Involvement of ERK and Protein Tyrosine Phosphatase Signaling Pathways in EGCG-Induced Cyclooxygenase-2 Expression in Raw 264.7 Cells

2001 ◽  
Vol 286 (4) ◽  
pp. 721-725 ◽  
Author(s):  
Jong-Wook Park ◽  
Yoon Jung Choi ◽  
Seong-IL Suh ◽  
Taeg Kyu Kwon
Keyword(s):  
Signaling Pathways ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Cyclooxygenase 2 ◽  
Raw 264.7 Cells ◽  
Raw 264.7 ◽  
Protein Tyrosine

The Involvement of the Mammalian Target of Rapamycin, Protein Tyrosine Phosphatase 1b and Dipeptidase 4 Signaling Pathways in Cancer and Diabetes: A Narrative Review

2020 ◽  
Vol 20 ◽  
Author(s):  
Jiajia Zhang ◽  
Ning Wu ◽  
Dayong Shi
Keyword(s):  
Signaling Pathways ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Mammalian Target Of Rapamycin ◽  
Eukaryotic Cell ◽  
Target Of Rapamycin ◽  
Protein Tyrosine Phosphatase 1B ◽  
Protein Tyrosine ◽  
Transduction Mechanisms ◽  
Specific Proteins

Background: The mammalian target of rapamycin (mTOR), protein tyrosine phosphatase 1b (PTP1B) and dipeptidase 4 (DPP4) signaling pathways regulate eukaryotic cell proliferation and metabolism. Previous researches described different transduction mechanisms in the progression of cancer and diabetes. Methodology: We reviewed recent advances in the signal transduction pathways of mTOR, PTP1B and DPP4 regulation and determined the crosstalk and common pathway in diabetes and cancer. Results: We showed that according to numerous past studies, the proteins participate in the signaling networks for both diseases. Conclusion: There are common pathways and specific proteins involved in diabetes and cancer. This article demonstrates and explains the potential mechanisms of association and future prospects for targeting these proteins in pharmacological studies.

scholarly journals Role of Protein Tyrosine Phosphatase Non-Receptor Type 7 in the Regulation of TNF-α Production in RAW 264.7 Macrophages

PLoS ONE ◽  
2013 ◽  
Vol 8 (11) ◽  
pp. e78776 ◽  
Author(s):  
Huiyun Seo ◽  
In-Seon Lee ◽  
Jae Eun Park ◽  
Sung Goo Park ◽  
Do Hee Lee ◽  
...  
Keyword(s):  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Receptor Type ◽  
Raw 264.7 ◽  
Raw 264.7 Macrophages ◽  
Protein Tyrosine ◽  
Tnf Α

scholarly journals Protein tyrosine phosphatase 1B modulates GSK3β/Nrf2 and IGFIR signaling pathways in acetaminophen-induced hepatotoxicity

2013 ◽  
Vol 4 (5) ◽  
pp. e626-e626 ◽  
Author(s):  
M A Mobasher ◽  
Á González-Rodriguez ◽  
B Santamaría ◽  
S Ramos ◽  
M Á Martín ◽  
...  
Keyword(s):  
Signaling Pathways ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Protein Tyrosine Phosphatase 1B ◽  
Protein Tyrosine

scholarly journals The PTPN14 Tumor Suppressor Is a Degradation Target of Human Papillomavirus E7

2017 ◽  
Vol 91 (7) ◽  
Author(s):  
Anita Szalmás ◽  
Vjekoslav Tomaić ◽  
Om Basukala ◽  
Paola Massimi ◽  
Suruchi Mittal ◽  
...  
Keyword(s):  
Human Papillomavirus ◽  
High Risk ◽  
Tumor Suppressor ◽  
Signaling Pathways ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Beta Catenin ◽  
Protein Tyrosine ◽  
Hpv E7 ◽  
Potential Tumor Suppressor

ABSTRACT Activation of signaling pathways ensuring cell growth is essential for the proliferative competence of human papillomavirus (HPV)-infected cells. Tyrosine kinases and phosphatases are key regulators of cellular growth control pathways. A recently identified potential cellular target of HPV E7 is the cytoplasmic protein tyrosine phosphatase PTPN14, which is a potential tumor suppressor and is linked to the control of the Hippo and Wnt/beta-catenin signaling pathways. In this study, we show that the E7 proteins of both high-risk and low-risk mucosal HPV types can interact with PTPN14. This interaction is independent of retinoblastoma protein (pRb) and involves residues in the carboxy-terminal region of E7. We also show that high-risk E7 induces proteasome-mediated degradation of PTPN14 in cells derived from cervical tumors. This degradation appears to be independent of cullin-1 or cullin-2 but most likely involves the UBR4/p600 ubiquitin ligase. The degree to which E7 downregulates PTPN14 would suggest that this interaction is important for the viral life cycle and potentially also for the development of malignancy. In support of this we find that overexpression of PTPN14 decreases the ability of HPV-16 E7 to cooperate with activated EJ-ras in primary cell transformation assays. IMPORTANCE This study links HPV E7 to the deregulation of protein tyrosine phosphatase signaling pathways. PTPN14 is classified as a potential tumor suppressor protein, and here we show that it is very susceptible to HPV E7-induced proteasome-mediated degradation. Intriguingly, this appears to use a mechanism that is different from that employed by E7 to target pRb. Therefore, this study has important implications for our understanding of the molecular basis for E7 function and also sheds important light on the potential role of PTPN14 as a tumor suppressor.

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