PTPRS Antibody
- Known as:
- PTPRS Antibody
- Catalog number:
- XW-7828
- Product Quantity:
- 0.05 mg
- Category:
- -
- Supplier:
- Prosci
- Gene target:
- PTPRS Antibody
Related genes to: PTPRS Antibody
- Gene:
- PTPRS NIH gene
- Name:
- protein tyrosine phosphatase receptor type S
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 19p13.3
- Locus Type:
- gene with protein product
- Date approved:
- 1995-04-27
- Date modifiied:
- 2019-02-14
Related products to: PTPRS Antibody
Related articles to: PTPRS Antibody
- Many studies have linked socioeconomic status (SES) and cardiovascular outcomes, yet the biologic mechanisms mediating these associations are only partially understood. The objective of this study was to identify molecular mediators of the association of low SES with coronary heart disease (CHD) and stroke. - Source: PubMed
Publication date: 2026/03/13
Odden Michelle CLiu XiaojuanShah Amil MYang YiminLamberson VictoriaBrody Jennifer ASitlani Colleen MHuber MattKalani RizwanShojaie AliRaffield Laura MGlover LáShauntáPalta PriyaKucharska-Newton Anna MPsaty Bruce MFloyd James S - Myocardial infarction (MI) and subsequent heart failure are frequently accompanied by chronic kidney disease, further impairing outcomes and complicating treatment. To better understand heart-kidney crosstalk, we used RNA sequencing data to infer interorgan signalling after experimentally induced MI in mice, focusing on secreted biomolecules and interorgan cross talk that may drive cardiorenal syndrome (CRS). To assess acute and chronic effects, we examined kidneys at 5d and 28d post-MI, evaluating changes in renal gene expression and fibrosis. During the acute phase 5d post-MI, several genes inferred to target kidney receptors were highly upregulated in the cardiac infarct zone, with Postn and Spp1 being the most probable ligands. However, only minor changes in gene expression were detected in the kidney 5d post-MI. At 28d post-MI, renal fibrosis and the number of differentially expressed genes (DEGs) in the kidney increased. Gene ontology enrichment suggested metabolic adaptions as part of a long-term response. Based on upregulated DEGs in kidney 28d post-MI, we suggest two kidney-to-heart interactions: Slitrk6-Ptprs and Gdf15-Tgfbr2. In vitro, GDF-15 treatment of human cardiac fibroblasts induced pro-fibrotic gene expression, mirroring in vivo changes in the heart. Our data suggest that MI in mice elicits minimal acute response in kidney but triggers chronic transcriptional and pro-fibrotic changes in kidney, potentially driven by altered renal metabolism. The inference of interorgan signalling molecules such as GDF-15 points towards candidate mediators of CRS and provides a basis for future mechanistic and clinical studies. - Source: PubMed
Publication date: 2025/12/05
Wolf HannaKupsch SvenjaHaacke Virginia KBacmeister LucasWeber SusanneHilgendorf IngoKeller TillDechend RalfHuber Tobias BWestermann DirkLindner Diana - Neoantigen-targeted immunotherapies hold promise for cancer treatment, but current personalized approaches are time-consuming and costly. Here, we identify neoantigens encoded by and that are shared across murine mismatch repair-deficient colorectal and breast tumors and unexpectedly conserved in human colorectal, endometrial, gastric, and prostate cancers. These neoantigens elicit spontaneous, organ-spanning CD8+ T cell-mediated memory responses that are enhanced by immune checkpoint blockade. Vaccination with mRNA/lipid nanoparticles encoding these conserved neoantigens suppresses tumor growth across prophylactic and therapeutic models, including checkpoint-resistant orthotopic tumors. Tumor rejection is accompanied by antigen spreading, abscopal effects, and infiltration by clonally diverse T cells, dendritic cells, and MHC I/II+ macrophages producing CXCL9/10, CCL5/8, and TNF. Tumor cells also show activation of innate and adaptive pathways, including MHC and ISGs overexpression. Our results uncover a conserved anti-tumor immune mechanism and support the development of off-the-shelf neoantigen vaccines across tissues and species. - Source: PubMed
Publication date: 2025/09/29
Mestrallet GuillaumeWard Ross WBrown MatthewBoumelha JesseRentzeperis FrederikaVaninov NatalieSaffern MiriamOlumuyide EzekielSuri PrernaBalan SreekumarVelazquez LeandraAnanthanarayanan AparnaChen ZhihongLucas Aimee LMerad MiriamBozkus Cansu CimenVabret NicolasSamstein Robert MBhardwaj Nina - Protein-tyrosine phosphatase receptor-type D (PTPRD) is an adhesion-coupled phosphatase that translates extracellular binding codes into intracellular phosphotyrosine signaling from embryogenesis through adulthood. Alternative inclusion of the Ig-domain mini-exons meA and meB tailors the ectodomain surface, thereby dictating high-affinity engagement with IL1RAPL1, IL1RAP, Slitrks, LRFN4/5 (SALM3/5), neuroligin-3, and other postsynaptic partners. Intracellularly, the catalytically active D1 domain and scaffold-like D2 module, anchored to liprin-α, coordinate presynaptic vesicle release, postsynaptic receptor composition, and synaptic plasticity. Beyond synapses, PTPRD restrains embryonic neurogenesis, promotes STAT3-dependent gliogenesis, accelerates oligodendrocyte myelination, and guides Sema3a/Fyn-mediated axon and dendrite patterning. In the adult brain it serves as the high-affinity hypothalamic and cerebellar receptor for asprosin, thereby coupling systemic energy and hydration states to feeding and drinking behavior. Human genetic studies and mouse models link these molecular activities to a spectrum of conditions-including restless legs syndrome, addiction, Alzheimer's disease, ADHD, OCD, autism spectrum disorder, and metabolic syndrome. Because PTPRD functions are pathway-specific and shaped by mini-exon usage or redundancy with other family members (PTPRS/PTPRF), domain- or ligand-selective interventions represent plausible therapeutic strategies. Elucidating its full ligand repertoire, substrate landscape, and structural basis for allosteric regulation will be critical for converting this versatile receptor from a mechanistic curiosity into a tractable target for neurodevelopmental, neuropsychiatric, and metabolic disorders. - Source: PubMed
Kim SeoyeongShin Jae JinKang MuwonYi YunhoKim Eunjoon - High throughput proteomics has enabled hypothesis free biomarker discovery. However, differences in sample sizes, biological fluid, and quantification technologies have limited replication and validation of the results, and studies on the cross-platform variability are lacking. Here, we present the first orthogonal validation across three platforms in Parkinson's disease (PD) to understand the technical and biological challenges of proteomic studies. - Source: PubMed
Publication date: 2025/09/28
Kumar RavindraBeric AleksandraWestern DanielYang ZiningLin WenjingTimsina JigyashaCruchaga CarlosIbanez Laura