Anti_Human, mab Furin Source Mouse
- Known as:
- Anti_Human, mab Furin Source Mouse
- Catalog number:
- 101-M423
- Product Quantity:
- 100 µg
- Category:
- -
- Supplier:
- Reliatech
- Gene target:
- Anti_Human mab Furin Source Mouse
Related genes to: Anti_Human, mab Furin Source Mouse
- Gene:
- FURIN NIH gene
- Name:
- furin, paired basic amino acid cleaving enzyme
- Previous symbol:
- PCSK3, FUR, PACE
- Synonyms:
- SPC1
- Chromosome:
- 15q26.1
- Locus Type:
- gene with protein product
- Date approved:
- 1991-08-08
- Date modifiied:
- 2016-02-22
Related products to: Anti_Human, mab Furin Source Mouse
Related articles to: Anti_Human, mab Furin Source Mouse
- The epithelial sodium channel (ENaC) plays a key role in salt and water homeostasis in tetrapod vertebrates. There are four ENaC subunits (α, β, γ and δ) which form heterotrimeric αβγ- or δβγ-ENaC assemblies. ENaC activity is tightly coupled to proteolytic processing of ENaC subunits, but this effect is specific to ENaC subunit assembly and mechanistically not completely understood. Guinea pig αβγ- or δβγ-ENaCs were heterologously expressed in oocytes and their control by extracellular proteases was investigated using protein biochemistry, two-electrode voltage-clamp and patch-clamp electrophysiology. Guinea pig αβγ-ENaC activity was tightly coupled to cleavage of its α- and γ-subunits by the endoprotease furin and extracellular chymotrypsin or trypsin. By contrast, δβγ-ENaC activity was not affected by proteases, despite cleavage of its γ-subunit by chymotrypsin. Experiments using a β-ENaC substitution, which locks ENaC in an open state after exposure to the sulfhydryl-reagent [2-(trimethylammonium)ethyl] methanethiosulfonate (MTSET), demonstrated that guinea pig δβγ-ENaCs are almost fully open when expressed in oocytes. On-cell single-channel patch-clamp recordings confirmed that the open probability of guinea pig δβγ-ENaC is nearly 90%. These data indicate that guinea pig δβγ-ENaC is locked in an open state and thereby uncoupled from channel control by proteases. - Source: PubMed
Publication date: 2026/04/25
Lawong Rene YufenyuyEtang Etang CollinsMay FabianVorrat PhilippRauh OliverAlthaus Mike - Fibroblast growth factor 23 (FGF23) is a phosphate-regulating hormone produced by osteocytes. In iron deficiency anemia (IDA) and in chronic kidney disease (CKD), FGF23 is also produced by erythroid cells. Recent studies have suggested that rising circulating FGF23 is negatively associated with erythropoiesis in IDA and CKD. However, the distinct contributions of bone- and erythroid-produced FGF23 to anemia in IDA remain unclear. Using the conditional deletion of Fgf23 in osteocytes (Fgf23Dmp1-cKO) and in erythroid cells (Fgf23HbB-cKO) in mice fed a control (Ctr) or an iron deficient (ID) diet, we first determined that in ID, osteocytes and erythroid cells are distinct sources of circulating intact FGF23 (iFGF23) and FGF23 cleaved peptides, respectively. We further show that erythroid-specific deletion of Fgf23 corrected anemia in ID mice, and overexpression induced anemia in Ctr mice unlike osteocyte-specific deletion or overexpression of Fgf23. Importantly, erythroid-specific deletion of Furin (FurinHbB-cKO), the enzyme responsible for FGF23 cleavage, led to increased production of iFGF23 from erythroid cells and aggravated ID-induced anemia. iFGF23 also dose-dependently blocked the differentiation of erythroid progenitors in culture triggering mitochondrial dysfunction leading to impaired erythropoiesis. These effects were fully suppressed by co-treatment with an FGFR1 inhibitor. Finally, erythroid-specific deletion of Fgf23 in an animal model of progressive CKD prevented the development of anemia of CKD. In aggregate, our results show that erythroid-expressed FGF23 is a negative regulator of erythropoiesis that contributes to anemia via direct paracrine FGFR1 activation in erythroid precursors. - Source: PubMed
Publication date: 2026/04/21
