Ask about this productRelated genes to: SPRY2 Blocking Peptide
- Gene:
- SPRY2 NIH gene
- Name:
- sprouty RTK signaling antagonist 2
- Previous symbol:
- -
- Synonyms:
- hSPRY2
- Chromosome:
- 13q31.1
- Locus Type:
- gene with protein product
- Date approved:
- 1998-11-09
- Date modifiied:
- 2015-08-26
Related products to: SPRY2 Blocking Peptide
Related articles to: SPRY2 Blocking Peptide
- To screen for differentially expressed genes in retinoblastoma (RB) gene chips using GEO2R and validate them clinically. - Source: PubMed
Publication date: 2026/05/18
Liu Chun-YiLuo RuiLiu HanXie Ruo-YiChai YongXu Yu - Developing reliable biomarkers capable of differentiating Parkinson's disease from other neurological conditions is crucial for both patient care and research. In this study, we leveraged recent advances in high-throughput proteomic technology and machine learning to develop candidate biomarkers for Parkinson's disease. Using the Olink Explore 3072 assay, we obtained plasma proteomic profiles from 698 study participants, comprising Parkinson's disease cases (n = 149), neurologically healthy controls (n = 230), and participants with other neurological conditions (n = 319). The study cohort was split into Training Set (n = 560) and Test Set (n = 138). We conducted differential protein abundance analysis and pathway enrichment analysis, and subsequently applied the Boruta algorithm to identify differentially abundant proteins that are predictive of Parkinson's disease. To create a diagnostic biomarker panel, we trained a stacking ensemble machine learning (ML) model on the Training Set (n = 118 Parkinson's patients, n = 184 healthy controls, and n = 258 individuals with other neurological disorders) using eleven proteins (APOH, ARG1, CCN1, CXCL1, CXCL8, DDC, GRAP2, IL1RAP, OSM, PRL, and SPRY2) as model features. We used the Shapley Additive Explanations (SHAP) framework and network analysis to evaluate predictive importance and biological relevance of each protein in the ML model. The model demonstrated high accuracy in the held-out Test Set (n = 138) and three external cohorts-the UK Biobank (n = 43,969), the Parkinson's Disease Biomarkers Program (n = 138), and the Parkinson's Progression Markers Initiative (n = 385), with areas under the receiver operating characteristic curve of 0.939, 0.789, 0.909, 0.816, respectively. Additionally, network and pathway analyses helped interpret the model, revealing activity related to inflammatory mediators, ErbB signaling, T-cell receptor signaling, and lipid metabolism. Our findings highlight the potential of plasma protein biomarkers to improve Parkinson's disease diagnosis and deepen biological understanding of this complex neurological disorder. Our model demonstrates high specificity and reliability across multiple independent cohorts, indicating the significant potential of proteomics-based biomarkers and the clinical utility of ML-supported diagnosis in Parkinson's disease care. The model also helps to elucidate potential novel risk factors and pathways associated with Parkinson's disease. - Source: PubMed
Publication date: 2026/04/22
Adewale BoluwatifeChia RuthMoaddel RuinLandeck NatalieRasheed MemoonaAlba CamilleReho PaoloVasta RosarioCalvo AndreaMoglia CristinaCanosa AntonioManera UmbertoSnyder AllisonLee Yi-JungGrassano MaurizioGao ChristineZhu MinBrunetti MauraCasale FedericoArvind Kumar Dawson Ted MRosenthal Liana SHall Anna JPantelyat Alexander YDing JinhuiGibbs J RaphaelEgan Josephine MCandia JuliánTanaka ToshikoFerrucci LuigiChiò AdrianoNarendra Derek PKwan Justin YEhrlich Debra JDalgard Clifton LTraynor Bryan JScholz Sonja W - Sprouty2 (Spry2) acts as a modulator of the MAPK-ERK signaling pathway by exerting both positive and negative regulation in a highly context- and cell type-specific manner. While its role in controlling the migration of non-immune cells in growth factor-dependent contexts is well established and continuously expanding, its function as a modulator of immune cell responses has only recently begun to emerge. Spry2 appears to critically and differentially influence B- and T-cell responses, consistent with its cell type-specific nature. However, its role in dendritic cells (DCs) remains unexplored. DCs serve as the cellular link between innate and adaptive immunity, and hence, DCs rely on their ability to navigate through different tissues and migrate to distinct target locations to initiate and coordinate effective immune responses. In the present study, we show that Spry2 expression is regulated during bone marrow-derived (BM)DC maturation and established a CD11c-specific Spry2 knockout mouse model to analyze the and immune functions of Spry2-deficient DCs. Unexpectedly, we found that its complete absence does not alter essential DC immune functions. Spry2-deficient DCs display intact DC differentiation and , efficient CCR7-driven migration and effective lymph node homing . Furthermore, we demonstrate that Spry2-deficient DCs retain an unaltered ability to stimulate CD8 T-cell activation and proliferation, ultimately resulting in normal CD8 T-cell effector differentiation during acute viral infection. Collectively, our findings shed light on the function of Spry2 in DCs, thereby extending and reinforcing current knowledge of its diverse immunomodulatory functions. - Source: PubMed
Publication date: 2026/03/18
Anslinger NadineSamson Guerric P BPurvanov VladimirBasler MichaelLegler Daniel F - The role of the adapter protein Sprouty2 (Spry2) in lipopolysaccharide (LPS)/TLR4-mediated signaling is unknown. In the present study we show that Spry2 positively regulates NF-κB signaling by sequestering the negative regulator PP2Ac in LPS-stimulated bone marrow derived macrophages (BMDM). Spry2 deficient BMDM display impaired LPS/TLR4-induced cytokine production and NF-κB activation. This impaired cytokine production in Spry2 deficient macrophages is not due to defects in receptor proximal signaling events or dysregulated MAPK activation. Mechanistically, we show that upon LPS stimulation, Spry2 is serine phosphorylated and associated with the phosphatase PP2Ac. The PP2Ac sequestration by Spry2 heightens NF-κB activation, enhances nuclear translocation of p65 and augments cytokine production. On the other hand, macrophages from Spry2 deficient mice display enhanced interaction between PP2Ac and p65, increased p65 dephosphorylation, reduced nuclear translocation of p65 and curtailed cytokine secretion. Pretreatment of Spry2 deficient macrophages with PP2Ac inhibitors restores p65 nuclear translocation and cytokine secretion in response to LPS. Collectively, our study suggest a novel role for Spry2 in modulation of NF-κB activation in response to LPS. - Source: PubMed
Sripada AnandVarma RangatiSirohi KapilSahu AnitaVerma MukeshAlam Rafeul - Artificial sweeteners (ASs) are widely used sugar substitutes, but chronic exposure is linked to male infertility. We integrated computational prediction, network analysis, and wet-lab validation to explore mechanisms. - Source: PubMed
Publication date: 2026/02/17
Meng ChunyangLi YuqiZhou TaoZhu XinyaoLi YifanTan XiaojunXiang Nana