Receptor-Type Tyrosine-Protein Phosphatase Epsilon

2020 ◽  
Author(s):  
Keyword(s):  
Protein Phosphatase ◽  
Receptor Type

scholarly journals Hydroxyindole Carboxylic Acid-Based Inhibitors for Receptor-Type Protein Tyrosine Protein Phosphatase Beta

2014 ◽  
Vol 20 (14) ◽  
pp. 2130-2140 ◽  
Author(s):  
Li-Fan Zeng ◽  
Ruo-Yu Zhang ◽  
Yunpeng Bai ◽  
Li Wu ◽  
Andrea M. Gunawan ◽  
...  
Keyword(s):  
Carboxylic Acid ◽  
Protein Phosphatase ◽  
Receptor Type ◽  
Protein Tyrosine ◽  
Type Protein

scholarly journals Impaired local regulation of ryanodine receptor type 2 by protein phosphatase 1 promotes atrial fibrillation

2014 ◽  
Vol 103 (1) ◽  
pp. 178-187 ◽  
Author(s):  
David Y. Chiang ◽  
Na Li ◽  
Qiongling Wang ◽  
Katherina M. Alsina ◽  
Ann P. Quick ◽  
...  
Keyword(s):  
Atrial Fibrillation ◽  
Ryanodine Receptor ◽  
Protein Phosphatase ◽  
Receptor Type ◽  
Protein Phosphatase 1 ◽  
Local Regulation

scholarly journals Receptor-type tyrosine-protein phosphatase κ directly targets STAT3 activation for tumor suppression in nasal NK/T-cell lymphoma

Blood ◽  
2015 ◽  
Vol 125 (10) ◽  
pp. 1589-1600 ◽  
Author(s):  
Yun-Wen Chen ◽  
Tianhuan Guo ◽  
Lijun Shen ◽  
Kai-Yau Wong ◽  
Qian Tao ◽  
...  
Keyword(s):  
T Cell ◽  
Protein Phosphatase ◽  
Tumor Suppression ◽  
Cell Lymphoma ◽  
T Cell Lymphoma ◽  
Receptor Type ◽  
Nasal Type ◽  
Key Points ◽  
Nk T Cell

Key Points PTPRK binds to STAT3 and directly dephosphorylates phospho-STAT3 at Tyr705. Loss of PTPRK, located in the deleted 6q region, leads to STAT3 activation and contributes to nasal-type NK/T-cell lymphoma pathogenesis.

scholarly journals Impaired local regulation of ryanodine receptor type-2 by protein phosphatase 1 promotes atrial fibrillation

2013 ◽  
Vol 34 (suppl 1) ◽  
pp. P5016-P5016
Author(s):  
D. Y. Chiang ◽  
N. Li ◽  
G. Wang ◽  
Q. Wang ◽  
A. Quick ◽  
...  
Keyword(s):  
Atrial Fibrillation ◽  
Ryanodine Receptor ◽  
Protein Phosphatase ◽  
Receptor Type ◽  
Protein Phosphatase 1 ◽  
Local Regulation

scholarly journals Tyrosine-Protein Phosphatase Non-receptor Type 9 (PTPN9) Negatively Regulates the Paracrine Vasoprotective Activity of Bone-Marrow Derived Pro-angiogenic Cells: Impact on Vascular Degeneration in Oxygen-Induced Retinopathy

2021 ◽  
Vol 9 ◽  
Author(s):  
Michel Desjarlais ◽  
Pakiza Ruknudin ◽  
Maëlle Wirth ◽  
Isabelle Lahaie ◽  
Rabah Dabouz ◽  
...  
Keyword(s):  
Bone Marrow ◽  
Rat Model ◽  
Protein Phosphatase ◽  
Ex Vivo ◽  
Stem Cell Differentiation ◽  
Negative Regulator ◽  
Receptor Type ◽  
Vegf Receptor ◽  
Tubule Formation ◽  
Oxygen Induced Retinopathy

Background and AimInsufficient post-ischemic neovascularization is an initial key step in the pathogenesis of Oxygen-Induced Retinopathy (OIR). During neovascularization, pro-angiogenic cells (PACs) are mobilized from the bone marrow and integrate into ischemic tissues to promote angiogenesis. However, the modulation of PAC paracrine activity during OIR and the specific mechanisms involved remain to be explored. Because Tyrosine-protein phosphatase non-receptor type 9 (PTPN9) is reported to be a negative regulator of stem cell differentiation and angiogenesis signaling, we investigated its effect on PAC activity in the context of OIR.Methods and ResultsIn a rat model of OIR, higher levels of PTPN9 in the retina and in bone marrow derived PACs are associated with retinal avascular areas, lower levels of the mobilization factor SDF-1 and decreased number of CD34+/CD117+/CD133+ PACs. PACs exposed ex vivo to hyperoxia display increased PTPN9 expression, which is associated with impaired ability of PAC secretome to promote angiogenesis ex vivo (choroidal vascular sprouting) and in vitro (endothelial cell tubule formation) compared to the secretome of PACs maintained in normoxia. Suppression of PTPN9 (using siRNA) increases VEGF and SDF-1 expression to normalize PAC secretome during hyperoxia, leading to restored angiogenic ability of PAC secretome. Moreover, endothelial cells exposed to the secretome of siPTPN9-treated PACs expressed increased levels of activated form of VEGF receptor 2 (VEGFR2). In the rat model of OIR, intravitreal injection of secretome from siPTPN9-treated PACs significantly reduced retinal vaso-obliteration; this was associated with higher retinal levels of VEGF/SDF-1, and increased recruitment of PACs (CD34+ cells) to the retinal and choroidal vessels.ConclusionOur results suggest that hyperoxia alters the paracrine proangiogenic activity of BM-PACs by inducing PTPN9, which can contribute to impair post-ischemic revascularization in the context of OIR. Targeting PTPN9 restores PAC angiogenic properties, and provide a new target for vessel integrity in ischemic retinopathies.

Tyrosine-Protein Phosphatase Non-receptor Type 11 (PTPN11)

2017 ◽  
pp. 1-9
Author(s):  
Takenori Kotani ◽  
Yoji Murata ◽  
Yasuyuki Saito ◽  
Takashi Matozaki
Keyword(s):  
Protein Phosphatase ◽  
Receptor Type
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