Bibliografías temáticas / Phosphatase, PTPRG, Endothelial cells, permeability

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Literatura académica sobre el tema "Phosphatase, PTPRG, Endothelial cells, permeability"

Autor: Grafiati
Publicado: 11 de marzo de 2023

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Artículos de revistas sobre el tema "Phosphatase, PTPRG, Endothelial cells, permeability"

1

Essler, Markus, Karin Hermann, Mutsuki Amano, et al. "Pasteurella multocida Toxin Increases Endothelial Permeability via Rho Kinase and Myosin Light Chain Phosphatase." Journal of Immunology 161, no. 10 (1998): 5640–46. http://dx.doi.org/10.4049/jimmunol.161.10.5640.

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Abstract Pasteurella multocida toxin (PMT) has been shown to induce actin reorganization through activation of the GTPase Rho. Here we investigated the involvement of the Rho target proteins Rho kinase and myosin light chain (MLC) phosphatase in the PMT-induced increase in endothelial permeability and the underlying actin reorganization of endothelial cells. Stimulation of endothelial layers with PMT enhanced transendothelial permeability >10-fold, and this was abolished by pretreatment with the specific Rho inactivator C3 transferase from Clostridium botulinum. The PMT-induced increase
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2

Vestweber, Dietmar. "Vascular Endothelial Protein Tyrosine Phosphatase Regulates Endothelial Function." Physiology 36, no. 2 (2021): 84–93. http://dx.doi.org/10.1152/physiol.00026.2020.

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Vascular endothelial protein tyrosine phosphatase (VE-PTP) is a receptor-type PTP (RPTP), predominantly expressed in vascular endothelial cells. It regulates embryonic and tumor angiogenesis and controls vascular permeability and homeostasis in inflammation. Major substrates are the tyrosine kinase receptor Tie-2 and the adhesion molecule VE-cadherin. This review describes how VE-PTP controls vascular functions by its various substrates and the therapeutic potential of VE-PTP in various pathophysiological settings.
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3

Wachtel, M., K. Frei, E. Ehler, A. Fontana, K. Winterhalter, and S. M. Gloor. "Occludin proteolysis and increased permeability in endothelial cells through tyrosine phosphatase inhibition." Journal of Cell Science 112, no. 23 (1999): 4347–56. http://dx.doi.org/10.1242/jcs.112.23.4347.

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Regulation of epithelial and endothelial permeability is essential for proper function of compartmentalized organisms, and tyrosine phosphorylation plays an important role in this process. We analyzed the impact of protein tyrosine phosphatase (PTP) inhibition on the structure of endothelial junctional proteins. In human umbilical vein endothelial cells (HUVECs) the PTP inhibitors phenylarsine oxide (PAO) and pervanadate induced proteolysis of the tight junction protein occludin. Occludin proteolysis was inhibited by the metalloproteinase inhibitor 1,10-phenanthroline (PHEN), but not by inhibi
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4

Kaestner, Charlotte L., Amin Sobh, Jianping Li, Alberto Riva, Richard Lynn Bennett, and Jonathan D. Licht. "Functional CRISPR Screening Identifies Ptprg As a Driver of Migration and Adhesion in NSD2-E1099K ALL." Blood 138, Supplement 1 (2021): 1149. http://dx.doi.org/10.1182/blood-2021-154009.

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Abstract Background: Acute Lymphoblastic Leukemia (ALL) is the most common childhood cancer and frequently infiltrates the central nervous system (CNS). CNS-directed therapy is currently limited to intrathecal and systemic high-dose methotrexate, or less commonly craniospinal irradiation, both of which are associated with substantial neurotoxicity. A lack of mechanistic understanding of the mechanisms of CNS infiltration presents an obstacle for the development of more specific and less toxic therapeutic approaches. We previously showed that ALL cells with a specific mutation (E1099K) in the h
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5

Kevil, Christopher G., Naotsuka Okayama, and J. Steven Alexander. "H2O2-mediated permeability II: importance of tyrosine phosphatase and kinase activity." American Journal of Physiology-Cell Physiology 281, no. 6 (2001): C1940—C1947. http://dx.doi.org/10.1152/ajpcell.2001.281.6.c1940.

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We previously reported that exposure of endothelial cells to H2O2results in a loss of cell-cell apposition and increased endothelial solute permeability. The purpose of this study was to determine how tyrosine phosphorylation and tyrosine phosphatases contribute to oxidant-mediated disorganization of endothelial cell junctions. We found that H2O2caused a rapid decrease in total cellular phosphatase activity that facilitates a compensatory increase in cellular phosphotyrosine residues. H2O2exposure also results in increased endothelial monolayer permeability, which was attenuated by pp60, an in
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6

Gloor, Sergio M., Adrien Weber, Naoto Adachi, and Karl Frei. "Interleukin-1 Modulates Protein Tyrosine Phosphatase Activity and Permeability of Brain Endothelial Cells." Biochemical and Biophysical Research Communications 239, no. 3 (1997): 804–9. http://dx.doi.org/10.1006/bbrc.1997.7557.

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Kelly, J. J., T. M. Moore, P. Babal, A. H. Diwan, T. Stevens, and W. J. Thompson. "Pulmonary microvascular and macrovascular endothelial cells: differential regulation of Ca2+and permeability." American Journal of Physiology-Lung Cellular and Molecular Physiology 274, no. 5 (1998): L810—L819. http://dx.doi.org/10.1152/ajplung.1998.274.5.l810.

