for their size, morphology, number and presence of surface markers. Further, liquid chromatography-tandem mass spectrometry (LC–MS/MS) analysis of EV protein was performed to identify differentially expressed proteins (DEPs). In total 508 proteins with unique peptides were identified. Among these 330 proteins were differentially expressed between patients and controls, out of which 94 were significantly expressed ( < 0.05). Based on the expression pattern, 25 proteins were upregulated (log2FC > 1, < 0.05) and 69 were downregulated. GO enrichment and KEGG pathway enrichment indicated involvement of pathways such as innate immune response, neutrophil degranulation, complement cascade regulation and intrinsic pathway of fibrin clot formation. Protein-protein interaction analysis identified 10 hub proteins (,,,,,,,,,) potentially implicated in RPL pathophysiology. While preliminary, this study provides molecular insights into EV-associated proteins in RPL and highlights potential biomarkers for future validation. - Source: PubMed
Publication date: 2026/04/09
Bhardwaj ChitraSrivastava PriyankaBhadoriya Ravi Pratap SinghRohilla MinakshiKaur AnupriyaPanigrahi InushaChopra Seema - Inherited blood disorders (IBDs) are a major health concern in the Kingdom of Saudi Arabia (KSA), largely due to the high prevalence of consanguineous marriages. - Source: PubMed
Publication date: 2026/04/01
Younis Nancy SAlkabsh Rahma MNasser Alqahtani Shahad MAljuail HajerAlhashim Manar ABokhamsin Shahad AAlbaqshi Layla JAlqadhib Salsabil FAldandan Jumanah AAlshakhs Zahra AAltaweel Maryam HMohamed Maged E