Human PRL-2 (2-167) Active Enzyme
- Known as:
- Human PRL-2 (2-167) Active Enzyme
- Catalog number:
- x1658e
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Exalpha
- Gene target:
- Human PRL-2 (2-167) Active Enzyme
Related genes to: Human PRL-2 (2-167) Active Enzyme
- Gene:
- CHST5 NIH gene
- Name:
- carbohydrate sulfotransferase 5
- Previous symbol:
- -
- Synonyms:
- I-GLCNAC-6-ST, FLJ22167
- Chromosome:
- 16q23.1
- Locus Type:
- gene with protein product
- Date approved:
- 1999-12-07
- Date modifiied:
- 2018-05-14
- Gene:
- CTBP1-DT NIH gene
- Name:
- CTBP1 divergent transcript
- Previous symbol:
- C4orf42, CTBP1-AS1, CTBP1-AS2
- Synonyms:
- MGC21675
- Chromosome:
- 4p16.3
- Locus Type:
- RNA, long non-coding
- Date approved:
- 2007-12-19
- Date modifiied:
- 2018-03-22
- Gene:
- FBXO30 NIH gene
- Name:
- F-box protein 30
- Previous symbol:
- -
- Synonyms:
- MGC21674, Fbx30
- Chromosome:
- 6q24.3
- Locus Type:
- gene with protein product
- Date approved:
- 2001-05-15
- Date modifiied:
- 2016-10-05
- Gene:
- FPR3 NIH gene
- Name:
- formyl peptide receptor 3
- Previous symbol:
- FPRL2
- Synonyms:
- FPRH1, FMLPY, RMLP-R-I
- Chromosome:
- 19q13.41
- Locus Type:
- gene with protein product
- Date approved:
- 1991-12-04
- Date modifiied:
- 2016-01-15
- Gene:
- LCE1B NIH gene
- Name:
- late cornified envelope 1B
- Previous symbol:
- SPRL2A
- Synonyms:
- LEP2
- Chromosome:
- 1q21.3
- Locus Type:
- gene with protein product
- Date approved:
- 2001-10-26
- Date modifiied:
- 2015-09-03
Related products to: Human PRL-2 (2-167) Active Enzyme
Related articles to: Human PRL-2 (2-167) Active Enzyme
- : Heart failure (HF) arises from multiple interrelated pathological processes. Among these, lysosomal impairment and loss of autophagic homeostasis are increasingly recognized as important contributors to myocardial damage and ventricular remodeling. This study sought to identify lysophagy-associated signature genes in HF and to define their biological roles, cellular origins, and potential diagnostic relevance. : Bulk myocardial transcriptome datasets, including GSE16499, GSE57338, and GSE76701, were integrated with the human cardiac single-cell dataset GSE145154. Differential expression analysis was first performed to identify lysophagy-related differentially expressed genes (DEGs). Candidate hub genes were then screened using support vector machine-recursive feature elimination (SVM-RFE) and least absolute shrinkage and selection operator (LASSO) regression. Functional enrichment analysis, Gene Set Enrichment Analysis (GSEA), immune infiltration assessment, single-cell transcriptomic mapping, and regulatory network analysis were subsequently conducted. The expression profiles of the selected genes were validated in a murine HF model, and VAMP8 overexpression assays were performed in H9c2 cells. : Five hub genes, namely , , , , and , were consistently and markedly decreased in failing myocardial tissue. These genes were mainly linked to SNARE-dependent vesicle trafficking and lysophagy regulation. A diagnostic model incorporating these hub genes demonstrated good discriminatory performance in both the training dataset and a small independent validation cohort, supporting further evaluation of their potential diagnostic value. Single-cell analysis further indicated that these genes were primarily enriched in cardiac FOLR2 tissue-resident macrophages (TRMs). Pseudotime and cell-cell communication analyses associated this module with FOLR2 TRM cell states and predicted interactions with cardiac stromal cells. In the HF mouse model, the mRNA levels of all five hub genes were decreased, with concurrent reductions in VAMP8, MCOLN1 and DERL1 protein expression. In Ang II/LLOMe-induced H9c2 cells, VAMP8 overexpression was associated with reduced cardiomyocyte injury, attenuation of changes in the abundance of lysosome- and autophagy-related proteins, and fewer ultrastructural abnormalities, suggesting a potential cardioprotective effect. : , , , , and were identified as candidate molecular markers of HF that reflect alterations in a lysophagy- and vesicular-transport-related program associated with FOLR2 tissue-resident macrophages. These findings provide new insights into immune-microenvironment remodeling in HF and suggest potential directions for mechanistic and therapeutic investigations. - Source: PubMed
Publication date: 2026/08/15
