scholarly journals Protein tyrosine phosphatase ?-deficient mice show aberrant cytoarchitecture and structural abnormalities in the central nervous system

2002 ◽  
Vol 70 (1) ◽  
pp. 24-35 ◽  
Author(s):  
Karen Meathrel ◽  
Tamara Adamek ◽  
Jane Batt ◽  
Daniela Rotin ◽  
Laurie C. Doering
Keyword(s):  
Central Nervous System ◽  
Nervous System ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Protein Tyrosine ◽  
Structural Abnormalities ◽  
The Central Nervous System ◽  
Deficient Mice

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 Critical Role for Protein Tyrosine Phosphatase SHP-1 in Controlling Infection of Central Nervous System Glia and Demyelination by Theiler's Murine Encephalomyelitis Virus

2002 ◽  
Vol 76 (16) ◽  
pp. 8335-8346 ◽  
Author(s):  
Paul T. Massa ◽  
Stacie L. Ropka ◽  
Sucharita Saha ◽  
Karen L. Fecenko ◽  
Kathryn L. Beuler
Keyword(s):  
Central Nervous System ◽  
Nervous System ◽  
Virus Replication ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Protein Tyrosine ◽  
Normal Littermate ◽  
Encephalomyelitis Virus ◽  
Deficient Mice

ABSTRACT We previously characterized the expression and function of the protein tyrosine phosphatase SHP-1 in the glia of the central nervous system (CNS). In the present study, we describe the role of SHP-1 in virus infection of glia and virus-induced demyelination in the CNS. For in vivo studies, SHP-1-deficient mice and their normal littermates received an intracerebral inoculation of an attenuated strain of Theiler's murine encephalomyelitis virus (TMEV). At various times after infection, virus replication, TMEV antigen expression, and demyelination were monitored. It was found that the CNS of SHP-1-deficient mice uniquely displayed demyelination and contained substantially higher levels of virus than did that of normal littermate mice. Many infected astrocytes and oligodendrocytes were detected in both brains and spinal cords of SHP-1-deficient but not normal littermate mice, showing that the virus replicated and spread at a much higher rate in the glia of SHP-1-deficient animals. To ascertain whether the lack of SHP-1 in the glia was primarily responsible for these differences, glial samples from these mice were cultured in vitro and infected with TMEV. As in vivo, infected astrocytes and oligodendrocytes of SHP-1-deficient mice were much more numerous and produced more virus than did those of normal littermate mice. These findings indicate that SHP-1 is a critical factor in controlling virus replication in the CNS glia and virus-induced demyelination.

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.

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