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Cytosolic Ca2+concentration ([Ca2+]i) plays an important role in control of pulmonary vascular endothelial cell (ECs) barrier function. In this study, we investigated whether thapsigargin- and ionomycin-induced changes in cytosolic Ca2+induce permeability in rat pulmonary microvascular (RPMV) versus macrovascular (RPA) ECs. In Transwell cultures, RPMVECs formed a tighter, more restrictive barrier than RPAECs to 12,000-, 72,000-, and 150,000-molecular-weight FITC-labeled dextrans. Thapsigargin (1 μM) produced higher [Ca2+]ilevels in RPAECs than in RPMVECs and increased permeability in RPAEC but
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8

Kim, Soo Hyeon, Young-Rak Cho, Hyeon-Ju Kim та ін. "Antagonism of VEGF-A–induced increase in vascular permeability by an integrin α3β1-Shp-1-cAMP/PKA pathway". Blood 120, № 24 (2012): 4892–902. http://dx.doi.org/10.1182/blood-2012-05-428243.

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Abstract In cancer, VEGF-induced increase in vascular permeability results in increased interstitial pressure, reducing perfusion and increasing hypoxia, which reduce delivery of chemotherapeutic agents and increase resistance to ionizing radiation. Here, we show that both TIMP-2 and Ala + TIMP-2, a TIMP-2 mutant without matrix metalloproteinase inhibitory activity, antagonize the VEGF-A–induced increase in vascular permeability, both in vitro and in vivo. Like other agents known to preserve endothelial barrier function, TIMP-2 elevates cytosolic levels of cAMP and increases cytoskeletal-assoc
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9

Staddon, J. M., K. Herrenknecht, C. Smales, and L. L. Rubin. "Evidence that tyrosine phosphorylation may increase tight junction permeability." Journal of Cell Science 108, no. 2 (1995): 609–19. http://dx.doi.org/10.1242/jcs.108.2.609.

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Tight junction permeability control is important in a variety of physiological and pathological processes. We have investigated the role of tyrosine phosphorylation in the regulation of tight junction permeability. MDCK epithelial cells and brain endothelial cells were grown on filters and tight junction permeability was determined by transcellular electrical resistance (TER). The tyrosine phosphatase inhibitor pervanadate caused a concentration- and time-dependent decrease in TER in both MDCK and brain endothelial cells. However, as expected, pervanadate resulted in the tyrosine phosphorylati
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10

Juettner, Vanessa V., Kevin Kruse, Arkaprava Dan, et al. "VE-PTP stabilizes VE-cadherin junctions and the endothelial barrier via a phosphatase-independent mechanism." Journal of Cell Biology 218, no. 5 (2019): 1725–42. http://dx.doi.org/10.1083/jcb.201807210.

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Vascular endothelial (VE) protein tyrosine phosphatase (PTP) is an endothelial-specific phosphatase that stabilizes VE-cadherin junctions. Although studies have focused on the role of VE-PTP in dephosphorylating VE-cadherin in the activated endothelium, little is known of VE-PTP’s role in the quiescent endothelial monolayer. Here, we used the photoconvertible fluorescent protein VE-cadherin-Dendra2 to monitor VE-cadherin dynamics at adherens junctions (AJs) in confluent endothelial monolayers. We discovered that VE-PTP stabilizes VE-cadherin junctions by reducing the rate of VE-cadherin intern
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Tesis sobre el tema "Phosphatase, PTPRG, Endothelial cells, permeability"

1

Spring, Kathleen. "Role of the protein tyrosine phosphatase DEP-1 in Src activation and the mediation of biological cell functions of endothelial and breast cancer cells." Thèse, 2012. http://hdl.handle.net/1866/8811.

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L’implication des protéines tyrosines phosphatases (PTPs) dans la régulation de la signalisation et la médiation des fonctions cellulaires a été bien établie dans les dernières années. Cependant, les mécanismes moléculaires par lesquels les PTPs régulent les processus fondamentaux tels que l’angiogenèse demeurent méconnus. Il a été rapporté que l’expression de la PTP DEP-1 (Density-enhanced phosphatase 1) augmente avec la densité cellulaire et corrèle avec la déphosphorylation du récepteur VEGFR2. Cette déphosphorylation contribue à l’inhibition de contact dans les cellules endothéliales à con
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2

Fournier, Patrick. "Rôles de la protéine tyrosine phosphatase DEP-1 dans l'angiogenèse, la perméabilité vasculaire et la progression tumorale." Thèse, 2015. http://hdl.handle.net/1866/13902.

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L’angiogenèse et l’augmentation de la perméabilité vasculaire sont des éléments clés pour la croissance et la progression tumorale. Par conséquent, de nombreux efforts sont déployés à comprendre les mécanismes moléculaires impliqués dans la formation et le remodelage des vaisseaux sanguins de manière à identifier de nouvelles cibles thérapeutiques potentielles. De cette optique, les travaux de cette thèse se sont concentrés sur la protéine tyrosine phosphatase DEP-1, initialement identifiée comme un régulateur négatif de la prolifération et de la phosphorylation du VEGFR2 lorsque fortement exp
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