Cheng QiWang YanliWang DeqiangWu GuoxingLiu BiyunYuan QienZhu Fen - The phosphatase and tensin homolog deleted on chromosome 10 (PTEN) is one of the most frequently inactivated tumor suppressors in human cancers, serving as a critical negative regulator of phosphatidylinositol 3-kinase (PI3K)-AKT signaling. Although genetic mutation or deletion commonly underlie functional PTEN loss, accumulating evidence indicates that post-transcriptional and post-translational mechanisms also substantially contribute to PTEN suppression. Phosphatases of regenerating liver (PRLs), comprising PRL1, PRL2, and PRL3, are oncogenic phosphatases frequently overexpressed in both solid and hematological malignancies. Emerging studies reveal that PRLs can downregulate PTEN through a post-translational mechanism by direct dephosphorylation of PTEN at Tyr336, therefore promoting PTEN ubiquitination and proteasomal degradation. PRLs can also reduce PTEN expression through a post-transcriptional mechanism by dephosphorylating the inhibitory Tyr570 in JAK2, thereby activating the JAK2/STAT3-mediated miR-21 expression. These coordinated actions collectively amplify PI3K-AKT signaling, consequently promoting proliferation, survival, and metastasis. In the present review, we synthesize current knowledge of PRL structure, evolution, and functional diversity, evaluate genetic, biochemical, and organismal evidence linking PRLs to PTEN regulation, and discuss insights on PRL oncogenicity derived from experimental models. We further examine context-dependent functions of PRLs, unresolved questions regarding catalytic versus scaffold activities, and the therapeutic potential of targeting the PRL-PTEN axis. Understanding how PRLs modulate PTEN activity may reveal new strategies to restore tumor suppressor function in PTEN-deficient cancers. - Source: PubMed
Abou-Shanab Ahmed MYu JingmeiBai YunpengZhang Zhong-Yin - Non-small cell lung cancer (NSCLC) is a major subtype of lung cancer and accounts for a large proportion of cancer-related deaths worldwide. Despite extensive research progress in recent years, the diagnosis and treatment of lung cancer remain insufficient. There is an urgent need to deepen the mechanistic understanding of lung cancer, develop early diagnostic strategies, and explore novel therapeutic targets. In this study, qRT-PCR was used to detect the expression of circPTP4A2 (circular RNA PTP4A2) in tumor and adjacent normal tissues from 50 NSCLC patients. CircPTP4A2 was significantly upregulated in tumor tissues and was closely associated with patient survival and prognosis. In vitro silencing of circPTP4A2 in NSCLC cell lines SPCA1 and H1299 significantly inhibited cell proliferation and malignant metastatic potential. Moreover, modulating the expression of miR-127-5p and SMC3 effectively reversed the phenotypic changes induced by circPTP4A2 knockdown. In conclusion, circPTP4A2 is upregulated in NSCLC and promotes tumorigenesis and progression through the miR-127-5p/SMC3 signaling axis. - Source: PubMed
Publication date: 2026/05/07
Feng YaliHong JiangYang ChanggangCheng ChunXue YujieZhang JiaqiLu YuCao XiangJiang GengxiChong Xiaodan - Acute myeloid leukemia (AML) is an aggressive hematological malignancy that is sustained by leukemia-initiating cells (LICs). Although protein tyrosine phosphatase 4A2 (PTP4A2), also known as phosphatase of regenerating liver 2 (PRL2), is highly expressed in AML, the mechanisms by which PTP4A2 promotes leukemogenesis are largely unexplored. In this study, we demonstrate that PTP4A2 promotes AML by inhibiting the p53 tumor suppressor pathway in LICs. Using KMT2A-MLLT3-driven AML as a model, we found that PTP4A2 deficiency activates p53 and induces LIC apoptosis and senescence, thereby extending the survival of recipient mice repopulated with Ptp4a2-/- LICs. Mechanistically, PTP4A2 directly interacts with p53 and dephosphorylates it at serine 392, decreasing p53 stability and activity to enhance LIC proliferation and survival. Collectively, our findings identify p53 as a potential PTP4A2 substrate in leukemia cells and uncover a novel mechanism by which PTP4A2 enhances LIC maintenance. - Source: PubMed
Xiao ShiyuKobayashi MichihiroBai YunpengCai WenjieBarajas SergioAmin Mohammed AbdullahelVemula SasidharYao ChonghuaYang YuxiaBorchers ChristopherMays Tiffany MSotelo MagdalenaPan HaoJia YuzhiShen JianHu Sophie KAli MoiezVeranga SophiaOgino JaymeEggleston Sydney GLiu HuipingPerlman Harris RLi Loretta SAltman Jessica KAbaza YasminEklund Elizabeth AJi PengZhang Christine RKhan IrumMayo Lindsey DMulloy James CSukhanova MadinaDou YaliPlatanias Leonidas CZhang Zhong-YinChen HongxiaLiu Yan - Premature ovarian insufficiency (POI) profoundly compromises female reproductive health through accelerated follicle depletion and endocrine disruption. Emerging evidence highlights the therapeutic potential of mesenchymal stem cell-derived exosomes (MSC-Exs), particularly when their function is enhanced by hypoxic preconditioning. In this study, the ability of hypoxia-preconditioned MSC-Exs (H-Exs) to ameliorate oxidative damage to granulosa cells (GCs) and restore ovarian function, was systematically evaluated, and a POI rat model was used to investigate the underlying mechanism. - Source: PubMed
Publication date: 2026/01/22
Zhu XiaolanShi XuyanLu JingjingLi WenxinLiu YueqinJiang LinLv Yanting