Increased Proteolytic Processing of Protein Tyrosine Phosphatase μ in Confluent Vascular Endothelial Cells:  The Role of PC5, a Member of the Subtilisin Family†

Biochemistry ◽  
1996 ◽  
Vol 35 (12) ◽  
pp. 3797-3802 ◽  
Author(s):  
Michel Campan ◽  
Masao Yoshizumi ◽  
Nabil G. Seidah ◽  
Mu-En Lee ◽  
Cesario Bianchi ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Protein Tyrosine Phosphatase ◽  
Vascular Endothelial Cells ◽  
Tyrosine Phosphatase ◽  
Proteolytic Processing ◽  
Vascular Endothelial ◽  
Protein Tyrosine

Vascular Endothelial Protein Tyrosine Phosphatase Regulates Endothelial Function

Physiology ◽  
2021 ◽  
Vol 36 (2) ◽  
pp. 84-93
Author(s):  
Dietmar Vestweber
Keyword(s):  
Endothelial Cells ◽  
Adhesion Molecule ◽  
Tumor Angiogenesis ◽  
Protein Tyrosine Phosphatase ◽  
Therapeutic Potential ◽  
Vascular Endothelial Cells ◽  
Tyrosine Phosphatase ◽  
Tyrosine Kinase Receptor ◽  
Vascular Endothelial ◽  
Protein Tyrosine

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.

scholarly journals Shear Stress-induced Redistribution of Vascular Endothelial-Protein-tyrosine Phosphatase (VE-PTP) in Endothelial Cells and Its Role in Cell Elongation

2014 ◽  
Vol 289 (10) ◽  
pp. 6451-6461 ◽  
Author(s):  
Kemala Isnainiasih Mantilidewi ◽  
Yoji Murata ◽  
Munemasa Mori ◽  
Chihiro Otsubo ◽  
Takenori Kotani ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Shear Stress ◽  
Protein Tyrosine Phosphatase ◽  
Cell Elongation ◽  
Tyrosine Phosphatase ◽  
Vascular Endothelial ◽  
Protein Tyrosine

scholarly journals Role of protein tyrosine phosphatase 1B (PTP1B) in the increased sensitivity of endothelial cells to a promigratory effect of erythropoietin in an inflammatory environment

2020 ◽  
Vol 401 (10) ◽  
pp. 1167-1180
Author(s):  
María Eugenia Chamorro ◽  
Romina Maltaneri ◽  
Agustina Schiappacasse ◽  
Alcira Nesse ◽  
Daniela Vittori
Keyword(s):  
Endothelial Cells ◽  
Cell Migration ◽  
Cross Talk ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Endothelial Cell Migration ◽  
Protein Tyrosine Phosphatase 1B ◽  
Vascular Events ◽  
Protein Tyrosine ◽  
Sensitizing Effect

AbstractThe proliferation and migration of endothelial cells are vascular events of inflammation, a process which can also potentiate the effects of promigratory factors. With the aim of investigating possible modifications in the activity of erythropoietin (Epo) in an inflammatory environment, we found that Epo at a non-promigratory concentration was capable of stimulating EA.hy926 endothelial cell migration when TNF-α was present. VCAM-1 and ICAM-1 expression, as well as adhesion of monocytic THP-1 cells to endothelial layers were also increased. Structurally modified Epo (carbamylation or N-homocysteinylation) did not exhibit these effects. The sensitizing effect of TNF-α on Epo activity was mediated by the Epo receptor. Inhibition assays targeting the PI3K/mTOR/NF-κB pathway, shared by Epo and TNF-α, show a cross-talk between both cytokines. As observed in assays using antioxidants, cell migration elicited by TNF-α + Epo depended on TNF-α-generated reactive oxygen species (ROS). ROS-mediated inactivation of protein tyrosine phosphatase 1B (PTP1B), involved in Epo signaling termination, could explain the synergistic effect of these cytokines. Our results suggest that ROS generated by inflammation inactivate PTP1B, causing the Epo signal to last longer. This mechanism, along with the cross-talk between both cytokines, could explain the sensitizing action of TNF-α on the migratory effect of Epo.

