scholarly journals The Lysyl Oxidase Propeptide Interacts with the Receptor-Type Protein Tyrosine Phosphatase Kappa and Inhibits  -Catenin Transcriptional Activity in Lung Cancer Cells

2011 ◽  
Vol 31 (16) ◽  
pp. 3286-3297 ◽  
Author(s):  
N. Sanchez-Morgan ◽  
K. H. Kirsch ◽  
P. C. Trackman ◽  
G. E. Sonenshein
Oncotarget ◽  
2018 ◽  
Vol 9 (34) ◽  
pp. 23334-23348 ◽  
Author(s):  
Sabrina D’Agostino ◽  
Delia Lanzillotta ◽  
Mariaconcetta Varano ◽  
Cirino Botta ◽  
Antonio Baldrini ◽  
...  

Oncogenesis ◽  
2020 ◽  
Vol 9 (1) ◽  
Author(s):  
Joo-Young Im ◽  
Bo-Kyung Kim ◽  
Kang-Woo Lee ◽  
So-Young Chun ◽  
Mi-Jung Kang ◽  
...  

AbstractDNA damage-induced apoptosis suppressor (DDIAS) regulates cancer cell survival. Here we investigated the involvement of DDIAS in IL-6–mediated signaling to understand the mechanism underlying the role of DDIAS in lung cancer malignancy. We showed that DDIAS promotes tyrosine phosphorylation of signal transducer and activator of transcription 3 (STAT3), which is constitutively activated in malignant cancers. Interestingly, siRNA protein tyrosine phosphatase (PTP) library screening revealed protein tyrosine phosphatase receptor mu (PTPRM) as a novel STAT3 PTP. PTPRM knockdown rescued the DDIAS-knockdown-mediated decrease in STAT3 Y705 phosphorylation in the presence of IL-6. However, PTPRM overexpression decreased STAT3 Y705 phosphorylation. Moreover, endogenous PTPRM interacted with endogenous STAT3 for dephosphorylation at Y705 following IL-6 treatment. As expected, PTPRM bound to wild-type STAT3 but not the STAT3 Y705F mutant. PTPRM dephosphorylated STAT3 in the absence of DDIAS, suggesting that DDIAS hampers PTPRM/STAT3 interaction. In fact, DDIAS bound to the STAT3 transactivation domain (TAD), which competes with PTPRM to recruit STAT3 for dephosphorylation. Thus we show that DDIAS prevents PTPRM/STAT3 binding and blocks STAT3 Y705 dephosphorylation, thereby sustaining STAT3 activation in lung cancer. DDIAS expression strongly correlates with STAT3 phosphorylation in human lung cancer cell lines and tissues. Thus DDIAS may be considered as a potential biomarker and therapeutic target in malignant lung cancer cells with aberrant STAT3 activation.


2021 ◽  
pp. jclinpath-2020-206927
Author(s):  
Maryam Ahmed Al Barashdi ◽  
Ahlam Ali ◽  
Mary Frances McMullin ◽  
Ken Mills

The leucocyte common antigen, protein tyrosine phosphatase receptor type C (PTPRC), also known as CD45, is a transmembrane glycoprotein, expressed on almost all haematopoietic cells except for mature erythrocytes, and is an essential regulator of T and B cell antigen receptor-mediated activation. Disruption of the equilibrium between protein tyrosine kinase and phosphatase activity (from CD45 and others) can result in immunodeficiency, autoimmunity, or malignancy. CD45 is normally present on the cell surface, therefore it works upstream of a large signalling network which differs between cell types, and thus the effects of CD45 on these cells are also different. However, it is becoming clear that CD45 plays an essential role in the innate immune system and this is likely to be a key area for future research. In this review of PTPRC (CD45), its structure and biological activities as well as abnormal expression of CD45 in leukaemia and lymphoma will be discussed.


2021 ◽  
Vol 26 ◽  
pp. 100974
Author(s):  
Shaoting Zhang ◽  
Liangying Zhang ◽  
Zongying Jiang ◽  
Yue Guo ◽  
Hui Zhao ◽  
...  

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