Ask about this productRelated genes to: VEGF165 protein
- Gene:
- NRP1 NIH gene
- Name:
- neuropilin 1
- Previous symbol:
- -
- Synonyms:
- NRP, VEGF165R, CD304
- Chromosome:
- 10p11.22
- Locus Type:
- gene with protein product
- Date approved:
- 1998-12-23
- Date modifiied:
- 2016-10-05
- Gene:
- NRP2 NIH gene
- Name:
- neuropilin 2
- Previous symbol:
- -
- Synonyms:
- VEGF165R2
- Chromosome:
- 2q33.3
- Locus Type:
- gene with protein product
- Date approved:
- 1998-12-23
- Date modifiied:
- 2015-09-01
Related products to: VEGF165 protein
Related articles to: VEGF165 protein
- H2A.Z is a conserved histone variant that plays essential roles in various DNA-templated processes. Although both histone H3 acetylation and H2A.Z enrichment levels are important epigenetic marks that regulate gene expression, their functional interplay remains incompletely understood. This study integrates genetic, molecular, and genomic approaches to investigate how GCN5 - a conserved histone acetyltransferase - couples H3 acetylation with H2A.Z dynamics in Arabidopsis, and how this interplay shapes gene expression and plant development. We found that the increase in H2A.Z levels observed in the nrp1-1 nrp2-2 double mutant (defective in NAP1-RELATED PROTEIN 1 and 2) suppresses the morphological and molecular phenotypes of gcn5-7. Conversely, H2A.Z-depleted mutants aggravate these phenotypes of gcn5-7/c1. Notably, the reduction in H3 acetylation caused by GCN5 loss promotes the decrease in H2A.Z level, and this requires the function of NRPs. The integrated analysis of ChIP-Seq and RNA-Seq data revealed that the differential gene expression in the GCN5 deletion mutant is correlated with H2A.Z distribution and enrichment levels. Moreover, H2A.Z overaccumulation at genes in the nrp1-1 nrp2-2 mutant promotes increased H3 acetylation in a GCN5-dependent manner. In conclusion, our findings support a model in which GCN5-mediated H3 acetylation shapes H2A.Z occupancy, linking chromatin dynamics to precise gene expression control and proper plant development. - Source: PubMed
Publication date: 2026/04/26
Su YingpeiHu QinLiu MinQian WeiyeXu ChaoXu JunjieAusin IsraelWang Yafei - Cardiometabolic and inflammatory pathways may play important roles in Alzheimer's disease (AD) pathogenesis contributing to neuronal dysfunction even in the absence of cognitive symptoms. Our objective is to characterize proteomic signatures of these pathways in AD. - Source: PubMed
Publication date: 2026/03/25
Hajjar Ihab MNeal ReemSingh NamrataYang ZhiyiObideen MalikShah Amil MDammer Eric B - The guinea pig with guinea pig cytomegalovirus (GPCMV) is the only small-animal model for congenital cytomegalovirus, a leading cause of cognitive impairment and hearing loss in newborns. GPCMV encodes human cytomegalovirus (HCMV) homologues of viral entry glycoprotein complexes, which are neutralizing-antibody vaccine targets. As with HCMV, GPCMV has two pathways of cell entry (direct and endocytic). Specific viral gH/gL-based complexes are necessary for receptor interaction and cell entry: gH/gL/gO trimer (direct) and pentamer complex (PC) (endocytic). Both pathways also require gB as the fusogenic protein. Direct GPCMV cell entry requires platelet-derived growth factor receptor alpha (PDGFRA), but an endocytic PC receptor remains unknown. We hypothesized that cellular knockout of direct and endocytic receptors would completely block infection, which cannot be achieved by gB-based antibodies. Candidate receptors including neuropilin proteins (NRP1, NRP2) and CD147 present on all established guinea pig cell lines were selected based on importance as common virus receptors or in fetal development. Results demonstrated that NRP2 interacted with PC, unlike NRP1 or CD147, in immunoprecipitation assays and eliminated NRP1/NRP2 heterodimer receptor interaction. The viral trimer only interacted with PDGFRA. Double knockout of PDGFRA/NRP2 completely blocked GPCMV infection. In contrast, the CD147/PDGFRA double knockout had limited GPCMV inhibition, and the single knockout of CD147 had no impact. Knockout of the various receptors had no effect on control HSV-1 infection. Ectopic expression of guinea pig cell receptors restored GPCMV infection but not human NRP2/PDGFRA, indicating a basis for the species-specific barrier for GPCMV and HCMV infection. Overall, results increase the translational relevance of GPCMV for the development of CMV intervention strategies. - Source: PubMed
