CD148 / PTPRJ antibody Host Chicken
- Known as:
- CD148 / PTPRJ (anti-) Host Chicken
- Catalog number:
- 'GTX82146
- Product Quantity:
- 50
- Category:
- -
- Supplier:
- ACR
- Gene target:
- CD148 / PTPRJ antibody Host Chicken
Related genes to: CD148 / PTPRJ antibody Host Chicken
- Gene:
- PTPRJ NIH gene
- Name:
- protein tyrosine phosphatase receptor type J
- Previous symbol:
- -
- Synonyms:
- DEP1, HPTPeta, CD148
- Chromosome:
- 11p11.2
- Locus Type:
- gene with protein product
- Date approved:
- 1994-09-14
- Date modifiied:
- 2019-02-14
Related products to: CD148 / PTPRJ antibody Host Chicken
Related articles to: CD148 / PTPRJ antibody Host Chicken
- CD148 is the primary receptor-type protein tyrosine phosphatase (PTP) regulating platelet activation, and its inhibition has been proposed as a novel anti-thrombotic strategy with potentially lower bleeding risk than current therapies. However, selective and potent inhibitors of CD148 are currently lacking. AKB-9778 (razuprotafib), a potent inhibitor of the closely related vascular endothelial-PTP (VE-PTP), has also been reported to inhibit CD148. This study investigated the effect of AKB-9778 on in vitro whole-blood thrombogenicity, examined the molecular basis of its interaction with the CD148 catalytic domain using molecular docking, and assessed inhibitor selectivity with an in vitro phosphatase assay. In a total-thrombus formation analysis system (T-TAS), AKB-9778 partially inhibited thrombus formation, reducing AUC by 28%, without significantly affecting occlusion start time or occlusion time. The inhibitor did not alter collagen-stimulated CD62P platelet surface expression or PAC-1 binding to the activated integrin αIIbβ3. Molecular docking using CB-Dock predicted a binding configuration in which the phenylsulfamic acid group of AKB-9778 is orientated towards the catalytic cysteine, with additional conformations reflecting ligand flexibility. Site-directed mutagenesis of Tyr1071, Gln1283, His1206, and Asn1073 to alanine reduced the inhibitory effect in phosphatase assays, supporting interaction with these residues. Notably, the IC of AKB-9778 against CD148 was approximately 300-fold higher than previously reported values, consistent with the wide variability across studies. Despite this reduced potency, these findings support the concept of CD148 inhibition as a potential anti-thrombotic strategy and suggest that AKB-9778 may serve as a useful prototype for developing more selective and efficacious CD148 inhibitors. - Source: PubMed
El Badaoui LinaJurcevic StipoSenis Yotis ABarr Alastair J - Protein tyrosine phosphatase receptor J (PTPRJ) restrains cell proliferation and migration by dephosphorylating receptor tyrosine kinases (RTKs) including the epidermal growth factor receptor (EGFR). PTPRJ is a purported tumor suppressor, and alterations to its expression and/or function are associated with colorectal, breast, lung, and other cancers. While there is interest in controlling PTPRJ-regulated phenotypes, efforts are limited by the complexity of PTPRJ-mediated signaling. PTPRJ dephosphorylates multiple RTKs, and the degree to which PTPRJ control of signaling and phenotypes depends on local cellular RTK activation profiles is unknown. To probe the context dependence of PTPRJ signaling regulation, we collected signaling measurements across 16 pathway nodes at two time points in a panel of HSC3 carcinoma cells engineered with different PTPRJ expression profiles. Cells were treated with three different RTK ligands, and paired phenotype measurements (viability, wound healing, xCELLigence cell index) were made. Partial least squares regression models were developed to predict relationships between PTPRJ-regulated signaling pathways and cell phenotypes. The model effectively separated contributions to variance arising from the PTPRJ expression background and growth factor context. In testing model predictions, we demonstrated that PTPRJ suppressed MET-induced cell cell proliferation via regulation of a HER3/AKT signaling axis that stabilized PTPRJ expression through an unanticipated feedback mechanism. We also found that PTPRJ regulated HSC3 cell migration via JNK signaling that was preferentially activated by MET. Our results identify new regulatory nodes through which PTPRJ influences cancer cell phenotypes and demonstrates that these processes preferentially occur in the context of distinct RTK activation states. - Source: PubMed
Publication date: 2026/05/04
