Oxidative stress and heat shock induce a human gene encoding a protein-tyrosine phosphatase

Nature ◽  
1992 ◽  
Vol 359 (6396) ◽  
pp. 644-647 ◽  
Author(s):  
Stephen M. Keyse ◽  
Elizabeth A. Emslie
Keyword(s):  
Oxidative Stress ◽  
Heat Shock ◽  
Protein Tyrosine Phosphatase ◽  
Human Gene ◽  
Tyrosine Phosphatase ◽  
Gene Encoding ◽  
Protein Tyrosine

scholarly journals Alteration in the Gene Encoding Protein Tyrosine Phosphatase Nonreceptor Type 6 (PTPN6/SHP1) May Contribute to Neutrophilic Dermatoses

2011 ◽  
Vol 178 (4) ◽  
pp. 1434-1441 ◽  
Author(s):  
Andrew B. Nesterovitch ◽  
Zsuzsa Gyorfy ◽  
Mark D. Hoffman ◽  
Ellen C. Moore ◽  
Nada Elbuluk ◽  
...  
Keyword(s):  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Gene Encoding ◽  
Protein Tyrosine ◽  
Neutrophilic Dermatoses ◽  
Encoding Protein

scholarly journals The Gene Encoding Human Nuclear Protein Tyrosine Phosphatase, PRL-1

1998 ◽  
Vol 273 (27) ◽  
pp. 17286-17295 ◽  
Author(s):  
Yong Peng ◽  
Anna Genin ◽  
Nancy B. Spinner ◽  
Robert H. Diamond ◽  
Rebecca Taub
Keyword(s):  
Protein Tyrosine Phosphatase ◽  
Nuclear Protein ◽  
Tyrosine Phosphatase ◽  
Gene Encoding ◽  
Protein Tyrosine

scholarly journals AP-1 elements and TCL1 protein regulate expression of the gene encoding protein tyrosine phosphatase PTPROt in leukemia

Blood ◽  
2011 ◽  
Vol 118 (23) ◽  
pp. 6132-6140 ◽  
Author(s):  
Tasneem Motiwala ◽  
Nicola Zanesi ◽  
Jharna Datta ◽  
Satavisha Roy ◽  
Huban Kutay ◽  
...  
Keyword(s):  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Lymphocytic Leukemia ◽  
Potential Mechanism ◽  
Wild Type ◽  
Truncated Form ◽  
Gene Encoding ◽  
Protein Tyrosine ◽  
Encoding Protein

Abstract We previously demonstrated that the gene encoding PTPROt, the truncated form of protein tyrosine phosphatase receptor type O expressed predominantly in hematopoietic cells, is a candidate tumor suppressor and is down-regulated in chronic lymphocytic leukemia (CLL). Here, we show that PTPROt expression is significantly reduced in CD19+ spleen B cells from Eμ-T cell leukemia 1 (TCL1) transgenic mice relative to the wild-type mice. Strikingly, as much as a 60% decrease in PTPROt expression occurs at 7 weeks independently of promoter methylation. To elucidate the potential mechanism for this early suppression of PTPROt in these mice, we explored the role of activating protein-1 (AP-1) in its expression. We first demonstrate that AP-1 activation by 12-O-tetradecanoylphorbol-13-acetate induces PTPROt expression with concurrent recruitment of c-fos and c-jun to its promoter. The PTPROt promoter is also responsive to over- and underexpression of AP-1, confirming the role of AP-1 in PTPROt expression. Next, we demonstrate that TCL1 can repress the PTPROt promoter by altering c-fos expression and c-jun activation state. Finally, using primary CLL cells we have shown an inverse relationship between TCL1 and PTPROt expression. These findings further substantiate the role of TCL1 in PTPROt suppression and its importance in the pathogenesis of CLL.

scholarly journals Hepatic Oxidative Stress Promotes Insulin-STAT-5 Signaling and Obesity by Inactivating Protein Tyrosine Phosphatase N2

2014 ◽  
Vol 20 (1) ◽  
pp. 85-102 ◽  
Author(s):  
Esteban N. Gurzov ◽  
Melanie Tran ◽  
Manuel A. Fernandez-Rojo ◽  
Troy L. Merry ◽  
Xinmei Zhang ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Protein Tyrosine ◽  
Hepatic Oxidative Stress

scholarly journals Protein tyrosine phosphatase containing SH2 domains: characterization, preferential expression in hematopoietic cells, and localization to human chromosome 12p12-p13.

1992 ◽  
Vol 12 (2) ◽  
pp. 836-846 ◽  
Author(s):  
T L Yi ◽  
J L Cleveland ◽  
J N Ihle
Keyword(s):  
Tyrosine Phosphorylation ◽  
Protein Tyrosine Phosphatase ◽  
Human Gene ◽  
Tyrosine Phosphatase ◽  
Hematopoietic Cells ◽  
Protein Tyrosine Phosphatases ◽  
Hematopoietic Cell ◽  
Protein Tyrosine Phosphorylation ◽  
Tyrosine Phosphatases ◽  
Protein Tyrosine

Protein tyrosine phosphorylation has been implicated in the growth and functional responses of hematopoietic cells. Recently, approaches have been developed to characterize the protein tyrosine phosphatases that may contribute to regulation of protein tyrosine phosphorylation. One novel protein tyrosine phosphatase was expressed predominantly in hematopoietic cells. Hematopoietic cell phosphatase encodes a 68-kDa protein that contains a single phosphatase conserved domain. Unlike other known protein tyrosine phosphatases, hematopoietic cell phosphatase contains two src homology 2 domains. We also cloned the human homolog, which has 95% amino acid sequence identity. Both the murine and human gene products have tyrosine-specific phosphatase activity, and both are expressed predominantly in hematopoietic cells. Importantly, the human gene maps to chromosome 12 region p12-p13. This region is associated with rearrangements in approximately 10% of cases of acute lymphocytic leukemia in children.

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