Ask about this productRelated genes to: Nptx1 Blocking Peptide
- Gene:
- NPTX1 NIH gene
- Name:
- neuronal pentraxin 1
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 17q25.3
- Locus Type:
- gene with protein product
- Date approved:
- 1995-05-12
- Date modifiied:
- 2019-04-16
Related products to: Nptx1 Blocking Peptide
Related articles to: Nptx1 Blocking Peptide
- The synaptic transmission of memory engrams is important for their roles in memory storage and retrieval, and can be regulated by multiple neuronal adhesion molecules. This study focuses on the roles of neuronal pentraxin (NPTX) family members (NPTX1 and NPTX2), which are biomarkers for cognitive decline, in the synaptic transmission of Fos-(F-RAM) and Npas4-(N-RAM)-dependent engrams formed during contextual fear conditioning in the dentate gyrus. - Source: PubMed
Publication date: 2026/05/13
Mao FeihuangYang YangJiang ZhuyingLe QiuminJin Tao - Fluid protein studies in cerebrospinal fluid (CSF) and plasma have provided important insights into neurodegenerative dementias; however, there is a limited investigation of sex-related differences and cross-biofluid relationships. In Alzheimer's disease (AD), Lewy body dementia (LBD), and frontotemporal dementia (FTD), large-scale, sex-stratified analyses of paired CSF and plasma samples remain scarce. Using the multiplex and ultrasensitive capabilities of NULISAseq™ technology, this study aims to characterize sex- and disease-specific proteomic alterations associated with Central Nervous System (CNS) pathology to explore underlying mechanisms. - Source: PubMed
Publication date: 2026/05/08
Comas-Albertí AinaLladó AlbertEsteller-Gauxax DianaBorrego-Écija SergiFalgàs NeusDakterzada FaridaPérez-Millan AgnèsPuey RogerCollet-Romà TàniaGuillén NúriaMassons MiquelTort-Merino AdriàAugé Josep MariaFernandez-Villullas GuadalupeBosch BeaRuiz-García RaquelNaranjo LauraBalasa MirceaPiñol-Ripoll GerardAntonell AnnaSánchez-Valle Raquel - Parkinson's disease (PD) is characterized by progressive degeneration of nigrostriatal dopamine neurons and synucleinopathy, which is the accumulation of aggregated α-synuclein (α-syn). Increasing evidence implicates α-syn-associated neuroinflammation as a contributor to PD pathogenesis; however, immune mechanisms linking synucleinopathy to neurodegeneration remain incompletely defined. Activation of the complement cascade occurs in PD and other neurodegenerative disorders, but most studies report complement activation after overt neurodegeneration, making it difficult to conclude if complement is directly activated by pathological α-syn or secondarily following neurodegeneration. We used the rat α-syn preformed fibril (PFF) mode, complement assays and human postmortem PD tissue to test whether pathological α-syn directly activates complement prior to overt neurodegeneration. The α-syn PFF model exhibits a protracted pathological time course and distinct temporal separation between peak α-syn aggregation and nigrostriatal degeneration; thus we quantified complement expression, activation, and regulation during the aggregation phase. Synucleinopathy induced complement activation prior to nigrostriatal degeneration, including upregulation of components of both the classical ( ) and alternative ( ) pathways, the anaphylatoxin ( ) and phagocytic ( ) complement receptors, and activation of complement C3. During early synucleinopathy, microglia upregulated C3 which significantly correlated with synucleinopathy burden across several brain regions, including the substantia nigra pars compacta (SNc) and cortex. Concurrently, complement regulatory proteins, including CD55, CD59, neuronal pentraxin-1 (Nptx1), and the neuronal pentraxin receptor were downregulated in the synucleinopathy-affected SNc. Importantly, increased levels of C1q and iC3b along with downregulation of CD55 and NPTX1 were also observed in human postmortem PD SNc, supporting the translational relevance of our findings. Mechanistically, we demonstrate that aggregated, but not monomeric, α-syn directly binds C1q and activates the complement cascade in a C1q-dpendent manner. These data provide the first evidence that synucleinopathy triggers complement activation and dysregulation prior to neurodegeneration. - Source: PubMed
Publication date: 2026/04/30
Khan HinaGifford MaryKordbacheh ArashBury AsherPanoushek SpencerCole-Strauss AllysonKemp Christopher JLuk Kelvin CSteece-Collier KathyKuhn Nathan CKanaan Nicholas MSortwell Caryl EPatterson Joseph RBenskey Matthew J - ARL15, coding for a small GTPase, was identified as a non-HLA susceptibility gene in rheumatoid arthritis (RA) through a GWAS in a North Indian cohort, with serum adiponectin and ARL15 levels higher in RA patients with the associated genotype. This study aimed to delineate the functional role of ARL15 in RA pathobiology. - Source: PubMed
Kashyap SujitPandey Anuj KumarKumar ParitoshKanjilal MaumitaKumar UmaThelma B K - Osteoarthritis (OA) is a degenerative joint disease with high global prevalence, and YKL-40 is an important factor related to the pathological process of OA. Increased levels of YKL-40 exert a protective influence against TNF-α-induced apoptosis in chondrocytes, thereby enhancing chondrocyte survival and activation, while counteracting TNF-α-driven expression of specific inflammatory mediators such as S100A8/A9.This study aims to evaluate the role and molecular mechanism of YKL-40 on chondrocytes in OA and provide a potential therapeutic avenue requiring further validation. A meta-analysis compared serum YKL-40 and TNF-α levels between OA patients and healthy controls. In vitro experiments examined the effects of YKL-40 on TNF-α-induced OA chondrocytes, assessing proliferation, differentiation, apoptosis, and inflammatory pathways. Meta-analysis revealed significantly elevated serum levels of YKL-40 and TNF-α in osteoarthritis (OA) patients compared to healthy controls. In vitro, TNF-α (10 ng/mL) induced extracellular matrix (ECM) degradation in chondrocytes, significantly reducing glycosaminoglycan (GAG) and type II collagen content. This degradation was effectively rescued by YKL-40 (100 ng/mL). RNA sequencing identified differentially expressed genes in TNF-α-treated chondrocytes, enriched in pathways like IL-17 and NF-κB signaling. YKL-40 treatment reversed the expression of key genes altered by TNF-α. Crucially, these differentially expressed genes (including S100A8/A9, ISG15, CDSN, BAAT, PTPN4, NPTX1, SMARCA1) were validated in independent OA cartilage and synovium GEO datasets. Protein-protein interaction (PPI) networks highlighted central genes within treatment groups. Western blotting confirmed YKL-40 counteracted TNF-α-induced NF-κB pathway activation (reduced p65 and IκBα phosphorylation) and modulated key targets (S100A8/A9, ASB7, ZFPM2), consistent with qRT-PCR data. YKL-40 is a promising biomarker and therapeutic target for OA. Its interplay with TNF-α provides a molecular basis for novel therapies targeting chondrocyte dysfunction, guiding future translational research. - Source: PubMed
Publication date: 2026/04/27
Li ZhuozhengSun XueXie YongfangHong ZexinDou ZeminYan ShichaoZhang YulongQin HeLiu DanFeng TingtingWang Guohui