Ask about this productRelated genes to: TIE1 antibody
- Gene:
- TIE1 NIH gene
- Name:
- tyrosine kinase with immunoglobulin like and EGF like domains 1
- Previous symbol:
- TIE
- Synonyms:
- JTK14
- Chromosome:
- 1p34.2
- Locus Type:
- gene with protein product
- Date approved:
- 1993-08-24
- Date modifiied:
- 2016-10-05
Related products to: TIE1 antibody
Related articles to: TIE1 antibody
- Despite the introduction of genome sequencing (GS) for rare disease diagnostics, a genetic cause is not identified in most patients. Here, we explored the potential of proteomics to improve the diagnostic yield in 424 patients with rare diseases from the 100,000 Genomes Project (100kGP) without a genetic diagnosis. Serum proteomic profiling was performed using the Olink Explore 1536 assay ( = 1463 proteins). For 13 patients without genetic diagnoses, detection of lower serum protein "outliers" (-score < -2) led to confirmed genetic diagnoses by resolving variants of uncertain significance or prioritizing genes for targeted GS reanalysis. For 23 additional patients without genetic diagnoses (64% of findings), we identified candidate gene-disease links and variants through convergent evidence from lower protein outliers and variants ranked through the variant prioritization tool Exomiser. For example, we identified a candidate heterozygous missense variant [Genome Aggregation Database (gnomAD) minor allele frequency = 0.006%] in () that was only present in a patient with lower TIE1 serum abundance (-score = -5.12) and their father, both of whom were affected by the same monogenic cardiac disorder, but in no other individuals from the 100kGP. Missense (52.5%) and splice region (27.5%) variants accounted for most diagnostic or candidate variants prioritized. This proof-of-principle study demonstrated that serum proteomics can support rare disease diagnosis and identify disease-causing genes in patients undiagnosed after GS, although successful implementation will likely depend on tissue specificity of protein expression, detectability in blood, proteomic platform coverage, and sensitivity. - Source: PubMed
Publication date: 2026/09/09
Carrasco-Zanini JuliaAndrade JorgePietzner MaikKousathanas AthanasiosJacobsen Julius O BLord JennyTelugu NarasimhaDiecke SebastianMülleder MichaelBierbaum DominikVestito LetiziaRobinson Peter NRalser MarkusBaralle DianaWareham Nicholas JElgar GregPotente MichaelBrown Matthew ACaulfield MarkSmedley DamianLangenberg Claudia - Leptin, an adipokine primarily secreted by adipose tissue, has been implicated in tumor progression by regulating angiogenesis. Leptin also plays a key role in tumor vascularization by promoting vasculogenic mimicry (VM). During tumor progression, leptin activates several signaling pathways, including the focal adhesion kinase (FAK) pathway. This study aimed to determine whether leptin promotes and regulates angiogenesis and VM through the FAK pathway. We used the chick chorioallantoic membrane (CAM) as a model to evaluate blood vessel formation and to induce tumors to assess angiogenic expression. Matrigel-based cell cultures were used to analyze the formation of tubular structures characteristic of VM. The expression of specific markers was then evaluated for each process. These models were employed with or without the inhibitor PF-573,228. Our results showed that leptin enhances the sprouting, branching, and vasodilation of blood vessels via FAK signaling by increasing the expression of vascular endothelial growth factor (VEGF) and N-cadherin in tumors derived from MCF-7 and MDA-MB-231 cells. Furthermore, leptin stimulation promoted tubular-type VM in MCF-7 cells and matrix-type VM in MDA-MB-231 cells; the former was dependent on FAK signaling. Lastly, leptin increased the levels of several proteins associated with angiogenesis and VM, including TIE-1, MMP-9, VE-cadherin, ANG-2, VEGF, and VEGFR1. In conclusion, leptin promotes tumor vascularization in breast cancer through angiogenesis and VM, in a manner dependent on FAK signaling. - Source: PubMed
