Role of receptor protein tyrosine phosphatase α (RPTPα) and tyrosine phosphorylation in the serotonergic inhibition of voltage-dependent potassium channels

2000 ◽  
Vol 441 (2-3) ◽  
pp. 257-262 ◽  
Author(s):  
Paola Imbrici ◽  
Stephen J. Tucker ◽  
Maria Cristina D'Adamo ◽  
Mauro Pessia
Keyword(s):  
Potassium Channels ◽  
Tyrosine Phosphorylation ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Receptor Protein ◽  
Protein Tyrosine ◽  
Receptor Protein Tyrosine Phosphatase ◽  
Voltage Dependent

The role of receptor protein tyrosine phosphatase α in neuronal differentiation of embryonic stem cells

1996 ◽  
Vol 91 (2) ◽  
pp. 304-307 ◽  
Author(s):  
Wouter G. van Inzen ◽  
Maikel P. Peppelenbosch ◽  
Maria W.M. van den Brand ◽  
Leon G.J. Tertoolen ◽  
Siegfried de Laat
Keyword(s):  
Stem Cells ◽  
Embryonic Stem Cells ◽  
Neuronal Differentiation ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Embryonic Stem ◽  
Receptor Protein ◽  
Protein Tyrosine ◽  
Receptor Protein Tyrosine Phosphatase

scholarly journals Role of Receptor Protein Tyrosine Phosphatase γ in Sensing Extracellular CO2 and HCO3−

2016 ◽  
Vol 27 (9) ◽  
pp. 2616-2621 ◽  
Author(s):  
Yuehan Zhou ◽  
Lara A. Skelton ◽  
Lumei Xu ◽  
Margaret P. Chandler ◽  
Jessica M. Berthiaume ◽  
...  
Keyword(s):  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Receptor Protein ◽  
Protein Tyrosine ◽  
Receptor Protein Tyrosine Phosphatase

scholarly journals Lack of association between receptor protein tyrosine phosphatase RPTP mu and cadherins.

1996 ◽  
Vol 134 (6) ◽  
pp. 1513-1517 ◽  
Author(s):  
G C Zondag ◽  
W H Moolenaar ◽  
M F Gebbink
Keyword(s):  
Tyrosine Phosphorylation ◽  
Cell Density ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Surface Expression ◽  
Receptor Protein ◽  
Cell Contacts ◽  
Protein Tyrosine ◽  
Receptor Protein Tyrosine Phosphatase ◽  
Cell Cell

RPTP mu is a receptor-like protein tyrosine phosphatase that mediates homophilic cell-cell interactions. Surface expression of RPTP mu is restricted to cell-cell contacts and is upregulated with increasing cell density, suggesting a role for RPTP mu in contact-mediated signaling. It was recently reported (Brady-Kalnay, S.M., D.L. Rimm, and N.K. Tonks. 1995. J. Cell Biol. 130:977-986) that RPTP mu binds directly to cadherin/catenin complexes, and thus may regulate the tyrosine phosphorylation of such complexes. Here we report that this concept needs revision. Through reciprocal precipitations using a variety of antibodies against RPTP mu, cadherins, and catenins, we show that RPTP mu does not interact with cadherin/catenin complexes, even when assayed under very mild lysis conditions. We find that the anti-RPTP mu antiserum used by others precipitates cadherins in a nonspecific manner independent of RPTP mu. We conclude that, contrary to previous claims, RPTP mu does not interact with cadherin complexes and thus is unlikely to directly regulate cadherin/catenin function.

scholarly journals Receptor Protein Tyrosine Phosphatase γ Is a Marker for Pyramidal Cells and Sensory Neurons in the Nervous System and Is Not Necessary for Normal Development

2006 ◽  
Vol 26 (13) ◽  
pp. 5106-5119 ◽  
Author(s):  
Smaragda Lamprianou ◽  
Nathalie Vacaresse ◽  
Yoshihisa Suzuki ◽  
Hamid Meziane ◽  
Joseph D. Buxbaum ◽  
...  
Keyword(s):  
Sensory Neurons ◽  
Protein Tyrosine Phosphatase ◽  
Pyramidal Neurons ◽  
Tyrosine Phosphatase ◽  
Pyramidal Cells ◽  
Receptor Protein ◽  
Protein Tyrosine ◽  
Stratum Pyramidale ◽  
Receptor Protein Tyrosine Phosphatase

ABSTRACT In order to gain insight into the biological role of receptor protein tyrosine phosphatase γ (RPTPγ), we have generated RPTPγ-null mice. RPTPγ was disrupted by insertion of the β-galactosidase gene under the control of the RPTPγ promoter. As the RPTPγ-null mice did not exhibit any obvious phenotype, we made use of these mice to study RPTPγ expression and thus shed light on potential biological functions of this phosphatase. Inspection of mouse embryos shows that RPTPγ is expressed in a variety of tissues during embryogenesis. RPTPγ is expressed in both embryonic and adult brains. Specifically, we detected RPTPγ expression in cortical layers II and V and in the stratum pyramidale of the hippocampus, indicating that RPTPγ is a marker for pyramidal neurons. Mixed primary culture of glial cells showed a lack of expression of RPTPγ in astrocytes and a low expression of RPTPγ in oligodendrocytes and in microglia. Interestingly, RPTPγ expression was detected in all sensory organs, including the ear, nose, tongue, eye, and vibrissa follicles, suggesting a potential role of RPTPγ in sensory neurons. An initial behavioral analysis showed minor changes in the RPTPγ-null mice.

scholarly journals Role of Receptor Protein Tyrosine Phosphatase β/ζ in Neuron–Microglia Communication in a Cellular Model of Parkinson’s Disease

2021 ◽  
Vol 22 (13) ◽  
pp. 6646
Author(s):  
Marta del Campo ◽  
Rosalía Fernández-Calle ◽  
Marta Vicente-Rodríguez ◽  
Sara Martín Martínez ◽  
Esther Gramage ◽  
...  
Keyword(s):  
Parkinson’S Disease ◽  
Parkinson's Disease ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Neuroblastoma Cells ◽  
Specific Inhibitor ◽  
Receptor Protein ◽  
Protein Tyrosine ◽  
Receptor Protein Tyrosine Phosphatase

Pleiotrophin (PTN) is a neurotrophic factor that regulates glial responses in animal models of different types of central nervous system (CNS) injuries. PTN is upregulated in the brain in different pathologies characterized by exacerbated neuroinflammation, including Parkinson’s disease. PTN is an endogenous inhibitor of Receptor Protein Tyrosine Phosphatase (RPTP) β/ζ, which is abundantly expressed in the CNS. Using a specific inhibitor of RPTPβ/ζ (MY10), we aimed to assess whether the PTN/RPTPβ/ζ axis is involved in neuronal and glial injury induced by the toxin MPP+. Treatment with the RPTPβ/ζ inhibitor MY10 alone decreased the viability of both SH-SY5Y neuroblastoma cells and BV2 microglial cultures, suggesting that normal RPTPβ/ζ function is involved in neuronal and microglial viability. We observed that PTN partially decreased the cytotoxicity induced by MPP+ in SH-SY5Y cells underpinning the neuroprotective function of PTN. However, MY10 did not seem to modulate the SH-SY5Y cell loss induced by MPP+. Interestingly, we observed that media from SH-SY5Y cells treated with MPP+ and MY10 decreases microglial viability but may elicit a neuroprotective response of microglia by upregulating Ptn expression. The data suggest a neurotrophic role of microglia in response to neuronal injury through upregulation of Ptn levels.

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