PLCG2 (phospho-Tyr753) Antibody
- Known as:
- PLCG2 (phosphorilated-Tyr753) Antibody
- Catalog number:
- abx000245
- Product Quantity:
- EUR
- Category:
- -
- Supplier:
- Abbexa
- Gene target:
- PLCG2 (phospho-Tyr753) Antibody
Related genes to: PLCG2 (phospho-Tyr753) Antibody
- Gene:
- PLCG2 NIH gene
- Name:
- phospholipase C gamma 2
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 16q24.1
- Locus Type:
- gene with protein product
- Date approved:
- 1994-05-16
- Date modifiied:
- 2019-04-23
Related products to: PLCG2 (phospho-Tyr753) Antibody
Related articles to: PLCG2 (phospho-Tyr753) Antibody
- Understanding sex-dependent differences in disease risk, manifestation, and treatment response is essential for precision medicine. While funding agencies now mandate consideration of Sex as a Biological Variable (SABV), existing bioinformatics tools lack systematic approaches to characterize sex-related molecular mechanisms. Current practices frequently treat sex as a confounding variable, which may obscure important biological differences such as sex-specific alterations, sex-dimorphic changes (opposite effects between sexes), and sex-modulated changes (different effect magnitudes). We present XYomics, an open-source R package for systematic analysis of sex-dependent alterations in biomedical omics data. The software identifies sex-specific, sex-dimorphic, and sex-modulated changes at both individual feature and systems levels. XYomics implements dual analytical modes: sex-disease interaction term modeling for adequately powered datasets and sex-stratified analysis with robust non-significance filtering for smaller sample sizes. Using single-cell RNA sequencing data from Alzheimer's disease patients, we demonstrate how XYomics identifies sex-dimorphic genes largely undetected by standard sex-averaged analyses. By integrating statistical categorization with pathway enrichment and network analysis using a curated hormone signaling interactome, the software facilitates discovery of sex-specific biomarkers and disease mechanisms frequently obscured in sex-aggregated analyses. - Source: PubMed
Le Bars SophieSoudy MohamedGlaab Enrico - Phospholipase C gamma-2 (PLCγ2) catalyzes the hydrolysis of the membrane phosphatidylinositol-4,5-bisphosphate (PIP) to form diacylglycerol (DAG) and inositol trisphosphate (IP), feeding into diverse downstream signaling pathways. polymorphisms have been associated with reduced and/or increased risk of Alzheimer's disease (AD) and related dementias, longevity, autoinflammation, and immune disorders. In the brain, PLCγ2 is expressed in microglia, and other neuroimmune and vascular interface populations, yet its role in brain homeostasis remains incompletely defined. - Source: PubMed
Publication date: 2026/07/14
Gutierrez-Kuri EduardoGarcia-Rogers Juliet Lynn MariePerez JaidSmith SabrinaKenwood Matthew RArchuleta Kahealani SXiao YangmingCampos GabrielaBarannikov SavannahWang HuPardo SammyRomsdahl Trevor BMiller HenryStowe Ann MWilliam RussellGoldberg MarkHan XianlinBieniek Kevin FWeintraub Susan TGriffith Ann VHopp Sarah CPalavicini Juan Pablo - ObjectiveAutoimmune and autoinflammatory diseases (AIDs) represent a heterogeneous group of immune-mediated disorders characterized by dysregulated innate and adaptive immune responses. This study aimed to investigate the immunogenetic background of AIDS by assessing the distribution of genetic variants identified by a targeted next-generation sequencing (NGS) panel and elucidating genotype-phenotype correlations in the context of systemic immune dysregulation.Materials and methodsA targeted NGS panel encompassing 19 genes involved in immune regulation, inflammatory signaling pathways, and immune tolerance was utilized to evaluate a cohort of 110 patients presenting with clinical manifestations suggestive of autoinflammatory disease. Clinical severity was quantitatively assessed using longitudinal serum C-reactive protein (CRP) and erythrocyte sedimentation rate (ESR) measurements across acute and baseline periods. Detected variants were classified according to the American College of Medical Genetics and Genomics (ACMG) guidelines and correlated with patient clinical phenotypes and established immunogenetic literature.ResultsA total of 55 genetic variants were identified across 41 patients. Alterations predominantly clustered in MEFV (38.2%), HFE (29.1%), and SLC29A3 (21.8%), followed by NOD2, MVK, CARD14, IL10RB, and PLCG2 (1.8% each). According to ACMG criteria, 61.8% of the variants were pathogenic, 25.5% were likely pathogenic, and 12.7% were VUS. Genotype-phenotype correlation analyses successfully linked rare variants (including PLCG2, IL10RB, and CARD14) and oligogenic combinations to specific laboratory profiles. These findings revealed unexpected penetrance, variable expressivity, and distinct biomarker disassociations, most notably highlighted by isolated ESR elevations reaching 91 mm/h.ConclusionOur findings underscore the immunogenetic heterogeneity of autoinflammatory diseases and substantiate the diagnostic value of NGS-based profiling in deciphering complex genotype-phenotype associations. The integration of specific quantitative biomarkers and downstream mechanisms highlights how non-HLA regulatory variants reshape the chronic inflammatory immune microenvironment, lowering the threshold for inflammasome activation and systemic autoimmunity. - Source: PubMed
Publication date: 2026/07/06
Geniş Esra ÇolakÇam Fethi Sırrı - Mutations in the gene, which encodes the lysosomal glucocerebrosidase enzyme GCase, cause the lysosomal storage disorder Gaucher disease and represent the most common genetic risk factor for Parkinson's disease (PD). These mutations deplete lysosomal GCase activity and cause accumulation of GCase substrate, glucosylceramide, and its pathological metabolite, glucosylsphingosine. Impaired GCase activity then drives immune and neuronal dysfunction in Gaucher disease and promotes pathogenic aggregation of α-Synuclein in PD. As such, boosting the lysosomal activity of GCase is a therapeutic strategy to ameliorate substrate accumulation and prevent associated neurotoxicity. To identify the regulators of GCase activity in lysosomes, we conducted a genome-wide screen in primary mouse macrophages using a fluorescent enzyme activity reporter. By validating the screen hits in cellular biochemical and profiling assays, we identified pathways that promote or inhibit lysosomal GCase activity. Our screen identified PLCG2 as a regulator of lysosomal GCase activity. Mechanistically, PLCG2 depletion accumulates Golgi-associated phosphatidylinositols, promoting the transport of mutant GCase into lysosomes while reducing its Golgi-associated pool. Functionally, PLCG2 depletion boosts the activity of lysosomal mutant GCase, the cellular flux of glucosylceramide, and the clearance of pathogenic GCase substrates. In summary, our screen has uncovered the regulators of GCase abundance and trafficking at a whole-genome scale and identified potential pathways for future therapeutic interventions in Gaucher and Parkinson's to boost the activity of this enzyme in lysosomes. - Source: PubMed
Publication date: 2026/07/01
Lawrence JessicaKulkarni Vineet VinayTan Chan LekCallow MarinellaJuste YvesSangaraju DewakarCosta MikeBingol Baris - The Alzheimer's disease protective P522R PLCG2 coding variant (rs72824905) is downstream of TREM2, but how it confers disease protection is poorly understood. Using a Plcg2-R522 knock-in mouse and Plcg2-P522 control on both wildtype and Alzheimer's disease-like App amyloidosis mouse backgrounds, aged mice were assayed for amyloid load, microglial activity, and synaptic integrity. In the absence of Alzheimer's disease-like pathology, the R522 variant increased microglial coverage and was associated with reduced ramification complexity, fewer terminal points, and elevated lysosomal CD68 expression. On the App background, total amyloid burden was unaffected, but expression of the R522 variant led to increased plaque compaction compared to the P522 common variant. The protective R522 variant was also associated with: enhanced microglial engagement with less compact amyloid plaques; reduced microglial localisation around highly compacted plaques; protection from amyloid-induced synapse loss; and decreased engulfment of synaptic material by microglia. Our data indicate a significant direct PLCγ2 role in controlling microglial-plaque interactions and synaptic protection downstream of amyloid deposition, prioritizing it as a therapeutic target, potentially as an adjunct to other approaches, such as those targeting amyloid. - Source: PubMed
Bevan Ryan JMaguire EmilyMackinnon EilishSalis ElisaPhillips ThomasSimonazzi ElenaVassileva MarietaAllen Nicholas DWilliams JulieTaylor Philip R