Publication date: 2026/08/29
Herrera-Vargas Ana KJaime-Cruz RicardoRodríguez-Leviz AlejandraMendoza-Catalán Miguel AOlea-Flores MonserratVillavicencio-Guzmán LauraSalazar-García MarcelaPatiño-Morales Carlos CNavarro-Tito Napoleón - Fully autonomous apomixis with fertilization-independent embryo and endosperm development enables the production of clonal seeds to fix crop hybrid vigour. However, the mechanisms underlying autonomous endosperm development remain unclear. Here we show that TIE1 acts as a maternally expressed transcriptional repressor inhibiting autonomous endosperm. The disruption of four TIEs in tie1 tie2 tie3 tie4 (tieQ) mutants triggers the development of autonomous endosperm, recapitulating the phenotypes observed in fertilization-independent seeds (fis)-class mutants. TIE1 exhibits maternal genomic imprinting similar to MEDEA (MEA) that encodes a core component of the FIS-POLYCOMB REPRESSIVE COMPLEX 2 (PRC2). TIE1 recruits FIS-PRC2 to transcriptionally silence a subset of its target genes whose activation would otherwise trigger endosperm development in the absence of fertilization. Our findings reveal a maternally controlled brake mechanism that prevents autonomous endosperm development, providing both a molecular framework for understanding apomictic seed formation and a possible tool for engineering synthetic apomixis to fix heterosis in crops. - Source: PubMed
Publication date: 2026/07/28
Zhang ZeliangWang XinxueYuan RongrongLi YiyiPan YigeHe QingChen XuemeiQin Genji - Kinase inhibitors (KIs) are essential in targeted cancer therapy but frequently cause cardiotoxicity, limiting their clinical utility. A systematic resource to explore the underlying causal mechanisms is urgently needed. - Source: PubMed
Publication date: 2026/07/17
Wei JiaminLiu YinWu MiaoqingLi GuoyuanZheng XinyaoFu HuafengZhang JianLin Jijin - TIE-1 (TIE-1) is a metabolically versatile environmental bacterium that flourishes across gradients of iron, oxygen, and light. This versatility necessitates extensive regulatory control, exemplified by the aerobic-anaerobic metabolic shift controlled by the hierarchy of CRP/FNR-family regulators AadR and FixK. Many anaerobic metabolic pathways demand expression of iron cofactor-intensive proteins, and TIE-1 in particular can generate energy through phototrophic iron oxidation via the PioABC system. However, TIE-1 lacks canonical iron-sensing regulators: IscR, ancestral Fe(II)-sensing Fur, and Fe(II)-sensing RirA of , leaving it unclear how TIE-1 coordinates expression of these iron-requiring metabolisms with bioavailable iron levels. Here, we demonstrate that the AadR-FixK hierarchy plays a previously underappreciated role in iron regulation in TIE-1 by comparing growth and transcription in wild-type and regulatory mutants across wetland-inspired naturomimetic conditions. Δ and Δ showed defects in iron-dependent growth and Fe(II) oxidation, and the ΔΔ double mutant was synthetically lethal under anaerobiosis. The regulatory hierarchy of FixK and AadR influences expression of Fur-family regulators: the two paralogs were oppositely regulated in the presence of AadR, and absence of AadR perturbed iron-responsive expression of . Furthermore, the AadR regulon was significantly enriched for iron-related and iron-containing proteins. Despite initial predictions that AadR directly regulates , we found no conclusive evidence for direct AadR activity at the promoter, refining the search for regulators. Together, these findings establish AadR as a central integrator of oxygen and iron signals to coordinate iron-requiring anaerobic metabolism in TIE-1. - Source: PubMed
Publication date: 2026/06/29
Gallagher BrianRanaivoarisoa TahinaPrabhakar PremLi JingtaoRajkumar AnjaliGupta DineshKim JoshBose Arpita