Ask about this productRelated genes to: NECAB3 antibody
- Gene:
- NECAB3 NIH gene
- Name:
- N-terminal EF-hand calcium binding protein 3
- Previous symbol:
- SYTIP2, APBA2BP
- Synonyms:
- XB51, dJ63M2.4, NIP1, dJ63M2.5, EFCBP3
- Chromosome:
- 20q11.22
- Locus Type:
- gene with protein product
- Date approved:
- 2001-06-21
- Date modifiied:
- 2016-10-05
Related products to: NECAB3 antibody
Related articles to: NECAB3 antibody
- Air pollution exposure is increasingly recognized as a risk factor for chronic kidney disease (CKD), but the underlying mechanisms, especially the complex gene-environment interactions as reflected in genetic susceptibility, transcriptomic, and proteomic signatures, remain to be elucidated. - Source: PubMed
Publication date: 2026/05/09
Lu JianSun ShuaigangShang XinruDeng ZekaiWang ShunweiJiang ShiminLi Wenge - Chronic pancreatitis (CP) is characterized by inflammation, acinar cell death, fibrosis, and persistent pain. We investigated mesenchymal stem/stromal cell (MSC)-derived extracellular vesicles (EVs) for CP treatment. CP was modeled in male mice using bile duct TNBS infusion, and pancreatic tissues from CP patients were also analyzed. EVs from immortalized human MSCs overexpressing alpha-1 antitrypsin (iAAT-MSCs) were tested for their effects on ferroptosis, fibrosis, and pain. CP tissues showed reduced glutathione peroxidase 4 (GPx4) activity (p < 0.05) and iron accumulation, indicating ferroptosis. iMSC and iAAT-MSC-EVs alleviated CP symptoms by suppressing ferroptosis, restoring GPx4 activity, reducing MDA levels, and mitigating fibrosis markers (α-smooth muscle actin, transforming growth factor-β1, matrix metalloproteinase 2). EV treatment also alleviated pain by decreasing macrophage and mast cell infiltration into the pancreas and dorsal root ganglia while reducing pain-related gene expression (TRVP1, TacR1, Necab3). Additionally, iAAT-MSC-EVs were distinct in cytokine signaling, PI3K-Akt pathway activation, and upregulation of miRNAs like miR-9, miR-10a-5p, miR-92a, miR-200, miR-370, and miR-146a. These results suggest ferroptosis as a key mechanism in CP and highlight the therapeutic potential of iAAT-MSC-EVs in addressing ferroptosis, fibrosis, and pain, presenting a promising, cell-free therapeutic strategy for CP. - Source: PubMed
Publication date: 2025/03/22
Shoeibi SaraGou WenyuYeung TiffanyHelke KristiGreen EricaStrange CharlieWang Hongjun - Previous studies have shown cord-blood DNA methylation differences in newborns conceived using assisted reproductive technologies (ART) compared to those conceived naturally. However, whether these ART-related DNA methylation differences vary with children's sex is unknown. We hypothesize that the DNA methylation differences in cord blood between ART-conceived and naturally conceived newborns also varies by the sex of the child, with distinct patterns of differential methylation present in males and females. We investigated sex differences in cord-blood DNA methylation variation according to conception by ART using the Illumina MethylationEPIC platform, comparing 456 ART-conceived versus 507 naturally-conceived girls, and 503 ART-conceived and 473 naturally-conceived boys. We identified 37 differentially methylated CpGs according to ART-conception among girls, and 70 differentially methylated CpGs according to ART-conception among boys, when we used a 1% false discovery rate to account for multiple testing. Ten CpGs were differentially methylated according to conception by ART in both sexes. Among the genes that were associated with these CpGs, we found the BRCA1; NBR2 gene (two CpGs) was hypermethylated in girls while the APC2 (two CpGs) and NECAB3;ACTL10, (four CpGs) related to cellular signaling were hypomethylated in boys. These findings confirm the presence of sex-specific epigenetic differences, illustrating the nuanced impact of ART on the fetal epigenome. There is a need for further explorations into the implications for sex-specific developmental trajectories and health outcomes in ART-conceived children. - Source: PubMed
Publication date: 2024/10/02