Courbon GuillaumeThomas Jane JJ Duque EduardoKentrup DominikSpindler JadeahSemancheck WilliamTracey EmilyVaughan Douglas EChang WenhanCreemers John W MJi PengIsakova TamaraMartin AlineDavid Valentin - Placenta enriched 1 (PLAC1) is a conserved X chromosome-linked gene expressed in the mammalian placenta. We investigated the biology of PLAC1 in the rat and human placenta. Plac1 transcripts were expressed in the junctional zone of the rat placenta and in intrauterine invasive trophoblast cells. Genome-edited Plac1 mutant animals exhibited placentomegaly. Enlarged placentas were characterized by an expanded junctional zone, an irregular junctional zone-labyrinth zone boundary, a deficiency of intrauterine invasive trophoblast cells, and a late gestation stage uterine-placental interface infiltrated with natural killer cells. PLAC1 facilitated rat trophoblast cell differentiation. In contrast, PLAC1 showed minimal contributions to the regulation of the human invasive/extravillous trophoblast cell lineage, but instead PLAC1 expression and actions were linked to syncytiotrophoblast differentiation. Furthermore, PLAC1 impacts on cellular function were linked to furin, paired basic amino acid cleaving enzyme (FURIN), in rat and human trophoblast cells. Thus, PLAC1 is critically involved in hemochorial placentation; however, the responsive trophoblast cell lineages and its contributions to placentation are fundamentally distinct in the rat versus human. - Source: PubMed
Publication date: 2026/04/20
Moreno-Irusta AyelenUrosevic JovanaIqbal KhursheedSeetharam Arun SNteeba JacksonScott Regan LKuna MarijaMuto MasanagaKozai KeisukeCelic AndjelkaOkae HiroakiArima TakahiroJohnson David KTuteja GeetuSoares Michael J - Chikungunya virus (CHIKV) infection can induce acute kidney injury (AKI) and may be fatal in severe cases, yet effective therapeutic strategies remain unclear. This study integrated computational analysis (network pharmacology and molecular docking) with experiments to evaluate the protective potential of oxymatrine against CHIKV-induced AKI and to explore its underlying mechanisms. Network pharmacology analysis identified 605 overlapping targets between CHIKV- and AKI-related genes, with core targets including TNF, AKT1, IL6, IL1B, and TP53, which were primarily enriched in the PI3K/AKT signaling pathway. RT-qPCR analysis and molecular docking further indicated that oxymatrine may interact with 18 targets, such as BAX, BCL2, and TLR4, thereby modulating CHIKV-associated PI3K/AKT signaling. experiments showed that oxymatrine at concentrations of 250-2,000 μM significantly increased the viability of HEK293T cells infected with CHIKV at a MOI of 0.01 for 24 h, with an average increase of approximately 25.8%. At these concentrations, oxymatrine reduced the expression of the CHIKV entry factor and regulated the PI3K/AKT, NF-κB, and TNF signaling pathways, which may contribute to the inhibition of viral replication. Further analysis revealed that CHIKV-induced AKI involved 75 ferroptosis-related targets and was closely associated with inflammatory responses. Oxymatrine may attenuate these effects through the regulation of targets such as SIRT3, AR, and FURIN. Consistently, ELISA results demonstrated that 1,000 μM oxymatrine significantly decreased the levels of IL-1β, TNF-α, and IL-6 in HEK293T cells infected with CHIKV. In conclusion, these findings suggest that oxymatrine may protect against CHIKV-induced AKI by limiting viral replication, modulating PI3K/AKT and NF-κB/TNF signaling pathways, suppressing inflammation, and regulating ferroptosis-related processes. - Source: PubMed
Publication date: 2026/04/02
Xin JiaLiangLi FangJunKang LuLuYang JieWang HaiTongWang WeiFeng ShengLiao XinFeiLi WenJieZhang He - - Source: PubMed
Publication date: 2026/04/13
Ahmad Khan FMenzies RAshesh ABijker EBrode SCarter E JCasas E CCampbell JDenkinger CDeborggraeve SEvlampidou IFurin JFarhat MFarouk M M OGafar FGünther GGuglielmetti LIsaakidis PJouberton FKhambati NKhan P YKhan ULong RLaw SMatteelli AMalden DMotta IMurray MMasini TRich MRuslami RSepulcri CSunyoto TTunesi SWong E BZaffagnini A