scholarly journals The cloning of a receptor-type protein tyrosine phosphatase expressed in the central nervous system

1993 ◽  
Vol 268 (14) ◽  
pp. 10573-10581
Author(s):  
J.B. Levy ◽  
P.D. Canoll ◽  
O. Silvennoinen ◽  
G. Barnea ◽  
B. Morse ◽  
...  
Keyword(s):  
Central Nervous System ◽  
Nervous System ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Receptor Type ◽  
Protein Tyrosine ◽  
Type Protein ◽  
The Central Nervous System

scholarly journals Identification of a receptor-type protein tyrosine phosphatase expressed in postmitotic maturing neurons: its structure and expression in the central nervous system

1997 ◽  
Vol 321 (3) ◽  
pp. 865-872 ◽  
Author(s):  
Masatoshi TAGAWA ◽  
Takuji SHIRASAWA ◽  
Yu-ichi YAHAGI ◽  
Toshifumi TOMODA ◽  
Hidehito KUROYANAGI ◽  
...  
Keyword(s):  
Central Nervous System ◽  
Nervous System ◽  
Protein Tyrosine Phosphatase ◽  
Cortical Neurons ◽  
Tyrosine Phosphatase ◽  
Receptor Type ◽  
Phosphatase Domain ◽  
Protein Tyrosine ◽  
Type Protein ◽  
Developing Neocortex

We have isolated a rat cDNA encoding a receptor-type protein-tyrosine-phosphatase (RTP) expressed in brain and kidney (RPTP-BK) and characterized its expression in the developing central nervous system. RPTP-BK has seven fibronectin type III-like repeats in the extracellular region and a unique catalytic phosphatase domain in the cytoplasmic region. Bacterial expression of its phosphatase domain showed that the dephosphorylation of phosphotyrosine residues was mediated by the cytoplasmic catalytic domain. Sequence comparison revealed that RPTP-BK is homologous with GLEPP1, a rabbit PTP expressed in renal glomerular epithelia, and has the same phosphatase domain as murine PTPϕ expressed in macrophages. RPTP-BK has also significant homology with Drosophila DPTP10D in the phosphatase domain, whose expression is localized exclusively in growth cones of the embryonal brains. The gene for RPTP-BK is well conserved among other species, and the expression in the brain but not in the kidney is developmentally regulated during the neonatal stage. Hybridization in situ showed that RPTP-BK is highly expressed in the postmitotic maturing neurons of the olfactory bulb, developing neocortex, hippocampus and thalamus. Because the expression of RPTP-BK in the developing neocortex is correlated with the stage of axonogenesis in cortical neurons, RPTP-BK might be crucial in neural cell development of the mammalian central nervous system.

scholarly journals Insight into the Role of the STriatal-Enriched Protein Tyrosine Phosphatase (STEP) in A2A Receptor-Mediated Effects in the Central Nervous System

2021 ◽  
Vol 12 ◽  
Author(s):  
Maria Rosaria Domenici ◽  
Cinzia Mallozzi ◽  
Rita Pepponi ◽  
Ida Casella ◽  
Valentina Chiodi ◽  
...  
Keyword(s):  
Central Nervous System ◽  
Nervous System ◽  
Protein Tyrosine Phosphatase ◽  
Motor Behavior ◽  
Tyrosine Phosphatase ◽  
Neuroblastoma Cell ◽  
Rat Striatum ◽  
Protein Tyrosine ◽  
Neuropsychiatric Diseases ◽  
The Central Nervous System

The STriatal-Enriched protein tyrosine phosphatase STEP is a brain-specific tyrosine phosphatase that plays a pivotal role in the mechanisms of learning and memory, and it has been demonstrated to be involved in several neuropsychiatric diseases. Recently, we found a functional interaction between STEP and adenosine A2A receptor (A2AR), a subtype of the adenosine receptor family widely expressed in the central nervous system, where it regulates motor behavior and cognition, and plays a role in cell survival and neurodegeneration. Specifically, we demonstrated the involvement of STEP in A2AR-mediated cocaine effects in the striatum and, more recently, we found that in the rat striatum and hippocampus, as well as in a neuroblastoma cell line, the overexpression of the A2AR, or its stimulation, results in an increase in STEP activity. In the present article we will discuss the functional implication of this interaction, trying to examine the possible mechanisms involved in this relation between STEP and A2ARs.