Kristjansson DanaLee YunsungPage Christian MGjessing HåkonMagnus Maria CJugessur AstanandLyle RobertHåberg Siri E - Many calcium-binding proteins are expressed in a region-and cell-type specific manner in the mammalian hippocampus. Neuronal calcium-binding proteins (NECABs) are also expressed in hippocampal neurons, but few species have been investigated, with partly controversial findings. We here describe NECAB1, NECAB2 and NECAB3 as well as parvalbumin, calbindin, and calretinin in the European mole, and compare staining patterns of these proteins with those in mouse and other species. While subtle differences are present, NECAB staining in the European mole was generally similar to those in mouse. Common to European moles, mice, and other species we investigated, large hilar polymorphic cells, likely to represent mossy cells, were positive for all three NECABs. NECAB1 and 2 are suitable as markers for these cells along the entire septotemporal axis of the hippocampus. In the European mole, parvalbumin, calbindin and calretinin showed traits that have been described in other species before, albeit in a unique combination. In summary, we provide the first description of distribution of these proteins in the hippocampus of the European mole. This subterranean, insectivorous, and solitary living species belongs to the Order of Eulipotyphla. Despite many similarities with other subterranean species from the rodent order in terms of lifestyle, its hippocampus is cytoarchitecturally much more elaborated than in, e.g., mole-rats. It remains an open question if the hippocampal structure of the European mole reflects evolutionary constraints or ecology. Our descriptive study highlights the diversity in hippocampal cytoarchitecture even in small mammalian species. - Source: PubMed
Publication date: 2024/09/04
Maliković JovanaAmrein IrmgardVinciguerra LorenzoWolfer David PSlomianka Lutz - The N-terminal EF-hand calcium-binding proteins 1-3 (NECAB1-3) constitute a family of predominantly neuronal proteins characterized by the presence of at least one EF-hand calcium-binding domain and a functionally less well characterized C-terminal antibiotic biosynthesis monooxygenase domain. All three family members were initially discovered due to their interactions with other proteins. NECAB1 associates with synaptotagmin-1, a critical neuronal protein involved in membrane trafficking and synaptic vesicle exocytosis. NECAB2 interacts with predominantly striatal G-protein-coupled receptors, while NECAB3 partners with amyloid-β A4 precursor protein-binding family A members 2 and 3, key regulators of amyloid-β production. This demonstrates the capacity of the family for interactions with various classes of proteins. NECAB proteins exhibit distinct subcellular localizations: NECAB1 is found in the nucleus and cytosol, NECAB2 resides in endosomes and the plasma membrane, and NECAB3 is present in the endoplasmic reticulum and Golgi apparatus. The antibiotic biosynthesis monooxygenase domain, an evolutionarily ancient component, is akin to atypical heme oxygenases in prokaryotes but is not well-characterized in vertebrates. Prokaryotic antibiotic biosynthesis monooxygenase domains typically form dimers, suggesting that calcium-mediated conformational changes in NECAB proteins may induce antibiotic biosynthesis monooxygenase domain dimerization, potentially activating some enzymatic properties. However, the substrate for this enzymatic activity remains uncertain. Alternatively, calcium-mediated conformational changes might influence protein interactions or the subcellular localization of NECAB proteins by controlling the availability of protein-protein interaction domains situated between the EF hands and the antibiotic biosynthesis monooxygenase domain. This review summarizes what is known about genomic organization, tissue expression, intracellular localization, interaction partners, and the physiological and pathophysiological role of the NECAB family. - Source: PubMed
Publication date: 2024/06/26
Bueno DionesSchäfer Michael K EWang SudenaSchmeisser Michael JMethner Axel