Recombinant Human Phosphohistidine Phosphatase 1 PHPT1
- Known as:
- Recombinant Human Phosphohistidine Phosphatase 1 PHPT1
- Catalog number:
- enz-012
- Product Quantity:
- 5
- Category:
- -
- Supplier:
- Prospecbio
- Gene target:
- Recombinant Human Phosphohistidine Phosphatase 1 PHPT1
Related genes to: Recombinant Human Phosphohistidine Phosphatase 1 PHPT1
- Gene:
- PHPT1 NIH gene
- Name:
- phosphohistidine phosphatase 1
- Previous symbol:
- -
- Synonyms:
- PHP14, HSPC141, CGI-202, DKFZp564M173, bA216L13.10
- Chromosome:
- 9q34.3
- Locus Type:
- gene with protein product
- Date approved:
- 2004-03-23
- Date modifiied:
- 2016-10-20
Related products to: Recombinant Human Phosphohistidine Phosphatase 1 PHPT1
Related articles to: Recombinant Human Phosphohistidine Phosphatase 1 PHPT1
- The human protein histidine phosphatase PHPT1 is involved in several important cellular pathways and has been implicated in various cancers. However, the biological roles of this enzyme are not well understood due to a lack of chemical tools that enable its study. Herein we have identified phenylarsonic acids as general scaffolds which inhibit PHPT1 activity. Notably, phenylarsonic acids can be embedded into peptide sequences, providing the first known peptide-based inhibitors of PHPT1. In a counterscreen against a small panel of phosphatases, we demonstrate that these compounds exhibit some selectivity for PHPT1. Moreover, we show that these compounds exhibit mixed inhibition. We provide evidence that reduction of the phenylarsonic acids by reducing agents like dithiothreitol (DTT) to provide phenylarsine species gives rise to the observed PHPT1 inhibition. These As(III) species are known to be thiophilic and can interact with solvent-exposed cysteine residues of proteins. Finally, we demonstrate that mutating the three cysteine residues of PHPT1 to alanine results in a significant decrease in enzyme inhibition by the phenylarsonic acids, suggesting that these compounds likely interact at least in part with Cys residues in PHPT1. - Source: PubMed
Publication date: 2026/03/10
Keyes E DallesHollow Sophia EOblad PaulJohnstone Timothy CBarrios Amy M - While optimal fluoride (F) levels support oral health, chronic exposure to high concentrations can lead to skeletal and dental fluorosis, especially in children. Emerging evidence suggests that excessive fluoride intake may disrupt systemic physiology, yet the underlying mechanisms remain poorly understood. To address this gap, we performed a comparative urinary proteomic analysis using LC-MS/MS in schoolchildren residing in a high-fluoride region, categorizing participants into high-fluoride (HF) and low-fluoride (LF) groups based on urinary fluoride excretion. Among 460 quantified proteins, ten were differentially expressed in the HF group, six upregulated (PHPT1, SPP1, COLEC12, CST4, DCHS1, LDHB) and four downregulated (CTSH, NECTIN1, TNC, KLK1). Gene Ontology enrichment highlighted associations with cell adhesion, ossification, and tissue development. Notably marked alterations in osteopontin (SPP1) and tenascin-C (TNC), key regulators of bone remodeling and dental matrix organization, suggesting disrupted focal adhesion signaling, impaired matrix integrity, and dysregulated biomineralization. Additional changes in proteins associated with enamel formation, oxidative stress, and immune regulation suggest that high fluoride exposure may broadly disrupt extracellular matrix organization and trigger inflammatory pathways. These findings demonstrate that excessive fluoride exposure induces systemic molecular disturbances in children, with implications for bone and soft tissue homeostasis. This research adds to the body of human evidence concerning fluoride's biological impact, advocating for vigilant exposure monitoring. - Source: PubMed
Publication date: 2026/01/06
Pongsapipatana NawapanGavila PatcharapornCho Sung-DaeEl-Tanani MohamedRabbani Syed ArmanIslam SofiqulEssigmann John MSriwattanapong KanokwanPorntaveetus Thantrira - Phosphorylation is set by the opposing activities of kinases and phosphatases and this regulation likely contributes to exercise-induced adaptation. It does so by regulating mitochondrial biogenesis, muscle remodeling, and metabolic flexibility. The process by which exercise activates the AMPK, MAPK, and Akt-mTOR pathways, and how phosphatases (MKP, PHLPP, and PHPT1/LHPP) limit signal amplitude and duration to avoid maladaptive behavior, has been extensively studied. Some data suggest PHLPP2 may increase after HIIT, which could contribute to limiting Akt activity. In contrast, endurance training has been associated in some studies with relatively lower PHLPP activity; this observation may be consistent with sustained Akt-dependent mitochondrial adaptations, but direct causal evidence is limited. Systems-level phosphoproteomics unveils tissue- and time-resolved, modality-dependent phosphorylation programs and situates this axis within broader PTM crosstalk (lactylation). We outline manageable gaps linking kinase-phosphatase interactions to chromatin regulation, delineate non-canonical histidine phosphorylation, and present a condensed roadmap (time-resolving, compartment-aware phosphoproteomics integrated with epigenomic profiling) that connects enzyme function to phenotype and provides precise exercise recommendations and metabolic disease therapies. - Source: PubMed
Publication date: 2025/12/10
Chen HemingLi ZhihuiLiu YanyanJi YingLiu JunjieZheng Mi - Low barometric pressure hypoxia at high altitudes triggers vascular remodeling, resulting in high-altitude pulmonary hypertension (HAPH). The key step is the transformation of pulmonary artery smooth muscle cells (PASMCs) from a contractile to synthetic phenotype. Protein kinases and phosphatases contribute to phenotype transformation by altering phosphorylated protein expression. - Source: PubMed
Publication date: 2025/08/28
Guo GeZhu Ming-XiangXu XiangLi XinChen Yi-BingShen Yan-YingLi Han-LuCheng Li-TingHe Kun-LunYao Yong-MingLiu Chun-Lei - Lung squamous cell carcinoma (LUSC) is a subtype of non-small cell lung cancer. It has a grim prognosis for patients, primarily because the disease often remains asymptomatic in its early stages. As a result, it is frequently diagnosed at an advanced stage, limiting treatment options. This underscores the importance of studying potential biomarkers and developing personalized treatment strategies. In this study, we used an advanced bioinformatics approach, integrating two authoritative databases, NCBI's GEO and TCGA, to perform a large-scale cross-platform gene expression analysis. To deeply mine the gene expression data of a large number of lung squamous carcinoma samples, we used a screening strategy based on median absolute deviation to select genes that differed significantly in multiple datasets. The expression variations of these genes between normal and cancerous tissues provided us with valuable clues revealing key molecules that may be involved in the disease process. Through rigorous statistical tests, we identified 36 genes that were significantly associated with patient survival, and further constructed a model using Cox proportional risk model containing 11 key genes (MRPL40, GABPB1AS1, PTPN3, SNCA, PYGB, RAP1, VDR, PHPT1, KIAA0100, TBC1D30, CYP7B1) in a risk prediction model. The prediction model not only reflects the strong correlation between gene expression and LUSC prognosis, but also provides clinicians with an effective tool to predict patients' survival prospects. In the future, this model is expected to guide the development of individualized treatment plans, thereby improving the quality of life and overall prognosis of patients. - Source: PubMed
Publication date: 2024/12/26
Zhang QiqingHe HaidongWei YiLi GuopingShou Lu