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The Role of Phosphatases in Human Disease

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Biology".

Deadline for manuscript submissions: closed (20 April 2025) | Viewed by 2966

Special Issue Editor


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Guest Editor
Department of Medical Chemistry, Faculty of Medicine, University of Debrecen, H-4032 Debrecen, Hungary
Interests: endothelial cells; protein phosphatases; protein-protein interaction; cell signaling; lung diseases; angiogenesis; posttranslational modifications

Special Issue Information

Dear Colleagues,

Reversible protein phosphorylation is one of the most common post-translational modifications of proteins that regulates many, if not all, biological processes. Protein kinases attach a phosphate group to a specific side chain of proteins, while protein phosphatases are able to remove it via hydrolysis. The equilibrium between the activities of protein kinases and phosphatases is tightly regulated, ensuring the proper signal transduction of cells.

Abnormal protein phosphorylation, as well as insufficient dephosphorylation of proteins has been shown to cause various diseases such as cancer, neurodegenerative diseases, or immune system-related diseases. Thus, studying protein phosphatases themselves as well as their potential inhibitors or activators is an increasingly well-researched topic. A better understanding of protein dephosphorylation in signaling pathways is crucial in disease research and in therapeutic interventions in clinical trials.

This Special Issue welcomes comprehensive systematic reviews, impactful communications, and full research papers, including basic studies that will provide novel insights into the current knowledge of protein phosphatases in human diseases, while improving the understanding of novel molecular therapeutic applications.

Research topics may include (but are not limited to) the following:

  • Correlation between diseases and protein phosphatases;
  • Novel signaling mechanism related to phosphorylation;
  • Phosphorylation of specific disease-related proteins;
  • Therapeutic strategies based on targeting phosphatases or substrate proteins.

Dr. Boratkó Anita
Guest Editor

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Keywords

  • protein dephosphorylation
  • protein phosphatase
  • reversible phosphorylation
  • phospho-substrate
  • human diseases
  • cell signaling

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Published Papers (2 papers)

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Research

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25 pages, 2651 KiB  
Article
Cells of the Maternal–Fetal Interface May Contribute to Epidural-Related Maternal Fever After Administration of Ropivacaine: The Role of Phosphatases DUSP9 and PHLPP1
by Florian Horn, Verena Tretter, Victoria Kunihs, Peter Wohlrab, Bettina Trimmel, Kevin A. Janes, Tamara Djurkic, Meriem Mekiri, Martin Knöfler and Leila Saleh
Int. J. Mol. Sci. 2025, 26(12), 5520; https://doi.org/10.3390/ijms26125520 (registering DOI) - 9 Jun 2025
Abstract
Epidural-related maternal fever (ERMF) occurs with significant incidence in women receiving local anesthetics such as ropivacaine via epidural catheter for pain relief during labor. The causal mechanism behind this phenomenon is still not fully resolved, but evidence suggests that these anesthetics cause sterile [...] Read more.
Epidural-related maternal fever (ERMF) occurs with significant incidence in women receiving local anesthetics such as ropivacaine via epidural catheter for pain relief during labor. The causal mechanism behind this phenomenon is still not fully resolved, but evidence suggests that these anesthetics cause sterile inflammation. In this observational study, we investigated a possible contributory role of the dual-specificity phosphatase-9 (DUSP9) controlling the activity of mitogen-activated protein kinases (MAPK), and also PH-domain and Leucine-rich repeat phosphatase (PHLPP) regulating AKT kinases. The data show that ropivacaine differentially affects the expression of these phosphatases in distinct cell types of the umbilical cord and placenta. The gene expression of DUSP9 was almost completely switched off in the presence of ropivacaine in HUVECs and extravillous trophoblasts for up to 6 h, while the expression of PHLPP1 was upregulated in HUVECs and syncytiotrophoblasts. Extravillous trophoblasts were identified as a source of pro-inflammatory mediators and regulatory miRNAs in response to ropivacaine. Placentae at term exhibited a distinct DUSP9 expression pattern, whether the patients belonged to the control group or received epidural analgesia with or without elevated body temperature. The observed data imply that ropivacaine induces complex effects on the MAPK and AKT pathways at the feto–maternal interface, which contribute to the ERMF phenomenon. Full article
(This article belongs to the Special Issue The Role of Phosphatases in Human Disease)

Review

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41 pages, 8019 KiB  
Review
Role of Protein Phosphatases in Tumor Angiogenesis: Assessing PP1, PP2A, PP2B and PTPs Activity
by Márton Fonódi, Lilla Nagy and Anita Boratkó
Int. J. Mol. Sci. 2024, 25(13), 6868; https://doi.org/10.3390/ijms25136868 - 22 Jun 2024
Cited by 2 | Viewed by 2386
Abstract
Tumor angiogenesis, the formation of new blood vessels to support tumor growth and metastasis, is a complex process regulated by a multitude of signaling pathways. Dysregulation of signaling pathways involving protein kinases has been extensively studied, but the role of protein phosphatases in [...] Read more.
Tumor angiogenesis, the formation of new blood vessels to support tumor growth and metastasis, is a complex process regulated by a multitude of signaling pathways. Dysregulation of signaling pathways involving protein kinases has been extensively studied, but the role of protein phosphatases in angiogenesis within the tumor microenvironment remains less explored. However, among angiogenic pathways, protein phosphatases play critical roles in modulating signaling cascades. This review provides a comprehensive overview of the involvement of protein phosphatases in tumor angiogenesis, highlighting their diverse functions and mechanisms of action. Protein phosphatases are key regulators of cellular signaling pathways by catalyzing the dephosphorylation of proteins, thereby modulating their activity and function. This review aims to assess the activity of the protein tyrosine phosphatases and serine/threonine phosphatases. These phosphatases exert their effects on angiogenic signaling pathways through various mechanisms, including direct dephosphorylation of angiogenic receptors and downstream signaling molecules. Moreover, protein phosphatases also crosstalk with other signaling pathways involved in angiogenesis, further emphasizing their significance in regulating tumor vascularization, including endothelial cell survival, sprouting, and vessel maturation. In conclusion, this review underscores the pivotal role of protein phosphatases in tumor angiogenesis and accentuate their potential as therapeutic targets for anti-angiogenic therapy in cancer. Full article
(This article belongs to the Special Issue The Role of Phosphatases in Human Disease)
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