Qin YushuChoi K YeonEl-Hamdi NadiaMcGregor Alistair - Deep skin wounds demand tightly coordinated communication across diverse tissue systems, yet knowledge of the molecular logic governing organ-scale injury response remains incomplete. Existing wound atlases profile fragments of this process, capturing limited tissue groups and healing phases, obscuring how whole organs synchronize repair. Here, we present the Organ-Scale Wound Healing Atlas (OWHA), a 4D multimodal omnibus that integrates snRNA-seq, scRNA-seq, CITE-seq and high-definition spatial transcriptomics to reconstruct the complete spatial and temporal choreography of mammalian wound healing at single cell resolution. OWHA profiles over 725,000 murine single-cell and spatial transcriptomes encompassing the entire wound healing process from early to late healing phases across the vast skin microanatomical tissue niches. This omnibus overcomes long-standing technical limitations, enabling robust resolution of adipocytes, Schwann cells, fragile epithelial intermediates, and over 100 precisely annotated cell states, including populations missed in prior wound databases. This revealed that wound repair proceeds through sharp transcriptional and cellular inflection points driven by Central Orchestrator populations that coordinate healing via synchronized transcriptional activation and direct cross-tissue signaling. Key among these is a keratinocyte subpopulation (Basal IV), detectable only through snRNA-seq but entirely missed by conventional wound atlasing. After injury, Basal IV cells deviate from canonical differentiation programs and adopt a neurovasculogenic signaling state during the proliferation phase, forming a transient spatially privileged regulatory hub at the wound edge. This epithelial-anchored niche spatially aligns Basal IV keratinocytes with proliferative endothelial cells, Pericytes, and Repair Schwann Cells, synchronizing re-epithelialization, angiogenesis, and neurite guidance. Mechanistically, this is orchestrated by a conserved Sema3C-Nrp1/Nrp2 axis that coordinates epithelial-vascular-neuronal crosstalk at the wound site. Cross-species integration confirms that the Basal IV/SEMA3C axis is conserved in human skin, yet undetected by conventional scRNA-seq human atlases due to dissociation-induced artifacts - underscoring the critical need for multimodal atlasing to accurately capture organ-scale physiology. Notably, the Basal IV/SEMA3C circuitry is selectively disrupted in human diabetic wounds, but topical Sema3C treatments restores peri-wound angiogenic sprouting and accelerates re-epithelialization of diabetic ulcers . OWHA establishes the first 4D, organ-scale molecular blueprint of mammalian wound healing, creating a foundational platform for decoding systems-level principles of repair and regeneration for tissue wounds. - Source: PubMed
Publication date: 2026/01/16
Cheong Jonathan ChinVan Deursen SimonAmador DreytonHiner ShannonWoappi Yvon - Coronavirus disease 2019 (COVID-19) is associated with hyperinflammation, endothelialitis, hypoxemia, and hypercoagulation, contributing to thrombosis in acute severe and long COVID. While ACE2 is the primary severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) receptor, its low expression in certain infected cell types suggests alternative co-receptors. Neuropilins (NRP1 and NRP2), widely expressed, have been proposed as co-factors for viral entry. We analyzed NRP1 and NRP2 expression in autopsy tissues from heart, lung, and hematolymphoid organs using immunohistochemistry ( = 20) and compared findings with public single-cell RNA sequencing (scRNAseq) data. Selected cases were further examined by spatial multiplex immunofluorescence (CODEX). binding of NRP1/NRP2 to SARS-CoV-2 spike fragments S1 and S1' was assessed by immunofluorescence microscopy. NRP1 was abundantly expressed in myocardial capillary endothelial cells (ECs) and macrophages in the heart and lung; NRP2 was found in alveolar macrophages and mast cells. scRNAseq re-analysis confirmed these patterns. , NRP1 exclusively bound S1, while NRP2 bound both S1 and S1'. SARS-CoV-2 RNA was detected in neuropilin-positive, /-negative vascular EC and mast cells. The detection of SARS-CoV-2 RNA in neuropilin-positive but /-negative cell clusters supports that neuropilins are involved in systemic viral dissemination. NRP1 on vascular EC may contribute to angiogenesis, vascular damage, and microangiopathy, while NRP2 represents a potential immunomodulatory target to regulate macrophage activity, resolve inflammation, and potentially prevent the progression of pulmonary fibrosis and limit excessive mast cell activation in long COVID.IMPORTANCEThe well-known severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) receptor, angiotensin-converting enzyme 2 (ACE2), exhibits low expression in key cell types implicated in coronavirus disease 2019 (COVID-19) pathology, such as endothelial cells and B cells, macrophages, and mast cells. In contrast, neuropilins, identified as co-receptors for SARS-CoV-2, are abundantly expressed in these cells under physiological conditions and may be involved in virus-host interactions. This study presents a detailed analysis of Neuropilin 1 (NRP1) and Neuropilin 2 (NRP2) expression in fatal COVID-19 cases using immunohistochemistry and spatial multiplex immunofluorescence phenotyping, complemented by single cell RNA sequencing. Additionally, it demonstrates differential binding affinities of NRP1 and NRP2 to SARS-CoV-2 spike protein fragments S1 and S1' , suggesting distinct roles for these neuropilins in viral recognition. This study highlights the impact of the unique furin cleavage site in SARS-CoV-2, which may contribute to increased pathogenicity through its interaction with NRP1. - Source: PubMed
Publication date: 2025/10/29
Dette AMoers FMayr TStillfried S VBernhardt MFörster SWerlein CAckermann MMuders M HKristiansen GBoor PGütgemann I