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Last update 08 May 2025

PTPRU

Last update 08 May 2025

Basic Info

Synonyms

FMI, hPTP-J, Pancreatic carcinoma phosphatase 2

+ [17]

Introduction

Tyrosine-protein phosphatase which dephosphorylates CTNNB1. Regulates CTNNB1 function both in cell adhesion and signaling. May function in cell proliferation and migration and play a role in the maintenance of epithelial integrity. May play a role in megakaryocytopoiesis.

Drugs associated with PTPRU

CN116555262

Patent Mining

Target

PTPRU

Mechanism-

Active Org.

East China University of Science & Technology

Originator Org.

East China University of Science & Technology

Active Indication

Brain Cancer

Inactive Indication-

Drug Highest PhaseDiscovery

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with PTPRU

100 Translational Medicine associated with PTPRU

0 Patents (Medical) associated with PTPRU

201

Literatures (Medical) associated with PTPRU

01 Nov 2024·The Journal of Nutrition

Protein Biomarkers of Ultra-Processed Food Consumption and Risk of Coronary Heart Disease, Chronic Kidney Disease, and All-Cause Mortality

Article

Author: Coresh, Josef ; Lichtenstein, Alice H. ; Chen, Jingsha ; Rebholz, Casey M. ; Du, Shutong ; Rebholz, Casey M ; Yu, Bing ; Lichtenstein, Alice H ; Appel, Lawrence J. ; Kim, Hyunju ; Appel, Lawrence J

BACKGROUNDThere is a need to understand the underlying biological mechanisms through which ultra-processed foods negatively affect health. Proteomics offers a valuable tool with which to examine different aspects of ultra-processed foods and their impact on health.OBJECTIVESThe aim of this study was to identify protein biomarkers of usual ultra-processed food consumption and assess their relation to the incidence of coronary heart disease (CHD), chronic kidney disease (CKD), and all-cause mortality risk.METHODSA total of 9361 participants from the Atherosclerosis Risk in Communities visit 3 (1993-1995) were included. Dietary intake was assessed using a 66-item food-frequency questionnaire and the processing levels were categorized on the basis of the Nova classification. Plasma proteins were detected using an aptamer-based proteomic assay. We used multivariable linear regressions to examine the association between ultra-processed food and proteins, and Cox proportional hazard models to identify associations between ultra-processed food-related proteins and health outcomes. Models extensively controlled for sociodemographic characteristics, health behaviors, and clinical factors.RESULTSEight proteins (6 positive, 2 negative) were identified as significantly associated with ultra-processed food consumption. Over a median follow-up of 22 y, there were 1276, 3084, and 5127 cases of CHD, CKD, and death, respectively. Three, 5, and 3 ultra-processed food-related proteins were associated with each outcome, respectively. One protein (β-glucuronidase) was significantly associated with a higher risk of all 3 outcomes, and 3 proteins (receptor-type tyrosine-protein phosphatase U, C-C motif chemokine 25, and twisted gastrulation protein homolog 1) were associated with a higher risk of 2 outcomes.CONCLUSIONSWe identified a panel of protein biomarkers that were significantly associated with ultra-processed food consumption. These proteins may be considered potential biomarkers for ultra-processed food intake and may elucidate the biological processes through which ultra-processed foods impact health outcomes.

01 Sep 2024·Chemosphere

Porous β-cyclodextrin polymers for rapid and efficient removal of organic micropollutants from water: The role of sulfonation and porosity on adsorption performance

Article

Author: Zhang, Lin ; Sun, Xiaoyu ; Li, Hengye ; Bie, Wenwen ; Wang, Zhongxia ; Cai, Tianpei ; Kong, Fenying ; Wang, Wei ; Wei, Meijie ; Zhang, Shuzhao

Removal of organic micropollutants (OMPs) from water, especially hydrophilic and ionized ones, is challenging for water remediation. Herein, porous β-cyclodextrin polymers (PCPs) with tailored functionalization were prepared based on molecular expansion strategy and sulfonation. Partially benzylated β-cyclodextrin was knotted by external crosslinker to form PCP1, and knotting PCP1 by expansion molecule generated PCP2. PCP1 and PCP2 were sulfonated to achieve PCP1-SO₃H and PCP2-SO₃H. Based on systematical adsorption evaluation toward multiple categories of OMPs, it was found that the introduced strong polar -SO₃H group could bring strong hydrogen bonding and electrostatic interactions. PCP2 showed the highest surface (998.97 m²/g) displayed more excellent adsorption performance toward neutral and anionic OMPs, and the adsorption mechanism for this property of PCP2 was dominated by hydrophobic interactions. In addition, the PCP1-SO₃H with the lowest surface area (39.75 m²/g) rather than PCP2-SO₃H with higher surface (519.28 m²/g) exhibited more superior adsorption towards hydrophilic and cationic OMPs, benefiting by hydrogen bonding and electrostatic interactions as well as appropriate porosity. These results not only confirmed the performance enhancement of PCPs through the integration of novel preparation strategy, but also provided fundamental guidance for PCPs design for water remediation.

01 May 2024·Bioorganic & Medicinal Chemistry Letters

The mechanism of covalent inhibition of LAR phosphatase by illudalic acid

Article

Author: Dudley, Gregory B ; Levinzon, Nathan D ; Gaston, Robert ; Osburn-Staker, Sandra ; Cox, James E ; Barrios, Amy M ; Cheatham, Thomas E ; Rueb, Nicole J ; Hansen, Daniel T ; Tanvir Ahmed, Kh

Leukocyte antigen-related (LAR) phosphatase is a receptor-type protein tyrosine phosphatase involved in cellular signaling and associated with human disease including cancer and metabolic disorders. Selective inhibition of LAR phosphatase activity by well characterized and well validated small molecules would provide key insights into the roles of LAR phosphatase in health and disease, but identifying selective inhibitors of LAR phosphatase activity has been challenging. Recently, we described potent and selective inhibition of LAR phosphatase activity by the fungal natural product illudalic acid. Here we provide a detailed biochemical characterization of the adduct formed between LAR phosphatase and illudalic acid. A mass spectrometric analysis indicates that two cysteine residues are covalently labeled by illudalic acid and a related analog. Mutational analysis supports the hypothesis that inhibition of LAR phosphatase activity is due primarily to the adduct with the catalytic cysteine residue. A computational study suggests potential interactions between the illudalic acid moiety and the enzyme active site. Taken together, these data offer novel insights into the mechanism of inhibition of LAR phosphatase activity by illudalic acid.

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PTPRU

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