Ask about this productRelated genes to: PDGFRB antibody
- Gene:
- PDGFRB NIH gene
- Name:
- platelet derived growth factor receptor beta
- Previous symbol:
- PDGFR
- Synonyms:
- JTK12, CD140b, PDGFR1
- Chromosome:
- 5q32
- Locus Type:
- gene with protein product
- Date approved:
- 2001-06-22
- Date modifiied:
- 2016-10-05
Related products to: PDGFRB antibody
Related articles to: PDGFRB antibody
- Platelet-Derived Growth Factor Receptor Beta (PDGFR-β), a key marker of cerebrovascular pericytes, plays a crucial role in regulating pericyte function and maintaining the stability of the blood-brain barrier (BBB). Recent studies suggest that abnormalities in the PDGFR-β signaling pathway may be closely associated with the onset and progression of neurodegenerative diseases. However, the causal relationship and specific mechanisms by which PDGFR-β gene deficiency directly leads to systemic pathological alterations in the hippocampal microenvironment, subsequently causing impaired neurogenesis and cellular senescence, remain unclear. - Source: PubMed
Publication date: 2026/08/18
Chen HaichaoZhang LeZhu XiaolingGu ChengGao Fulin - Despite decades of investigation, effective therapies for medial arterial calcification in chronic kidney disease remain lacking. Emerging therapeutic targets increasingly extend beyond systemic drivers of calcification and now seek to address direct vascular cellular mechanisms and the calcium-phosphate mineralization itself. In this issue, Öztürk et al. describe platelet-derived growth factor receptor β activation as a potent mediator of chronic kidney disease-induced vascular smooth muscle cell osteogenic differentiation and calcification, supporting vascular cell targeting as an emerging therapeutic axis in chronic kidney disease-associated medial arterial calcification. - Source: PubMed
Turner Mandy EAikawa Elena - Fibrotic scarring acutely corrals inflammation but chronically impedes axon regeneration via dense border structures after spinal cord injury (SCI). Although the origin and heterogeneity of fibroblasts have been extensively studied, effective strategies to prevent fibrotic scarring, especially the formation of its border structure, remain elusive. Here, we identified a distinct fibroblast subpopulation with markedly upregulated tight junction protein 1 (ZO-1) expression, which contributes to the formation of fibrotic scar borders after SCI. While ZO-1 has been conventionally considered restricted to epithelial/endothelial cells, our data may indicate a novel role in the formation of fibrotic scar border by platelet-derived growth factor receptor beta (PDGFRβ)-positive fibroblasts. Genetic ablation of Tjp1 (encoding ZO-1) in fibroblasts disrupted the fibrotic scar border, allowing serotonergic and tyrosine hydroxylase axons to grow into the lesion core after SCI. Disruption of the fibrotic scar border induced by ZO-1 knockout did not exacerbate inflammatory spread or damage residual neurons after SCI. Furthermore, PDGFB/PDGFRβ pathway activation induced ZO-1 expression and scar border formation in the intact spinal cord, whereas its inhibition suppressed ZO-1 upregulation and disrupted the scar border after SCI. Remarkably, combined targeting of PDGFRβ (using SU16f) and ZO-1 function (via LAT-A) synergistically promoted axonal growth across the lesion. Our findings identify ZO-1 as a critical orchestrator of the fibrotic scar border and reveal a combined therapeutic approach for enhancing axon regeneration after SCI. - Source: PubMed
Publication date: 2026/08/14
Li ZiyuYu ShuishengWang XuYu XiaoyangTao DaobaoMa YongqingXu JiaqiWu ZhonghanMa ZhidaTian DashengDing XinZheng MeigeCheng LiLi YiJing Juehua - Not available. - Source: PubMed
Publication date: 2026/08/13
Huang MorrisShopsowitz KevinBahmanyar MohammadHamadeh ZeidMerkeley HayleyStubbins RyanLai Chi KienMcGinnis Eric - The transmembrane protein E5 from bovine papillomavirus is the shortest naturally occurring oncoprotein. As a dimer, it activates the platelet-derived growth factor receptor β (PDGFRβ) in a ligand-independent manner by specific helix-helix interactions within the lipid bilayer. For both proteins, we determined the detailed orientations of their transmembrane helices in aligned membrane samples. Solid-state N-NMR was used to study either protein segment alone, as well as in the heterocomplex. Remarkably, the assembly of E5 with PDGFRβ led to structural rearrangements of both partners. Binding of E5 triggers a rotation of the PDGFRβ helices around their axes. At the same time, the E5 helices rotate in the membrane to expose Gln17 as well as Asp33, allowing their respective interaction with Thr513 and Lys499 on PDGFRβ. Based on these distinct membrane orientations, we present structural models of the heteromeric E5-PDGFRβ complex, and a mechanism for oncogenic receptor activation. - Source: PubMed
Publication date: 2026/08/17
Otteni SebastianWindisch DirkZiegler ColinGrage Stephan LWadhwani ParveshAfonin SergiiKara NerminSchneider ViolettaMast ThiloWalther Torsten HUlrich Anne S