Ask about this productRelated genes to: SERPINA10 antibody
- Gene:
- SERPINA10 NIH gene
- Name:
- serpin family A member 10
- Previous symbol:
- -
- Synonyms:
- PZI, ZPI
- Chromosome:
- 14q32.13
- Locus Type:
- gene with protein product
- Date approved:
- 2001-06-27
- Date modifiied:
- 2016-04-06
Related products to: SERPINA10 antibody
Related articles to: SERPINA10 antibody
- The susceptibility to periprosthetic joint infection (PJI) likely has a genetic component. However, the responsible genes are unknown. We performed whole-exome sequencing on four siblings, three of whom had undergone total knee arthroplasty (TKA), of whom two suffered from recurrent PJI. Evaluation of rare genetic variants found in the affected siblings (TKA with PJI) yielded a list of 22 candidate genes. Searching each of these in the NCBI database yielded two with a plausible role in susceptibility to PJI: JAGN1 and SERPINA10. - Source: PubMed
Publication date: 2026/07/18
Metz Allan KKelly MackenzieJurynec Michael JCertain Laura KBlackburn Brenna ERainey Joshua PGililland Jeremy M - Acute myeloid leukemia (AML) is a heterogeneous hematologic malignancy with complex genetic underpinnings. Understanding the causal relationships between genetic factors and AML risk is crucial for developing targeted therapeutic strategies. - Source: PubMed
Publication date: 2026/05/30
Xia TianWen RuitingWu GuocaiHong YunguangLuo Dasi - One of the biggest challenges in plasma proteomics is to reduce the dynamic range of plasma proteins to capture the expression of low-abundance proteins. Although abundant protein depletion and proximity extension assay are widely used for human samples, the application to animal species in non-clinical assessment remains limited. Here, we evaluated the Mag-Net and ENRICH-iST methods using 20 μl of plasma from both healthy and type 2 diabetes model rats. By combining with the optimized LC-MS method, Mag-Net identified more proteins than ENRICH-iST with high precision, although both methods identified over 5000 proteins. Using integrative proteomics and analytical approaches, including extracellular vesicle (EV) database comparison, Gene Ontology analysis, Simple Western, nanoparticle tracking analysis, and contamination assessments, we demonstrated in rat plasma that Mag-Net preferentially enriches EV proteins, whereas ENRICH-iST more evenly captures low-abundance proteins, including EV proteins. Regardless of the protein enrichment method employed, more than half of the tissue-specific proteins were classified as being specific to either the liver or the brain tissues. Whereas, several liver-specific proteins involved in protein-protein interactions, including Proz/Serpina10 and Ambp/Itih1/Itih2, were identified as exhibiting over a ten-fold increase in mean quantification values in the Mag-Net method compared to ENRICH-iST, suggesting enhanced enrichment of protein-protein interaction network. Ingenuity Pathway Analysis identified 219 downregulated and 80 upregulated proteins in the Mag-Net method dataset (fold change ≥ 1.5, p ≤ 0.05), and 68 downregulated and 43 upregulated proteins in the ENRICH-iST method dataset (fold change ≥ 1.5, p ≤ 0.2). Some significantly downregulated pathways, such as elastic fiber formation, were uniquely identified by the Mag-Net method. This approach was shown to be a powerful tool for investigating deregulated proteins and pathways. Potential applications include biomarker discovery and the assessment of drug efficacy and safety during development. - Source: PubMed
Publication date: 2026/05/20
Takahashi RyoProdinger FlorianMatsui Akiko - Children with complicated severe malnutrition (CSM) face high mortality after hospital discharge, yet the underlying mechanisms remain poorly understood. While early post-discharge mortality (< 2 months) has been linked to a sepsis-like inflammatory profile measured at discharge, it is unclear whether this relationship persists (later mortality; 2-6 months post-discharge). This study investigated whether immune, inflammatory, and endothelial dysfunction at 2 months post-discharge are associated with later mortality in children recovering from CSM. - Source: PubMed
Publication date: 2026/01/22
Kamau BrendaMudibo Evans OWechessa CecilliaOmer ElishaGichuki Bonface MMburu David MMwalekwa LauraTimbwa MollineThitiri JohnstoneNgari Moses MBerkley James ANjunge James M - : Fabry disease (FD) is an X-linked lysosomal storage disorder caused by mutations, leading to deficient α-galactosidase A (α-Gal A) activity and progressive glycosphingolipid accumulation. While α-Gal A activity is the diagnostic gold standard, its sensitivity is reduced in late-onset or heterozygous patients. Conventional biomarkers such as lyso-Gb3 provide only limited insight into disease progression and therapeutic response. Exosomes, as stable carriers of disease-specific proteins, may offer complementary biomarkers for early detection and longitudinal monitoring. : Twenty-one pediatric FD patients with confirmed GLA mutations were enrolled. Clinical, enzymatic, renal, and cardiac parameters were assessed. Plasma-derived exosomes were characterized by transmission electron microscopy and proteomic profiling. Differentially expressed proteins were identified using mass spectrometry, analyzed using GO/KEGG enrichment, and validated using RT-PCR, ELISA, and immunofluorescence in patient samples and mice. : Male patients showed markedly reduced α-Gal A activity and elevated lyso-Gb3 compared with females. Although overt renal and cardiac dysfunction was uncommon, several patients exhibited early abnormalities such as proteinuria, an elevated LVMI, or increased cTnI levels. Proteomic analysis identified 2553 proteins, of which 188 were differentially expressed. Fibrosis- and inflammation-related proteins, including THBS1 and CFHR5, were upregulated, while protective factors such as APM1, SERPINA10, and CAB39 were downregulated. IGFBP3 was also elevated and closely linked to tissue remodeling. Enriched pathways were involved in PPAR/AMPK signaling, lipid metabolism, and complement activation. : Exosomal proteomic profiling revealed early molecular signatures of cardiorenal involvement in pediatric FD. Key proteins such as THBS1, CFHR5, IGFBP3, APM1, and CAB39 show strong potential as biomarkers for risk stratification, disease monitoring, and therapeutic evaluation. - Source: PubMed
Publication date: 2025/10/23
Lu ZhihongXia YuWang BingyingJiang PingpingMao Jianhua