Diphenylether Derivative as Selective Inhibitor of Protein Tyrosine Phosphatase 1B (PTP1B) Over T-cell Protein Tyrosine Phosphatase (TCPTP) Identified through Virtual Screening

2013 ◽  
Vol 13 (11) ◽  
pp. 1602-1606 ◽  
Author(s):  
M. Reddy ◽  
Chakshusmathi Ghadiyaram ◽  
Sunil Panigrahi ◽  
Subramanya Hosahalli ◽  
Lakshmi Mangamoori
Keyword(s):  
T Cell ◽  
Virtual Screening ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Selective Inhibitor ◽  
Cell Protein ◽  
Protein Tyrosine Phosphatase 1B ◽  
Protein Tyrosine

scholarly journals Conformation-assisted Inhibition of Protein-tyrosine Phosphatase-1B Elicits Inhibitor Selectivity over T-cell Protein-tyrosine Phosphatase

2006 ◽  
Vol 281 (12) ◽  
pp. 8010-8015 ◽  
Author(s):  
Ernest Asante-Appiah ◽  
Sangita Patel ◽  
Caroline Desponts ◽  
Jillian M. Taylor ◽  
Cheuk Lau ◽  
...  
Keyword(s):  
T Cell ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Cell Protein ◽  
Protein Tyrosine Phosphatase 1B ◽  
Protein Tyrosine ◽  
Inhibitor Selectivity

scholarly journals Loss of T-Cell Protein Tyrosine Phosphatase Induces Recycling of the Platelet-derived Growth Factor (PDGF) β-Receptor but Not the PDGF α-Receptor

2006 ◽  
Vol 17 (11) ◽  
pp. 4846-4855 ◽  
Author(s):  
Susann Karlsson ◽  
Katarzyna Kowanetz ◽  
Åsa Sandin ◽  
Camilla Persson ◽  
Arne Östman ◽  
...  
Keyword(s):  
T Cell ◽  
Growth Factor ◽  
Cell Surface ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Dominant Negative ◽  
Platelet Derived Growth Factor ◽  
Cell Protein ◽  
Protein Tyrosine ◽  
Β Receptor

We have previously shown that the T-cell protein tyrosine phosphatase (TC-PTP) dephosphorylates the platelet-derived growth factor (PDGF) β-receptor. Here, we show that the increased PDGF β-receptor phosphorylation in TC-PTP knockout (ko) mouse embryonic fibroblasts (MEFs) occurs primarily on the cell surface. The increased phosphorylation is accompanied by a TC-PTP–dependent, monensin-sensitive delay in clearance of cell surface PDGF β-receptors and delayed receptor degradation, suggesting PDGF β-receptor recycling. Recycled receptors could also be directly detected on the cell surface of TC-PTP ko MEFs. The effect of TC-PTP depletion was specific for the PDGF β-receptor, because PDGF α-receptor homodimers were cleared from the cell surface at the same rate in TC-PTP ko MEFs as in wild-type MEFs. Interestingly, PDGF αβ-receptor heterodimers were recycling. Analysis by confocal microscopy revealed that, in TC-PTP ko MEFs, activated PDGF β-receptors colocalized with Rab4a, a marker for rapid recycling. In accordance with this, transient expression of a dominant-negative Rab4a construct increased the rate of clearance of cell surface receptors on TC-PTP ko MEFs. Thus, loss of TC-PTP specifically redirects the PDGF β-receptor toward rapid recycling, which is the first evidence of differential trafficking of PDGF receptor family members.

scholarly journals The YRD Motif Is a Major Determinant of Substrate and Inhibitor Specificity in T-cell Protein-tyrosine Phosphatase

2001 ◽  
Vol 276 (28) ◽  
pp. 26036-26043 ◽  
Author(s):  
Ernest Asante-Appiah ◽  
Kristen Ball ◽  
Kevin Bateman ◽  
Kathryn Skorey ◽  
Rick Friesen ◽  
...  
Keyword(s):  
T Cell ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Major Determinant ◽  
Cell Protein ◽  
Inhibitor Specificity ◽  
Protein Tyrosine ◽  
The Yrd

scholarly journals Six New 3,5-Dimethylcoumarins from Chelonopsis praecox, Chelonopsis odontochila and Chelonopsis pseudobracteata

2021 ◽  
Author(s):  
Chang-An Geng ◽  
Zhen-Tao Deng ◽  
Qian Huang ◽  
Chun-Lei Xiang ◽  
Ji-Jun Chen
Keyword(s):  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
2D Nmr ◽  
Cell Protein ◽  
Protein Tyrosine Phosphatase 1B ◽  
Protein Tyrosine ◽  
Aerial Parts ◽  
Spectroscopic Analyses ◽  
New Compounds

AbstractTen 3,5-dimethylcoumarins (1–6 and 8‒11) involving six new ones (1–6), together with a known 3-methylcoumarin (7), were isolated from the aerial parts of three Chelonopsis plants, C. praecox, C. odontochila, and C. pseudobracteata. The structures of the new compounds were determined by extensive HRESIMS, 1D and 2D NMR spectroscopic analyses. According to the substitution at C-5, these coumarins were classified into 5-methyl, 5-hydroxymethyl, 5-formyl, and 5-nor types. All the isolates were assayed for their inhibition on α-glucosidase, protein tyrosine phosphatase 1B, and T-cell protein tyrosine phosphatase in vitro. Graphic Abstract

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