Hart Will SKnight Katie MRizzo SophieLee Sung HyunFetter RachelThevenin DamienLazzara Matthew J - The liver has a unique capacity for self-renewal, maintaining a proper liver-to-bodyweight ratio, which is essential for sustaining homeostasis. Regenerative process in the liver involves intricate communication between various cell types such as hepatocytes, hepatic stellate cells, endothelial cells, and inflammatory cells. Although the role of endothelial cells in liver regeneration has been extensively studied, detailed knowledge regarding specific endothelial cell-derived factors that promote the regeneration of liver endothelial cells (LECs) remains limited. This study aimed to identify the regenerative capacity of endothelial progenitor cells (EPCs) after acute liver injury. - Source: PubMed
Publication date: 2026/03/28
Lee Jong-MinHa Yoon-SuLee Seung-JunKim Hyun-YiAdpaikar Anish AshokKim Eun-JungOtsu KeishiChe XiangguoHan Dai HoonHer YoungChoi Je-YongKim Seung-JinJung Han-Sung - This study aimed to prioritize candidate transcriptomic mediators associated with human atherosclerosis progression by integrating transformer-based deep learning with classical bioinformatics and experimental validation. Gene expression profiles from dataset GSE100927 (69 plaques, 35 controls) were normalized and analyzed for differential expression using the limma package (FDR < 0.01). A TabTransformer model employing multi-head self-attention was trained (80/20 split, 10-fold cross-validation) to predict disease status, and SHapley Additive exPlanations (SHAP) analysis quantified gene-level contributions. Network topology was examined using STRING and Cytoscape to identify hub genes through betweenness centrality, while pathway enrichment was assessed via GO and KEGG analyses. Among 638 differentially expressed genes (402 upregulated, 236 downregulated), the TabTransformer achieved a mean AUC of 0.964, surpassing the LASSO baseline by 3.8%. The top-ranked genes, TYROBP, TNF, PTPRJ, DHRS9, and COL1A1, were primarily involved in leukocyte activation, NF-κB signaling, and smooth muscle dysfunction. Experimental assays in oxidized LDL-treated human umbilical vein endothelial cells confirmed significant upregulation of TYROBP (6.3-fold) and TNF (4.8-fold), validating computational predictions. These findings support an immunoinflammatory axis linked to the suppression of smooth muscle identity in atherosclerosis, and highlight TYROBP and TNF as mechanistically plausible candidate biomarkers and potential therapeutic targets. - Source: PubMed
Yan DongdongLi WenqiangXing ErkunWang PeiZhang Zheng - Receptor protein tyrosine phosphatases (RPTPs) are key regulators of cell signaling. However, their study and therapeutic targeting have been limited by the lack of known natural ligands or selective agonists, as well as an incomplete understanding of their structure-function relationships. Nonetheless, receptor homodimerization has been shown to suppress RPTP catalytic activity by restricting substrate access, offering a promising strategy for examining and modulating their function. Our previous work on PTPRJ, a member of the RPTP family, showed that its transmembrane domain regulates homodimerization, thereby controlling access to receptor tyrosine kinase (RTK) substrates and their phosphorylation levels. We also developed peptides that disrupt this dimerization, thereby inhibiting RTK phosphorylation and reducing cancer cell migration. These peptides were then engineered for selective, pH-sensitive insertion into the acidic tumor microenvironment to enhance efficacy while limiting off-target effects. Yet how broadly PTPRJ activation reshapes the phosphotyrosine landscape and whether those changes yield coherent cellular phenotypes remains unclear. In this study, we employed tyrosine phosphoproteomics, immunoblotting, immunofluorescence, and functional assays to assess the global impact of our lead peptide candidate, Hybrid 7, in A549 lung cancer cells that endogenously express PTPRJ. We find that Hybrid 7 decreases EGFR phosphorylation and selectively reduces phosphorylation across additional RTKs and motility adaptors, producing strong inhibition of EGF-driven migration and reduced proliferation. Hybrid 7 also elevates reactive oxygen species and DNA damage, and enforces CDK1-dependent G2/M arrest, indicating a primarily cytostatic, checkpoint-mediated response. These findings highlight the potential of RPTP-targeting peptides as valuable tools for dissecting RPTP function and as possible therapeutic agents capable of modulating key oncogenic pathways and inhibiting cancer progression. - Source: PubMed
Publication date: 2025/11/17
Rizzo SophieHart William SFetter Rachel LSong BokaiWhite Forest MLazzara Matthew JThévenin Damien