scholarly journals Emerging Role of AP-1 Transcription Factor JunB in Angiogenesis and Vascular Development

2021 ◽  
Vol 22 (6) ◽  
pp. 2804
Author(s):  
Yasuo Yoshitomi ◽  
Takayuki Ikeda ◽  
Hidehito Saito-Takatsuji ◽  
Hideto Yonekura
Keyword(s):  
Endothelial Cells ◽  
Transcription Factor ◽  
Blood Vessel ◽  
Vascular Endothelial Cells ◽  
Vascular Development ◽  
Endothelial Cell Migration ◽  
Vascular Endothelial ◽  
Blood Vessel Formation ◽  
Vessel Formation

Blood vessels are essential for the formation and maintenance of almost all functional tissues. They play fundamental roles in the supply of oxygen and nutrition, as well as development and morphogenesis. Vascular endothelial cells are the main factor in blood vessel formation. Recently, research findings showed heterogeneity in vascular endothelial cells in different tissue/organs. Endothelial cells alter their gene expressions depending on their cell fate or angiogenic states of vascular development in normal and pathological processes. Studies on gene regulation in endothelial cells demonstrated that the activator protein 1 (AP-1) transcription factors are implicated in angiogenesis and vascular development. In particular, it has been revealed that JunB (a member of the AP-1 transcription factor family) is transiently induced in endothelial cells at the angiogenic frontier and controls them on tip cells specification during vascular development. Moreover, JunB plays a role in tissue-specific vascular maturation processes during neurovascular interaction in mouse embryonic skin and retina vasculatures. Thus, JunB appears to be a new angiogenic factor that induces endothelial cell migration and sprouting particularly in neurovascular interaction during vascular development. In this review, we discuss the recently identified role of JunB in endothelial cells and blood vessel formation.

scholarly journals Translocation of protein tyrosine phosphatase Pez/PTPD2/PTP36 to the nucleus is associated with induction of cell proliferation

2000 ◽  
Vol 113 (17) ◽  
pp. 3117-3123 ◽  
Author(s):  
C. Wadham ◽  
J.R. Gamble ◽  
M.A. Vadas ◽  
Y. Khew-Goodall
Keyword(s):  
Cell Proliferation ◽  
Endothelial Cells ◽  
Nuclear Protein ◽  
Vascular Endothelial Cells ◽  
Tyrosine Phosphatase ◽  
Subcellular Localisation ◽  
Vascular Endothelial ◽  
Proliferating Cells ◽  
Wound Edge

Pez is a non-transmembrane tyrosine phosphatase with homology to the FERM (4.1, ezrin, radixin, moesin) family of proteins. The subcellular localisation of Pez in endothelial cells was found to be regulated by cell density and serum concentration. In confluent monolayers Pez was cytoplasmic, but in cells cultured at low density Pez was nuclear, suggesting that it is a nuclear protein in proliferating cells. This notion is supported by the loss of nuclear Pez when cells are serum-starved to induce quiescence, and the rapid return of Pez to the nucleus upon refeeding with serum to induce proliferation. Vascular endothelial cells normally exist as a quiescent confluent monolayer but become proliferative during angiogenesis or upon vascular injury. Using a ‘wound’ assay to mimic these events in vitro, Pez was found to be nuclear in the cells that had migrated and were proliferative at the ‘wound’ edge. TGFbeta, which inhibits cell proliferation but not migration, inhibited the translocation of Pez to the nucleus in the cells at the ‘wound’ edge, further strengthening the argument that Pez plays a role in the nucleus during cell proliferation. Together, the data presented indicate that Pez is a nuclear tyrosine phosphatase that may play a role in cell proliferation.

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