scholarly journals The protein tyrosine phosphatase RPTPζ/phosphacan is critical for perineuronal net structure

2019 ◽  
Vol 295 (4) ◽  
pp. 955-968 ◽  
Author(s):  
Geoffrey J. Eill ◽  
Ashis Sinha ◽  
Markus Morawski ◽  
Mariano S. Viapiano ◽  
Russell T. Matthews
Keyword(s):  
Central Nervous System ◽  
Nervous System ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Adult Brain ◽  
Neuronal Cultures ◽  
Perineuronal Net ◽  
Detailed Model ◽  
Protein Tyrosine ◽  
The Central Nervous System

Perineuronal nets (PNNs) are conspicuous neuron-specific substructures within the extracellular matrix of the central nervous system that have generated an explosion of interest over the last decade. These reticulated structures appear to surround synapses on the cell bodies of a subset of the neurons in the central nervous system and play key roles in both developmental and adult-brain plasticity. Despite the interest in these structures and compelling demonstrations of their importance in regulating plasticity, their precise functional mechanisms remain elusive. The limited mechanistic understanding of PNNs is primarily because of an incomplete knowledge of their molecular composition and structure and a failure to identify PNN-specific targets. Thus, it has been challenging to precisely manipulate PNNs to rigorously investigate their function. Here, using mouse models and neuronal cultures, we demonstrate a role of receptor protein tyrosine phosphatase zeta (RPTPζ) in PNN structure. We found that in the absence of RPTPζ, the reticular structure of PNNs is lost and phenocopies the PNN structural abnormalities observed in tenascin-R knockout brains. Furthermore, we biochemically analyzed the contribution of RPTPζ to PNN formation and structure, which enabled us to generate a more detailed model for PNNs. We provide evidence for two distinct kinds of interactions of PNN components with the neuronal surface, one dependent on RPTPζ and the other requiring the glycosaminoglycan hyaluronan. We propose that these findings offer important insight into PNN structure and lay important groundwork for future strategies to specifically disrupt PNNs to precisely dissect their function.

Structure, Function and Modulation of Striatal-enriched Protein Tyrosine Phosphatase (STEP)

2021 ◽  
Vol 28 ◽  
Author(s):  
Xiao Liang ◽  
Xuben Hou ◽  
Hao Fang
Keyword(s):  
Central Nervous System ◽  
Nervous System ◽  
Protein Tyrosine Phosphatase ◽  
Neurological Disorders ◽  
Tyrosine Phosphatase ◽  
Nervous System Diseases ◽  
Biological Functions ◽  
Protein Tyrosine ◽  
The Central Nervous System ◽  
Further Development

: Striatal-enriched protein tyrosine phosphatase (STEP) is exclusively expressed in the central nervous system and regulates various neuronal signaling factors through the dephosphorylation of different substrates. Dysregulated expression or uncontrollable enzymatic activity of STEP contributes to neurological disorders such as Alzheimer's disease, which makes it a promising pharmaceutical target. Herein, we reviewed the structure and biological functions of STEP, as well as the recent development of small- molecule STEP modulators. We hope this review will provide a reference for the further development of more potent and selective STEP inhibitors for the treatment of nervous system diseases.

scholarly journals The receptor-type protein tyrosine phosphatase CD45 promotes onset and severity of IL-1β–mediated autoinflammatory osteomyelitis

2021 ◽  
Vol 297 (4) ◽  
pp. 101131
Author(s):  
Jarmila Kralova ◽  
Nataliia Pavliuchenko ◽  
Matej Fabisik ◽  
Kristyna Ilievova ◽  
Frantisek Spoutil ◽  
...  
Keyword(s):  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Receptor Type ◽  
Protein Tyrosine ◽  
Type Protein
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